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Conserved domains on  [gi|148540050|ref|NP_001005292|]
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(3R)-3-hydroxyacyl-CoA dehydrogenase [Danio rerio]

Protein Classification

beta-ketoacyl-ACP reductase( domain architecture ID 10143190)

3-oxoacyl-[acyl-carrier-protein] reductase catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 10-254 8.83e-127

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


:

Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 359.17  E-value: 8.83e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRrYFQP 89
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEI--KALGGNAAALEADVSDREAVEALVEKVEA-EFGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd05333   78 VDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRR--SGRIINISSVVGLIGNPGQANYAASKAG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEV 249
Cdd:cd05333  156 VIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHV 235


                 ....*
gi 148540050 250 AGGLF 254
Cdd:cd05333  236 NGGMY 240
 
Name Accession Description Interval E-value
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 10-254 8.83e-127

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 359.17  E-value: 8.83e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRrYFQP 89
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEI--KALGGNAAALEADVSDREAVEALVEKVEA-EFGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd05333   78 VDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRR--SGRIINISSVVGLIGNPGQANYAASKAG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEV 249
Cdd:cd05333  156 VIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHV 235


                 ....*
gi 148540050 250 AGGLF 254
Cdd:cd05333  236 NGGMY 240
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
13-254 1.40e-100

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 293.22  E-value: 1.40e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK05653   9 LVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAA--GGEARVLVFDVSDEAAVRALIEAAVEA-FGALDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:PRK05653  86 LVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKAR--YGRIVNISSVSGVTGNPGQTNYSAAKAGVIG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAGG 252
Cdd:PRK05653 164 FTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVNGG 243


                 ..
gi 148540050 253 LF 254
Cdd:PRK05653 244 MY 245
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 5-255 1.11e-96

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 283.22  E-value: 1.11e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   5 TRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA--GGRALAVAADVTDEAAVEALVAAAVA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYA 164
Cdd:COG1028   80 A-FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGG--GRIVNISSIAGLRGSPGQAAYA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:COG1028  157 ASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLgaEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYI 236

                        250
                 ....*....|...
gi 148540050 243 TGVSIEVAGGLFI 255
Cdd:COG1028  237 TGQVLAVDGGLTA 249
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 13-254 3.16e-92

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 271.77  E-value: 3.16e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:TIGR01830   2 LVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKAL-GVKALGVVLDVSDREDVKAVVEEIEEE-LGTIDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAgsAKGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:TIGR01830  80 LVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQ--RSGRIINISSVVGLMGNAGQANYAASKAGVIG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAGG 252
Cdd:TIGR01830 158 FTKSLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDGG 237


                  ..
gi 148540050  253 LF 254
Cdd:TIGR01830 238 MY 239
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 19-253 4.38e-70

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 215.37  E-value: 4.38e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   19 SGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQehmALGVDVSSKDSVEKLVTSIQRRyFQPPSVCVNAAG 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELA-EELGAA---VLPCDVTDEEQVEALVAAAVEK-FGRLDILVNNAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   99 ITQDEF--ILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVsagsAKGSIITVGSIVGKVGNIGQVNYASSKAGVQGLTRT 176
Cdd:pfam13561  81 FAPKLKgpFLDTSREDFDRALDVNLYSLFLLAKAALPLMK----EGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148540050  177 AAKELSKFGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAGGL 253
Cdd:pfam13561 157 LAVELGPRGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 13-164 1.81e-18

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 80.22  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050    13 LVTGGGSGIGRAVCQRFATEGA-SVVVADRNEESANQTLELLPR-EHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPP 90
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAElEAAGARVTVVACDVADRDALAAVLAAIPAV-EGPL 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148540050    91 SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAgsakgsIITVGSIVGKVGNIGQVNYA 164
Cdd:smart00822  83 TGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDF------FVLFSSIAGVLGSPGQANYA 150
 
Name Accession Description Interval E-value
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 10-254 8.83e-127

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 359.17  E-value: 8.83e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRrYFQP 89
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEI--KALGGNAAALEADVSDREAVEALVEKVEA-EFGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd05333   78 VDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRR--SGRIINISSVVGLIGNPGQANYAASKAG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEV 249
Cdd:cd05333  156 VIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHV 235


                 ....*
gi 148540050 250 AGGLF 254
Cdd:cd05333  236 NGGMY 240
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
13-254 1.40e-100

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 293.22  E-value: 1.40e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK05653   9 LVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAA--GGEARVLVFDVSDEAAVRALIEAAVEA-FGALDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:PRK05653  86 LVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKAR--YGRIVNISSVSGVTGNPGQTNYSAAKAGVIG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAGG 252
Cdd:PRK05653 164 FTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVNGG 243


                 ..
gi 148540050 253 LF 254
Cdd:PRK05653 244 MY 245
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 5-255 1.11e-96

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 283.22  E-value: 1.11e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   5 TRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:COG1028    2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA--GGRALAVAADVTDEAAVEALVAAAVA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYA 164
Cdd:COG1028   80 A-FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGG--GRIVNISSIAGLRGSPGQAAYA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:COG1028  157 ASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLgaEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYI 236

                        250
                 ....*....|...
gi 148540050 243 TGVSIEVAGGLFI 255
Cdd:COG1028  237 TGQVLAVDGGLTA 249
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
 13-254 3.16e-92

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 271.77  E-value: 3.16e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:TIGR01830   2 LVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKAL-GVKALGVVLDVSDREDVKAVVEEIEEE-LGTIDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAgsAKGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:TIGR01830  80 LVNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQ--RSGRIINISSVVGLMGNAGQANYAASKAGVIG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAGG 252
Cdd:TIGR01830 158 FTKSLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDGG 237


                  ..
gi 148540050  253 LF 254
Cdd:TIGR01830 238 MY 239
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 5-256 1.30e-91

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 270.53  E-value: 1.30e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   5 TRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHrGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGAL-GGKALAVQGDVSDAESVERAVDEAKA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYA 164
Cdd:PRK05557  80 E-FGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRS--GRIINISSVVGLMGNPGQANYA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK05557 157 ASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITG 236

                        250
                 ....*....|..
gi 148540050 245 VSIEVAGGLFIG 256
Cdd:PRK05557 237 QTLHVNGGMVMG 248
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 13-249 7.02e-79

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 237.57  E-value: 7.02e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELlprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:cd05233    2 LVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAI---EALGGNAVAVQADVSDEEDVEALVEEALEE-FGRLDI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:cd05233   78 LVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGG--GRIVNISSVAGLRPLPGQAAYAASKAALEG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDK-ITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEV 249
Cdd:cd05233  156 LTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKeLAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPV 233
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-253 4.45e-78

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 235.92  E-value: 4.45e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGASVVV-ADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSI 82
Cdd:PRK12825   1 MGSLMGRVALVTGAARGLGRAIALRLARAGADVVVhYRSDEEAAEELVEAV--EALGRRAQAVQADVTDKAALEAAVAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 QRRyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVN 162
Cdd:PRK12825  79 VER-FGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQR--GGRIVNISSVAGLPGWPGRSN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:PRK12825 156 YAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYI 235

                        250
                 ....*....|.
gi 148540050 243 TGVSIEVAGGL 253
Cdd:PRK12825 236 TGQVIEVTGGV 246
PRK12826 PRK12826
SDR family oxidoreductase;
4-252 7.35e-76

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 230.57  E-value: 7.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQ 83
Cdd:PRK12826   1 TRDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELV--EAAGGKARARQVDVRDRAALKAAVAAGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  84 RRyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVG-KVGNIGQVN 162
Cdd:PRK12826  79 ED-FGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGG--GRIVLTSSVAGpRVGYPGLAH 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDK-ITSIIPLGRMGEPAEVADACAFLASDDSRY 241
Cdd:PRK12826 156 YAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEaIAAAIPLGRLGEPEDIAAAVLFLASDEARY 235

                        250
                 ....*....|.
gi 148540050 242 ITGVSIEVAGG 252
Cdd:PRK12826 236 ITGQTLPVDGG 246
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 19-253 4.38e-70

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 215.37  E-value: 4.38e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   19 SGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQehmALGVDVSSKDSVEKLVTSIQRRyFQPPSVCVNAAG 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELA-EELGAA---VLPCDVTDEEQVEALVAAAVEK-FGRLDILVNNAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   99 ITQDEF--ILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVsagsAKGSIITVGSIVGKVGNIGQVNYASSKAGVQGLTRT 176
Cdd:pfam13561  81 FAPKLKgpFLDTSREDFDRALDVNLYSLFLLAKAALPLMK----EGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148540050  177 AAKELSKFGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAGGL 253
Cdd:pfam13561 157 LAVELGPRGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-252 6.04e-69

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 212.78  E-value: 6.04e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVA-DRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:PRK05565   2 KLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLEEI--KEEGGDAIAVKADVSSEEDVENLVEQIVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RYfQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYA 164
Cdd:PRK05565  80 KF-GKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKS--GVIVNISSIWGLIGASCEVLYS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK05565 157 ASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITG 236


                 ....*...
gi 148540050 245 VSIEVAGG 252
Cdd:PRK05565 237 QIITVDGG 244
FabG-like PRK07231
SDR family oxidoreductase;
6-256 1.28e-68

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 212.00  E-value: 1.28e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALGV--DVSSKDSVEKLVTSIQ 83
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEI-----LAGGRAIAVaaDVSDEADVEAAVAAAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  84 RRyFQPPSVCVNAAGITQ-DEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVN 162
Cdd:PRK07231  77 ER-FGSVDILVNNAGTTHrNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEG--GGAIVNVASTAGLRPRPGLGW 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVI----DKITSIIPLGRMGEPAEVADACAFLASDD 238
Cdd:PRK07231 154 YNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTpenrAKFLATIPLGRLGTPEDIANAALFLASDE 233

                        250
                 ....*....|....*...
gi 148540050 239 SRYITGVSIEVAGGLFIG 256
Cdd:PRK07231 234 ASWITGVTLVVDGGRCVG 251
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 13-253 1.82e-64

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 201.82  E-value: 1.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPrehrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK12829  15 LVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLP----GAKVTATVADVADPAQVERVFDTAVER-FGGLDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQ-DEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvSAGSAKGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:PRK12829  90 LVNNAGIAGpTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLL-KASGHGGVIIALSSVAGRLGYPGRTPYAASKWAVV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKIT-----------SIIPLGRMGEPAEVADACAFLASDDSR 240
Cdd:PRK12829 169 GLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLGigldemeqeylEKISLGRMVEPEDIAATALFLASPAAR 248

                        250
                 ....*....|...
gi 148540050 241 YITGVSIEVAGGL 253
Cdd:PRK12829 249 YITGQAISVDGNV 261
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 13-253 2.26e-63

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 198.65  E-value: 2.26e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK08217   9 VITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAEC--GALGTEVRGYAANVTDEEDVEATFAQIAED-FGQLNG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQD---------EFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSaKGSIITVGSIvGKVGNIGQVNY 163
Cdd:PRK08217  86 LINNAGILRDgllvkakdgKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGS-KGVIINISSI-ARAGNMGQTNY 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDsrYIT 243
Cdd:PRK08217 164 SASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEALERLEKMIPVGRLGEPEEIAHTVRFIIEND--YVT 241

                        250
                 ....*....|
gi 148540050 244 GVSIEVAGGL 253
Cdd:PRK08217 242 GRVLEIDGGL 251
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 13-208 7.72e-63

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 195.14  E-value: 7.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRYfQPPSV 92
Cdd:pfam00106   4 LVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL--GGKALFIQGDVTDRAQVKALVEQAVERL-GRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSG--GRIVNISSVAGLVPYPGGSAYSASKAAVIG 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 148540050  173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKV 208
Cdd:pfam00106 159 FTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDE 194
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
9-255 1.38e-62

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 196.53  E-value: 1.38e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHmALGVDVSSKDSVEKLVTSIQRRYfQ 88
Cdd:PRK12824   2 KKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQVR-LKELDVTDTEECAEALAEIEEEE-G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK12824  80 PVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGY--GRIINISSVNGLKGQFGQTNYSAAKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIE 248
Cdd:PRK12824 158 GMIGFTKALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFITGETIS 237


                 ....*..
gi 148540050 249 VAGGLFI 255
Cdd:PRK12824 238 INGGLYM 244
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 9-253 2.42e-60

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 191.05  E-value: 2.42e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHmALGVDVSSKDSVEKLVTSIQRRyFQ 88
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAV-AVGADVTDKDDVEALIDQAVEK-FG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSaKGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:cd05366   80 SFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGH-GGKIINASSIAGVQGFPNLGAYSASKF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVID-----------KITSIIPLGRMGEPAEVADACAFLASD 237
Cdd:cd05366  159 AVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEiagkpegegfaEFSSSIPLGRLSEPEDVAGLVSFLASE 238

                        250
                 ....*....|....*.
gi 148540050 238 DSRYITGVSIEVAGGL 253
Cdd:cd05366  239 DSDYITGQTILVDGGM 254
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 6-252 7.56e-60

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 189.85  E-value: 7.56e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHmALGVDVSSKDSVEKLVTSIQRR 85
Cdd:cd05352    5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTK-AYKCDVSSQESVEKTFKQIQKD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQ--VNY 163
Cdd:cd05352   84 -FGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQG--KGSLIITASMSGTIVNRPQpqAAY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYIT 243
Cdd:cd05352  161 NASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYTT 240


                 ....*....
gi 148540050 244 GVSIEVAGG 252
Cdd:cd05352  241 GSDLIIDGG 249
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 13-241 1.55e-59

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 188.47  E-value: 1.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:COG4221    9 LITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL-----GGRALAVPLDVTDEAAVEAAVAAAVAE-FGRLDV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:COG4221   83 LVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGS--GHIVNISSIAGLRPYPGGAVYAATKAAVRG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRY 241
Cdd:COG4221  161 LSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQPAHV 229
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 12-253 2.17e-59

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 188.36  E-value: 2.17e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  12 TLVTGGGSGIGRAVCQRFATEGASVVVADRNEES-ANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPP 90
Cdd:cd05358    6 ALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDaAEEVVEEI--KAVGGKAIAVQADVSKEEDVVALFQSAIKE-FGTL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAgSAKGSIITVGSIVGKVGNIGQVNYASSKAGV 170
Cdd:cd05358   83 DILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKS-KIKGKIINMSSVHEKIPWPGHVNYAASKGGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 171 QGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV---PEKVIDkITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSI 247
Cdd:cd05358  162 KMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAwddPEQRAD-LLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGTTL 240


                 ....*.
gi 148540050 248 EVAGGL 253
Cdd:cd05358  241 FVDGGM 246
PRK06138 PRK06138
SDR family oxidoreductase;
6-256 1.25e-58

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 186.51  E-value: 1.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMAlgvDVSSKDSVEKLVTSIQRR 85
Cdd:PRK06138   2 RLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGGRAFARQG---DVGSAEAVEALVDFVAAR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK06138  79 -WGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGG--GSIVNTASQLALAGGRGRAAYVA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV------PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDS 239
Cdd:PRK06138 156 SKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIfarhadPEALREALRARHPMNRFGTAEEVAQAALFLASDES 235

                        250
                 ....*....|....*..
gi 148540050 240 RYITGVSIEVAGGLFIG 256
Cdd:PRK06138 236 SFATGTTLVVDGGWLAA 252
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 6-252 9.28e-58

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 184.12  E-value: 9.28e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHmalgvDVSSKDSVEKLVTSIQRR 85
Cdd:cd05341    2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHL-----DVTDEDGWTAVVDTAREA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:cd05341   77 -FGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAG--GGSIINMSSIEGLVGDPALAAYNA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSK--FGIRCNCVLPGFITTPMTDKVPEKVIDK-ITSIIPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:cd05341  154 SKGAVRGLTKSAALECATqgYGIRVNSVHPGYIYTPMTDELLIAQGEMgNYPNTPMGRAGEPDEIAYAVVYLASDESSFV 233

                        250
                 ....*....|
gi 148540050 243 TGVSIEVAGG 252
Cdd:cd05341  234 TGSELVVDGG 243
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 7-252 4.63e-57

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 182.56  E-value: 4.63e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRy 86
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLI--EKEGVEATAFTCDVSDEEAIKAAVEAIEED- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:cd05347   80 FGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGH--GKIINICSLLSELGGPPVPAYAAS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV--PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:cd05347  158 KGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVvaDPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNG 237


                 ....*...
gi 148540050 245 VSIEVAGG 252
Cdd:cd05347  238 QIIFVDGG 245
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 7-253 7.55e-57

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 181.84  E-value: 7.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVAD----RNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSI 82
Cdd:PRK12827   4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIEAA--GGKALGLAFDVRDFAATRAALDAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 QRRyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVN 162
Cdd:PRK12827  82 VEE-FGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRG-GRIVNIASVAGVRGNRGQVN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPekVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:PRK12827 160 YAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAA--PTEHLLNPVPVQRLGEPDEVAALVAFLVSDAASYV 237

                        250
                 ....*....|.
gi 148540050 243 TGVSIEVAGGL 253
Cdd:PRK12827 238 TGQVIPVDGGF 248
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
6-252 4.95e-56

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 180.22  E-value: 4.95e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK07067   3 RLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEI-----GPAAIAVSLDVTRQDSIDRIVAAAVER 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK07067  78 -FGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRG-GKIINMASQAGRRGEALVSHYCA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV-----------PEKVIDKITSIIPLGRMGEPAEVADACAFL 234
Cdd:PRK07067 156 TKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQVdalfaryenrpPGEKKRLVGEAVPLGRMGVPDDLTGMALFL 235

                        250
                 ....*....|....*...
gi 148540050 235 ASDDSRYITGVSIEVAGG 252
Cdd:PRK07067 236 ASADADYIVAQTYNVDGG 253
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
9-253 1.01e-54

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 176.84  E-value: 1.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIqRRYFQ 88
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKL--SKDGGKAIAVKADVSDRDQVFAAVRQV-VDTFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK08643  79 DLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHG-GKIINATSQAGVVGNPELAVYSSTKF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVID-----------KITSIIPLGRMGEPAEVADACAFLASD 237
Cdd:PRK08643 158 AVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVGEnagkpdewgmeQFAKDITLGRLSEPEDVANCVSFLAGP 237

                        250
                 ....*....|....*.
gi 148540050 238 DSRYITGVSIEVAGGL 253
Cdd:PRK08643 238 DSDYITGQTIIVDGGM 253
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
13-244 4.83e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 174.67  E-value: 4.83e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPRehRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:COG0300    9 LITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRA--AGARVEVVALDVTDPDAVAALAEAVLAR-FGPIDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:COG0300   86 LVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGR--GRIVNVSSVAGLRGLPGMAAYAASKAALEG 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSiiplgrmgePAEVADA-CAFLASDDSRYITG 244
Cdd:COG0300  164 FSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLLS---------PEEVARAiLRALERGRAEVYVG 227
PRK06484 PRK06484
short chain dehydrogenase; Validated
 9-252 1.81e-52

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 177.73  E-value: 1.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQ 88
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSL-----GPDHHALAMDVSDEAQIREGFEQLHRE-FG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGIT--QDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKaLVSAGSAKGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK06484  79 RIDVLVNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALR-LMIEQGHGAAIVNVASGAGLVALPKRTAYSAS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMT-DKVPEKVIDK--ITSIIPLGRMGEPAEVADACAFLASDDSRYIT 243
Cdd:PRK06484 158 KAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVaELERAGKLDPsaVRSRIPLGRLGRPEEIAEAVFFLASDQASYIT 237


                 ....*....
gi 148540050 244 GVSIEVAGG 252
Cdd:PRK06484 238 GSTLVVDGG 246
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 13-253 1.23e-51

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 168.62  E-value: 1.23e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQehmalgVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:cd05371    6 VVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGDNCRFVP------VDVTSEKDVKAALALAKAK-FGRLDI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFIL---KMEE---DDFDKVIKVNLKGTFLVTQAVSKALVS----AGSAKGSIITVGSIVGKVGNIGQVN 162
Cdd:cd05371   79 VVNCAGIAVAAKTYnkkGQQPhslELFQRVINVNLIGTFNVIRLAAGAMGKnepdQGGERGVIINTASVAAFEGQIGQAA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIP-LGRMGEPAEVADACAFLAsdDSRY 241
Cdd:cd05371  159 YSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPfPSRLGDPAEYAHLVQHII--ENPY 236

                        250
                 ....*....|..
gi 148540050 242 ITGVSIEVAGGL 253
Cdd:cd05371  237 LNGEVIRLDGAI 248
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 13-252 2.06e-51

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 167.76  E-value: 2.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:cd05369    7 FITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEI-SSATGGRAHPIQCDVRDPEAVEAAVDETLKE-FGKIDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVN-AAGitqdEFILKMEE---DDFDKVIKVNLKGTFLVTQAVSKALVSAGSaKGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:cd05369   85 LINnAAG----NFLAPAESlspNGFKTVIDIDLNGTFNTTKAVGKRLIEAKH-GGSILNISATYAYTGSPFQVHSAAAKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFI--TTPMTDKVPEKVI-DKITSIIPLGRMGEPAEVADACAFLASDDSRYITGV 245
Cdd:cd05369  160 GVDALTRSLAVEWGPYGIRVNAIAPGPIptTEGMERLAPSGKSeKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGT 239


                 ....*..
gi 148540050 246 SIEVAGG 252
Cdd:cd05369  240 TLVVDGG 246
PRK06484 PRK06484
short chain dehydrogenase; Validated
 9-253 4.15e-51

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 174.27  E-value: 4.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALGVDVSSKDSVEKLVTSIQRRYfQ 88
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEAL-----GDEHLSVQADITDEAAVESAFAQIQARW-G 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITqdEFILKMEE---DDFDKVIKVNLKGTFLVTQAVSKALVSAGSakgsIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK06484 343 RLDVLVNNAGIA--EVFKPSLEqsaEDFTRVYDVNLSGAFACARAAARLMSQGGV----IVNLGSIASLLALPPRNAYCA 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDK---VPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:PRK06484 417 SKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLAlkaSGRADFDSIRRRIPLGRLGDPEEVAEAIAFLASPAASYV 496

                        250
                 ....*....|.
gi 148540050 243 TGVSIEVAGGL 253
Cdd:PRK06484 497 NGATLTVDGGW 507
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 10-252 4.69e-51

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 166.68  E-value: 4.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVA-DRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQ 88
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVVVNyASSKAAAEEVVAEI--EAAGGKAIAVQADVSDPSQVARLFDAAEKA-FG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakgsIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:cd05362   81 GVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGGR----IINISSSLTAAYTPNYGAYAGSKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV-PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSI 247
Cdd:cd05362  157 AVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGkTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQVI 236


                 ....*
gi 148540050 248 EVAGG 252
Cdd:cd05362  237 RANGG 241
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 7-252 5.48e-51

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 167.07  E-value: 5.48e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRy 86
Cdd:PRK12939   5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAAL--EAAGGRAHAIAADLADPASVQRFFDAAAAA- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK12939  82 LGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGR--GRIVNLASDTALWGAPKLGAYVAS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP-EKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGV 245
Cdd:PRK12939 160 KGAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPaDERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQ 239


                 ....*..
gi 148540050 246 SIEVAGG 252
Cdd:PRK12939 240 LLPVNGG 246
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 13-255 3.47e-50

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 164.45  E-value: 3.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADR-NEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQPPS 91
Cdd:cd05359    2 LVTGGSRGIGKAIALRLAERGADVVINYRkSKDAAAEVAAEI--EELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAgITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:cd05359   80 LVSNAA-AGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGG--GRIVAISSLGSIRALPNYLAVGTAKAALE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEV 249
Cdd:cd05359  157 ALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPnrEDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVV 236


                 ....*.
gi 148540050 250 AGGLFI 255
Cdd:cd05359  237 DGGLSI 242
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 10-252 4.21e-50

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 164.59  E-value: 4.21e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLEllpreHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQP 89
Cdd:cd08944    4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVA-----QIAGGALALRVDVTDEQQVAALFERAVEEFGGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd08944   79 DLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGG--GSIVNLSSIAGQSGDPGYGAYGASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTD-KVPE-----------KVIDKITsiiplGRMGEPAEVADACAFLASD 237
Cdd:cd08944  157 IRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLaKLAGfegalgpggfhLLIHQLQ-----GRLGRPEDVAAAVVFLLSD 231

                        250
                 ....*....|....*
gi 148540050 238 DSRYITGVSIEVAGG 252
Cdd:cd08944  232 DASFITGQVLCVDGG 246
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 10-253 9.59e-50

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 163.98  E-value: 9.59e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRYFQP 89
Cdd:cd05344    2 KVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAG--GAGVLAVVADLTDPEDIDRLVEKAGDAFGRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 pSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd05344   80 -DILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGW--GRIVNISSLTVKEPEPNLVLSNVARAG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV-----------PEKVIDKITSIIPLGRMGEPAEVADACAFLASDD 238
Cdd:cd05344  157 LIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLlearaekegisVEEAEKEVASQIPLGRVGKPEELAALIAFLASEK 236

                        250
                 ....*....|....*
gi 148540050 239 SRYITGVSIEVAGGL 253
Cdd:cd05344  237 ASYITGQAILVDGGL 251
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 5-255 1.08e-49

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 163.64  E-value: 1.08e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   5 TRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVadrNEESANQTLELLPRE--HRGQEHMALGVDVSSKDSVEKLVTSi 82
Cdd:PRK12935   2 VQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAENLVNElgKEGHDVYAVQADVSKVEDANRLVEE- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 QRRYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGSIVGKVGNIGQVN 162
Cdd:PRK12935  78 AVNHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITE--AEEGRIISISSIIGQAGGFGQTN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSrYI 242
Cdd:PRK12935 156 YSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRDGA-YI 234

                        250
                 ....*....|...
gi 148540050 243 TGVSIEVAGGLFI 255
Cdd:PRK12935 235 TGQQLNINGGLYM 247
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-252 1.78e-49

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 162.96  E-value: 1.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEesanQTLELLPREHRGQehmALGVDVSSKDSVEKLVT 80
Cdd:PRK07060   1 MNMAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNA----AALDRLAGETGCE---PLRLDVGDDAAIRAALA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  81 SIQRRYFqppsvCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQ 160
Cdd:PRK07060  74 AAGAFDG-----LVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRG-GSIVNVSSQAALVGLPDH 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 161 VNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV---PEKViDKITSIIPLGRMGEPAEVADACAFLASD 237
Cdd:PRK07060 148 LAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAwsdPQKS-GPMLAAIPLGRFAEVDDVAAPILFLLSD 226

                        250
                 ....*....|....*
gi 148540050 238 DSRYITGVSIEVAGG 252
Cdd:PRK07060 227 AASMVSGVSLPVDGG 241
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 6-253 3.07e-49

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 162.24  E-value: 3.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESAnqtlELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:cd05326    1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAG----QAVAAELGDPDISFVHCDVTVEADVRAAVDTAVAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGI--TQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNY 163
Cdd:cd05326   77 -FGRLDIMFNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAK--KGSIVSVASVAGVVGGLGPHAY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSII-----PLGRMGEPAEVADACAFLASDD 238
Cdd:cd05326  154 TASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEDEAIEEAVrgaanLKGTALRPEDIAAAVLYLASDD 233

                        250
                 ....*....|....*
gi 148540050 239 SRYITGVSIEVAGGL 253
Cdd:cd05326  234 SRYVSGQNLVVDGGL 248
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 6-254 3.62e-49

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 162.36  E-value: 3.62e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK12429   1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKA--GGKAIGVAMDVTDEEAINAGIDYAVET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK12429  79 -FGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGG--GRIINMASVHGLVGSAGKAAYVS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDK-----------VPEKVIDK-ITSIIPLGRMGEPAEVADACAF 233
Cdd:PRK12429 156 AKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPLVRKqipdlakergiSEEEVLEDvLLPLVPQKRFTTVEEIADYALF 235

                        250       260
                 ....*....|....*....|.
gi 148540050 234 LASDDSRYITGVSIEVAGGLF 254
Cdd:PRK12429 236 LASFAAKGVTGQAWVVDGGWT 256
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 6-255 3.78e-49

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 162.52  E-value: 3.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGqehmaLGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKG-----LVCDVSDSQSVEAAVAAVISA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK06841  87 -FGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGG--GKIVNLASQAGVVALERHVAYCA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE-KVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK06841 164 SKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAgEKGERAKKLIPAGRFAYPEEIAAAALFLASDAAAMITG 243

                        250
                 ....*....|.
gi 148540050 245 VSIEVAGGLFI 255
Cdd:PRK06841 244 ENLVIDGGYTI 254
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 6-252 4.65e-49

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 161.79  E-value: 4.65e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALGVDVSSKDSVEKLV-TSIQR 84
Cdd:cd05345    2 RLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADI-----GEAAIAIQADVTKRADVEAMVeAALSK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 ryFQPPSVCVNAAGIT-QDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNY 163
Cdd:cd05345   77 --FGRLDILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGG--GVIINIASTAGLRPRPGLTWY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELSKFGIRCNCVLP-----GFITTPMTDKVPEKViDKITSIIPLGRMGEPAEVADACAFLASDD 238
Cdd:cd05345  153 NASKGWVVTATKAMAVELAPRNIRVNCLCPvagetPLLSMFMGEDTPENR-AKFRATIPLGRLSTPDDIANAALYLASDE 231

                        250
                 ....*....|....
gi 148540050 239 SRYITGVSIEVAGG 252
Cdd:cd05345  232 ASFITGVALEVDGG 245
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 10-255 5.81e-49

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 161.81  E-value: 5.81e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQT-LELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQ 88
Cdd:cd05364    4 KVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETrQSCLQAGVSEKKILLVVADLTEEEGQDRIISTTLAK-FG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAgsaKGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:cd05364   83 RLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT---KGEIVNVSSVAGGRSFPGVLYYCISKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTP------MTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:cd05364  160 ALDQFTRCTALELAPKGVRVNSVSPGVIVTGfhrrmgMPEEQYIKFLSRAKETHPLGRPGTVDEVAEAIAFLASDASSFI 239

                        250
                 ....*....|...
gi 148540050 243 TGVSIEVAGGLFI 255
Cdd:cd05364  240 TGQLLPVDGGRHL 252
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 4-256 6.23e-49

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 162.08  E-value: 6.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVA--DRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTS 81
Cdd:cd05355   21 SGKLKGKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEE--GRKCLLIPGDLGDESFCRDLVKE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  82 IqRRYFQPPSVCVNAAGITQDEF-ILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSagsaKGSIITVGSIVGKVGNIGQ 160
Cdd:cd05355   99 V-VKEFGKLDILVNNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK----GSSIINTTSVTAYKGSPHL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 161 VNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM-TDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDS 239
Cdd:cd05355  174 LDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLiPSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQDS 253

                        250
                 ....*....|....*..
gi 148540050 240 RYITGVSIEVAGGLFIG 256
Cdd:cd05355  254 SYVTGQVLHVNGGEIIN 270
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
7-256 7.43e-49

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 161.33  E-value: 7.43e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVA-DRNEESANQTLEllprehrgqEHMALGVDV-----------SSKDS 74
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGcGPNSPRRVKWLE---------DQKALGFDFiasegnvgdwdSTKAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  75 VEKLVTSIQRryfqpPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGK 154
Cdd:PRK12938  72 FDKVKAEVGE-----IDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGW--GRIINISSVNGQ 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 155 VGNIGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFL 234
Cdd:PRK12938 145 KGQFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWL 224

                        250       260
                 ....*....|....*....|..
gi 148540050 235 ASDDSRYITGVSIEVAGGLFIG 256
Cdd:PRK12938 225 ASEESGFSTGADFSLNGGLHMG 246
PRK06500 PRK06500
SDR family oxidoreductase;
5-252 8.04e-49

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 161.28  E-value: 8.04e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   5 TRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTlellpREHRGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:PRK06500   2 SRLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAA-----RAELGESALVIRADAGDVAAQKALAQALAE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RYFQPPSVCVNAaGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsagsAKG-SIITVGSIVGKVGNIGQVNY 163
Cdd:PRK06500  77 AFGRLDAVFINA-GVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLL-----ANPaSIVLNGSINAHIGMPNSSVY 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP------EKVIDKITSIIPLGRMGEPAEVADACAFLASD 237
Cdd:PRK06500 151 AASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGlpeatlDAVAAQIQALVPLGRFGTPEEIAKAVLYLASD 230

                        250
                 ....*....|....*
gi 148540050 238 DSRYITGVSIEVAGG 252
Cdd:PRK06500 231 ESAFIVGSEIIVDGG 245
PRK06172 PRK06172
SDR family oxidoreductase;
4-253 1.21e-48

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 161.07  E-value: 1.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQ 83
Cdd:PRK06172   2 SMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALI--REAGGEALFVACDVTRDAEVKALVEQTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  84 RRYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNY 163
Cdd:PRK06172  80 AAYGRLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGG--GAIVNTASVAGLGAAPKMSIY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE---KVIDKITSIIPLGRMGEPAEVADACAFLASDDSR 240
Cdd:PRK06172 158 AASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEadpRKAEFAAAMHPVGRIGKVEEVASAVLYLCSDGAS 237

                        250
                 ....*....|...
gi 148540050 241 YITGVSIEVAGGL 253
Cdd:PRK06172 238 FTTGHALMVDGGA 250
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 13-252 2.18e-48

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 159.94  E-value: 2.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREHRGQehmALGVDVSSKDSVEKLVTSIQRRyfqppSV 92
Cdd:cd05368    6 LITAAAQGIGRAIALAFAREGANVIATDINEEK----LKELERGPGIT---TRVLDVTDKEQVAALAKEEGRI-----DV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKV-GNIGQVNYASSKAGVQ 171
Cdd:cd05368   74 LFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKD--GSIINMSSVASSIkGVPNRFVYSTTKAAVI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV------PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGV 245
Cdd:cd05368  152 GLTKSVAADFAQQGIRCNAICPGTVDTPSLEERiqaqpdPEEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGT 231


                 ....*..
gi 148540050 246 SIEVAGG 252
Cdd:cd05368  232 AVVIDGG 238
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 6-253 2.79e-48

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 160.11  E-value: 2.79e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHL--EALGIDALWIAADVADEADIERLAEETLER 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSaKGSIITVGSIVGKVGN----IGQV 161
Cdd:PRK08213  87 -FGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPRG-YGRIINVASVAGLGGNppevMDTI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 162 NYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRY 241
Cdd:PRK08213 165 AYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERLGEDLLAHTPLGRLGDDEDLKGAALLLASDASKH 244

                        250
                 ....*....|..
gi 148540050 242 ITGVSIEVAGGL 253
Cdd:PRK08213 245 ITGQILAVDGGV 256
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
6-252 4.29e-48

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 159.97  E-value: 4.29e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMAlgvDVSSKDSVEKLVTSIQRR 85
Cdd:PRK08226   3 KLTGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRGHRCTAVVA---DVRDPASVAAAIKRAKEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YfQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGK-VGNIGQVNYA 164
Cdd:PRK08226  80 E-GRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARK--DGRIVMMSSVTGDmVADPGETAYA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV--------PEKVIDKITSIIPLGRMGEPAEVADACAFLAS 236
Cdd:PRK08226 157 LTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIarqsnpedPESVLTEMAKAIPLRRLADPLEVGELAAFLAS 236

                        250
                 ....*....|....*.
gi 148540050 237 DDSRYITGVSIEVAGG 252
Cdd:PRK08226 237 DESSYLTGTQNVIDGG 252
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 13-252 7.49e-48

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 159.41  E-value: 7.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNeesanqtlellPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK06171  13 IVTGGSSGIGLAIVKELLANGANVVNADIH-----------GGDGQHENYQFVPTDVSSAEEVNHTVAEIIEK-FGRIDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFIL---------KMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNY 163
Cdd:PRK06171  81 LVNNAGINIPRLLVdekdpagkyELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHD--GVIVNMSSEAGLEGSEGQSCY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFI-TTPMtdKVPE----------KVIDKI------TSIIPLGRMGEPAE 226
Cdd:PRK06171 159 AATKAALNSFTRSWAKELGKHNIRVVGVAPGILeATGL--RTPEyeealaytrgITVEQLragytkTSTIPLGRSGKLSE 236

                        250       260
                 ....*....|....*....|....*.
gi 148540050 227 VADACAFLASDDSRYITGVSIEVAGG 252
Cdd:PRK06171 237 VADLVCYLLSDRASYITGVTTNIAGG 262
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 7-253 8.19e-48

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 158.54  E-value: 8.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREhRGQEHMALGVDVSSKDSVEKLVTSIQRRy 86
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEK----LEALAAE-LGERVKIFPANLSDRDEVKALGQKAEAD- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK12936  78 LEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMR--RRYGRIINITSVVGVTGNPGQANYCAS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVS 246
Cdd:PRK12936 156 KAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQT 235


                 ....*..
gi 148540050 247 IEVAGGL 253
Cdd:PRK12936 236 IHVNGGM 242
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 6-253 1.09e-47

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 158.38  E-value: 1.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPRehRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:cd05329    3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWRE--KGFKVEGSVCDVSSRSERQELMDTVASH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQaVSKALVSAgSAKGSIITVGSIVG----KVGNIgqv 161
Cdd:cd05329   81 FGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSR-LAHPLLKA-SGNGNIVFISSVAGviavPSGAP--- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 162 nYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV---PEKvIDKITSIIPLGRMGEPAEVADACAFLASDD 238
Cdd:cd05329  156 -YGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPViqqKEN-LDKVIERTPLKRFGEPEEVAALVAFLCMPA 233

                        250
                 ....*....|....*
gi 148540050 239 SRYITGVSIEVAGGL 253
Cdd:cd05329  234 ASYITGQIIAVDGGL 248
PRK06114 PRK06114
SDR family oxidoreductase;
6-252 1.12e-47

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 158.41  E-value: 1.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESA-NQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGlAETAEHIEAA--GRRAIQIAADVTSKADLRAAVARTEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIG--QVN 162
Cdd:PRK06114  83 E-LGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENG--GGSIVNIASMSGIIVNRGllQAH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKvPEKV--IDKITSIIPLGRMGEPAEVADACAFLASDDSR 240
Cdd:PRK06114 160 YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTR-PEMVhqTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAAS 238

                        250
                 ....*....|..
gi 148540050 241 YITGVSIEVAGG 252
Cdd:PRK06114 239 FCTGVDLLVDGG 250
PRK06398 PRK06398
aldose dehydrogenase; Validated
 7-253 3.32e-47

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 157.30  E-value: 3.32e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTlellprehrgqEHmaLGVDVSSKDSVEKLVTSIQRRY 86
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDV-----------DY--FKVDVSNKEQVIKGIDYVISKY 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPpSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK06398  71 GRI-DILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQD--KGVIINIASVQSFAVTRNAAAYVTS 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFgIRCNCVLPGFITTPMTDKV--------PEKVIDKIT---SIIPLGRMGEPAEVADACAFLA 235
Cdd:PRK06398 148 KHAVLGLTRSIAVDYAPT-IRCVAVCPGSIRTPLLEWAaelevgkdPEHVERKIRewgEMHPMKRVGKPEEVAYVVAFLA 226

                        250
                 ....*....|....*...
gi 148540050 236 SDDSRYITGVSIEVAGGL 253
Cdd:PRK06398 227 SDLASFITGECVTVDGGL 244
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 4-256 5.14e-47

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 157.89  E-value: 5.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEES-ANQTLELLPREhrGQEHMALGVDVSS----KDSVEKL 78
Cdd:PRK06701  41 SGKLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANETKQRVEKE--GVKCLLIPGDVSDeafcKDAVEET 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  79 VTSIQRRyfqppSVCVNAAGITQD-EFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSaGSAkgsIITVGSIVGKVGN 157
Cdd:PRK06701 119 VRELGRL-----DILVNNAAFQYPqQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQ-GSA---IINTGSITGYEGN 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 158 IGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM--TDKVPEKViDKITSIIPLGRMGEPAEVADACAFLA 235
Cdd:PRK06701 190 ETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLipSDFDEEKV-SQFGSNTPMQRPGQPEELAPAYVFLA 268

                        250       260
                 ....*....|....*....|.
gi 148540050 236 SDDSRYITGVSIEVAGGLFIG 256
Cdd:PRK06701 269 SPDSSYITGQMLHVNGGVIVN 289
PRK08589 PRK08589
SDR family oxidoreductase;
6-253 7.58e-47

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 156.86  E-value: 7.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEEsANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK08589   3 RLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEA-VSETVDKI--KSNGGKAKAYHVDISDEQQVKDFASEIKEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YfQPPSVCVNAAGItqDEFILKMEE---DDFDKVIKVNLKGTFLVTQAVSKALVSAGsakGSIITVGSIVGKVGNIGQVN 162
Cdd:PRK08589  80 F-GRVDVLFNNAGV--DNAAGRIHEypvDVFDKIMAVDMRGTFLMTKMLLPLMMEQG---GSIINTSSFSGQAADLYRSG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP--------EKVIDKITSIIPLGRMGEPAEVADACAFL 234
Cdd:PRK08589 154 YNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTgtsedeagKTFRENQKWMTPLGRLGKPEEVAKLVVFL 233

                        250
                 ....*....|....*....
gi 148540050 235 ASDDSRYITGVSIEVAGGL 253
Cdd:PRK08589 234 ASDDSSFITGETIRIDGGV 252
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 4-253 2.70e-46

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 154.89  E-value: 2.70e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrgqEHMALGVDVSSKDSVEKLVTSIQ 83
Cdd:PRK06057   2 SQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEV-------GGLFVPTDVTDEDAVNALFDTAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  84 RRYFQPpSVCVNAAGIT--QDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGN-IGQ 160
Cdd:PRK06057  75 ETYGSV-DIAFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQG--KGSIINTASFVAVMGSaTSQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 161 VNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTD----KVPEKVIDKITSIiPLGRMGEPAEVADACAFLAS 236
Cdd:PRK06057 152 ISYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQelfaKDPERAARRLVHV-PMGRFAEPEEIAAAVAFLAS 230

                        250
                 ....*....|....*..
gi 148540050 237 DDSRYITGVSIEVAGGL 253
Cdd:PRK06057 231 DDASFITASTFLVDGGI 247
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 9-252 2.86e-46

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 155.19  E-value: 2.86e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQ 88
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMAYGFGADATSEQSVLALSRGVDEI-FG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsAKGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDG-IQGRIIQINSKSGKVGSKHNSGYSAAKF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPG-FITTPM---------------TDKVPEKVIDKitsiIPLGRMGEPAEVADACA 232
Cdd:PRK12384 160 GGVGLTQSLALDLAEYGITVHSLMLGnLLKSPMfqsllpqyakklgikPDEVEQYYIDK----VPLKRGCDYQDVLNMLL 235

                        250       260
                 ....*....|....*....|
gi 148540050 233 FLASDDSRYITGVSIEVAGG 252
Cdd:PRK12384 236 FYASPKASYCTGQSINVTGG 255
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 9-252 5.73e-46

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 154.03  E-value: 5.73e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQ 88
Cdd:cd08930    2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEEL-TNLYKNRVIALELDITSKESIKELIESYLEKFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVcVNAAGITQDEFILKMEE---DDFDKVIKVNLKGTFLVTQAVSKALvsAGSAKGSIITVGSIVGKVG----NIGQ- 160
Cdd:cd08930   81 IDIL-INNAYPSPKVWGSRFEEfpyEQWNEVLNVNLGGAFLCSQAFIKLF--KKQGKGSIINIASIYGVIApdfrIYENt 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 161 -----VNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGfittPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLA 235
Cdd:cd08930  158 qmyspVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG----GILNNQPSEFLEKYTKKCPLKRMLNPEDLRGAIIFLL 233

                        250
                 ....*....|....*..
gi 148540050 236 SDDSRYITGVSIEVAGG 252
Cdd:cd08930  234 SDASSYVTGQNLVIDGG 250
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 7-253 5.77e-46

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 154.50  E-value: 5.77e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADR-NEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEI--KKAGGEAIAVKGDVTVESDVVNLIQTAVKE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsAKGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK08936  83 -FGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHD-IKGNIINMSSVHEQIPWPLFVHYAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTdkvPEKVIDK-----ITSIIPLGRMGEPAEVADACAFLASDDSR 240
Cdd:PRK08936 161 SKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPIN---AEKFADPkqradVESMIPMGYIGKPEEIAAVAAWLASSEAS 237

                        250
                 ....*....|...
gi 148540050 241 YITGVSIEVAGGL 253
Cdd:PRK08936 238 YVTGITLFADGGM 250
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 13-253 6.17e-45

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 151.07  E-value: 6.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVA-DRNEESANQTLELLprehrGQEHMALGVDVSSKDSVEKLVTSIqRRYFQPPS 91
Cdd:cd05349    4 LVTGASRGLGAAIARSFAREGARVVVNyYRSTESAEAVAAEA-----GERAIAIQADVRDRDQVQAMIEEA-KNHFGPVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGI------TQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:cd05349   78 TIVNNALIdfpfdpDQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGS--GRVINIGTNLFQNPVVPYHDYTT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFI-TTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:cd05349  156 AKAALLGFTRNMAKELGPYGITVNMVSGGLLkVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTG 235


                 ....*....
gi 148540050 245 VSIEVAGGL 253
Cdd:cd05349  236 QNLVVDGGL 244
PRK09242 PRK09242
SDR family oxidoreductase;
6-255 9.48e-45

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 151.05  E-value: 9.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK09242   6 RLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsAGSAKGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK09242  86 -WDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLL--KQHASSAIVNIGSVSGLTHVRSGAPYGM 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV---PEKvIDKITSIIPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:PRK09242 163 TKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPlsdPDY-YEQVIERTPMRRVGEPEEVAAAVAFLCMPAASYI 241

                        250
                 ....*....|...
gi 148540050 243 TGVSIEVAGGLFI 255
Cdd:PRK09242 242 TGQCIAVDGGFLR 254
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 13-252 1.31e-44

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 150.60  E-value: 1.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:PRK07677   5 IITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEI--EQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGitqdEFI---LKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsAKGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:PRK07677  83 INNAAG----NFIcpaEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKG-IKGNIINMVATYAWDAGPGVIHSAAAKAG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKEL-SKFGIRCNCVLPGFIT-TPMTDKV--PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGV 245
Cdd:PRK07677 158 VLAMTRTLAVEWgRKYGIRVNAIAPGPIErTGGADKLweSEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYINGT 237


                 ....*..
gi 148540050 246 SIEVAGG 252
Cdd:PRK07677 238 CITMDGG 244
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-252 3.72e-44

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 149.50  E-value: 3.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANqTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDE-TRRLI--EKEGRKVTFVQVDLTKPESAEKVVKEALEE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YFQPpSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKgsIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK06935  89 FGKI-DILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGK--IINIASMLSFQGGKFVPAYTA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV--PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYIT 243
Cdd:PRK06935 166 SKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIraDKNRNDEILKRIPAGRWGEPDDLMGAAVFLASRASDYVN 245


                 ....*....
gi 148540050 244 GVSIEVAGG 252
Cdd:PRK06935 246 GHILAVDGG 254
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 5-253 4.92e-44

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 148.79  E-value: 4.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   5 TRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLP--REHRGqehmalGVDVSSKDSVEKLVTSI 82
Cdd:PRK12828   3 HSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPadALRIG------GIDLVDPQAARRAVDEV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 QRRyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVN 162
Cdd:PRK12828  77 NRQ-FGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGG--GRIVNIGAGAALKAGPGMGA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMtdkvpekvidkITSIIP---LGRMGEPAEVADACAFLASDDS 239
Cdd:PRK12828 154 YAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPP-----------NRADMPdadFSRWVTPEQIAAVIAFLLSDEA 222

                        250
                 ....*....|....
gi 148540050 240 RYITGVSIEVAGGL 253
Cdd:PRK12828 223 QAITGASIPVDGGV 236
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-256 5.43e-44

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 153.84  E-value: 5.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRneESANQTLELLPREHRGQehmALGVDVSSKDSVEKLVTSIQRRYfQP 89
Cdd:PRK08261 211 KVALVTGAARGIGAAIAEVLARDGAHVVCLDV--PAAGEALAAVANRVGGT---ALALDITAPDAPARIAEHLAERH-GG 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAvskaLVSAGS--AKGSIITVGSIVGKVGNIGQVNYASSK 167
Cdd:PRK08261 285 LDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEA----LLAAGAlgDGGRIVGVSSISGIAGNRGQTNYAASK 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP---EKVIDKITSiipLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK08261 361 AGVIGLVQALAPLLAERGITINAVAPGFIETQMTAAIPfatREAGRRMNS---LQQGGLPVDVAETIAWLASPASGGVTG 437

                        250
                 ....*....|..
gi 148540050 245 VSIEVAGGLFIG 256
Cdd:PRK08261 438 NVVRVCGQSLLG 449
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 13-221 1.32e-43

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 147.77  E-value: 1.32e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQEHmALGVDVSSKDSVEKLVTSIqRRYFQPPSV 92
Cdd:cd05339    3 LITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNV-RKAGGKVH-YYKCDVSKREEVYEAAKKI-KKEVGDVTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:cd05339   80 LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLE--RNHGHIVTIASVAGLISPAGLADYCASKAAAVG 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148540050 173 LTRTAAKEL---SKFGIRCNCVLPGFITTPMTDKV------------PEKVIDKITSIIPLGRM 221
Cdd:cd05339  158 FHESLRLELkayGKPGIKTTLVCPYFINTGMFQGVktprpllapilePEYVAEKIVRAILTNQQ 221
PRK07831 PRK07831
SDR family oxidoreductase;
7-249 2.64e-43

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 147.49  E-value: 2.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGG-GSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK07831  15 LAGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGLGRVEAVVCDVTSEAQVDALIDAAVER 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK07831  95 -LGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHG-GVIVNNASVLGWRAQHGQAHYAA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV-PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK07831 173 AKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKVtSAELLDELAAREAFGRAAEPWEVANVIAFLASDYSSYLTG 252


                 ....*
gi 148540050 245 VSIEV 249
Cdd:PRK07831 253 EVVSV 257
PRK07774 PRK07774
SDR family oxidoreductase;
6-255 4.75e-43

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 146.43  E-value: 4.75e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK07774   3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVAD--GGTAIAVQVDVSDPDSAKAMADATVSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YFQPPSVCVNAA--GITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKV-GNIgqvn 162
Cdd:PRK07774  81 FGGIDYLVNNAAiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGG--GAIVNQSSTAAWLySNF---- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV-PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRY 241
Cdd:PRK07774 155 YGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVtPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASW 234

                        250
                 ....*....|....
gi 148540050 242 ITGVSIEVAGGLFI 255
Cdd:PRK07774 235 ITGQIFNVDGGQII 248
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 9-253 6.80e-43

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 146.53  E-value: 6.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRYfQ 88
Cdd:cd08945    3 SEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREA--GVEADGRTCDVRSVPEIEALVAAAVARY-G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:cd08945   80 PIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAGGMLERGTGRIINIASTGGKQGVVHAAPYSASKH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV-----------PEKVIDKITSIIPLGRMGEPAEVADACAFLASD 237
Cdd:cd08945  160 GVVGFTKALGLELARTGITVNAVCPGFVETPMAASVrehyadiwevsTEEAFDRITARVPLGRYVTPEEVAGMVAYLIGD 239

                        250
                 ....*....|....*.
gi 148540050 238 DSRYITGVSIEVAGGL 253
Cdd:cd08945  240 GAAAVTAQALNVCGGL 255
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-253 9.77e-43

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 145.62  E-value: 9.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLEllprEHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALA----DELGDRAIALQADVTDREQVQAMFATATEH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YFQPPSVCVNAA-------GITQDEFIlKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSivgkvgNI 158
Cdd:PRK08642  78 FGKPITTVVNNAladfsfdGDARKKAD-DITWEDFQQQLEGSVKGALNTIQAALPGMREQGF--GRIINIGT------NL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 159 GQV------NYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFI-TTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADAC 231
Cdd:PRK08642 149 FQNpvvpyhDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLrTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAV 228

                        250       260
                 ....*....|....*....|..
gi 148540050 232 AFLASDDSRYITGVSIEVAGGL 253
Cdd:PRK08642 229 LFFASPWARAVTGQNLVVDGGL 250
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 10-252 1.41e-42

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 145.36  E-value: 1.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQP 89
Cdd:cd05330    4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFGRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVcVNAAGIT-QDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:cd05330   84 DGF-FNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGS--GMIVNTASVGGIRGVGNQSGYAAAKH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV--------PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSR 240
Cdd:cd05330  161 GVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSlkqlgpenPEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDDAG 240

                        250
                 ....*....|..
gi 148540050 241 YITGVSIEVAGG 252
Cdd:cd05330  241 YVNAAVVPIDGG 252
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 6-252 1.54e-42

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 145.16  E-value: 1.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVAD---------RNEESANQTLELLPRehrgqehmALGVDVSSKDSVE 76
Cdd:cd05353    2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDlggdrkgsgKSSSAADKVVDEIKA--------AGGKAVANYDSVE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  77 ---KLV-TSIQRryFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIV 152
Cdd:cd05353   74 dgeKIVkTAIDA--FGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQK--FGRIINTSSAA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 153 GKVGNIGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGfITTPMTDKV-PEKVIDKItsiiplgrmgEPAEVADAC 231
Cdd:cd05353  150 GLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA-AGSRMTETVmPEDLFDAL----------KPEYVAPLV 218

                        250       260
                 ....*....|....*....|.
gi 148540050 232 AFLASDDSRyITGVSIEVAGG 252
Cdd:cd05353  219 LYLCHESCE-VTGGLFEVGAG 238
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 7-256 4.68e-42

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 144.43  E-value: 4.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLEllprEHRGQEHMALGV--DVSSKDSVEKLVTSIQR 84
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLA----AYRELGIEAHGYvcDVTDEDGVQAMVSQIEK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYA 164
Cdd:PRK07097  84 E-VGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKG--HGKIINICSMMSELGRETVSAYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDK--------ITSIIPLGRMGEPAEVADACAFLAS 236
Cdd:PRK07097 161 AAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLRELQADGsrhpfdqfIIAKTPAARWGDPEDLAGPAVFLAS 240

                        250       260
                 ....*....|....*....|..
gi 148540050 237 DDSRYITGVSIEVAGGL--FIG 256
Cdd:PRK07097 241 DASNFVNGHILYVDGGIlaYIG 262
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 10-253 5.41e-42

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 143.76  E-value: 5.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVAD-RNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQ 88
Cdd:cd05337    2 PVAIVTGASRGIGRAIATELAARGFDIAINDlPDDDQATEVVAEVLAA--GRRAIYFQADIGELSDHEALLDQAWED-FG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEF--ILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAK----GSIITVGSIVGKVGNIGQVN 162
Cdd:cd05337   79 RLDCLVNNAGIAVRPRgdLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRFdgphRSIIFVTSINAYLVSPNRGE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITS-IIPLGRMGEPAEVADACAFLASDDSRY 241
Cdd:cd05337  159 YCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAAgLVPIRRWGQPEDIAKAVRTLASGLLPY 238

                        250
                 ....*....|..
gi 148540050 242 ITGVSIEVAGGL 253
Cdd:cd05337  239 STGQPINIDGGL 250
PRK07074 PRK07074
SDR family oxidoreductase;
9-256 7.07e-42

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 143.76  E-value: 7.07e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHrgqeHMALGVDVSSKDSVEKLVTSiQRRYFQ 88
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDAR----FVPVACDLTDAASLAAALAN-AAAERG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGkVGNIGQVNYASSKA 168
Cdd:PRK07074  77 PVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRS--RGAVVNIGSVNG-MAALGHPAYSAAKA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPM----TDKVPEkVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK07074 154 GLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAwearVAANPQ-VFEELKKWYPLQDFATPDDVANAVLFLASPAARAITG 232

                        250
                 ....*....|..
gi 148540050 245 VSIEVAGGLFIG 256
Cdd:PRK07074 233 VCLPVDGGLTAG 244
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 13-252 1.22e-41

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 142.72  E-value: 1.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEesanqtlelLPREHRGQEHMALgvDVSSKDSVEKLVTSIQRRYfQPPSV 92
Cdd:PRK08220  12 WVTGAAQGIGYAVALAFVEAGAKVIGFDQAF---------LTQEDYPFATFVL--DVSDAAAVAQVCQRLLAET-GPLDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:PRK08220  80 LVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRS--GAIVTVGSNAAHVPRIGMAAYGASKAALTS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPM------TDKVPEKVIDKITSI----IPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:PRK08220 158 LAKCVGLELAPYGVRCNVVSPGSTDTDMqrtlwvDEDGEQQVIAGFPEQfklgIPLGKIARPQEIANAVLFLASDLASHI 237

                        250
                 ....*....|
gi 148540050 243 TGVSIEVAGG 252
Cdd:PRK08220 238 TLQDIVVDGG 247
PRK07063 PRK07063
SDR family oxidoreductase;
6-253 1.43e-41

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 142.88  E-value: 1.43e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK07063   4 RLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK07063  84 -FGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGR--GSIVNIASTHAFKIIPGCFPYPV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV------PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDS 239
Cdd:PRK07063 161 AKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWwnaqpdPAAARAETLALQPMKRIGRPEEVAMTAVFLASDEA 240

                        250
                 ....*....|....
gi 148540050 240 RYITGVSIEVAGGL 253
Cdd:PRK07063 241 PFINATCITIDGGR 254
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 4-253 3.27e-41

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 142.07  E-value: 3.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGA-SVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSI 82
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAaGLVICGRNAEKGEAQAAEL--EALGAKAVFVQADLSDVEDCRRVVAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 QRRyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsAKGSIITVGSIVGKVGNIGQVN 162
Cdd:PRK06198  79 DEA-FGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRK-AEGTIVNIGSMSAHGGQPFLAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV-------PEKVIDKITSIIPLGRMGEPAEVADACAFLA 235
Cdd:PRK06198 157 YCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATEGEDRIqrefhgaPDDWLEKAAATQPFGRLLDPDEVARAVAFLL 236

                        250       260
                 ....*....|....*....|..
gi 148540050 236 SDDSRYITGVSIE----VAGGL 253
Cdd:PRK06198 237 SDESGLMTGSVIDfdqsVWGAY 258
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 5-255 4.52e-41

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 141.61  E-value: 4.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   5 TRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:PRK07478   2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAE--GGEAVALAGDVRDEAYAKALVALAVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RyFQPPSVCVNAAGITQDEF-ILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVG-KVGNIGQVN 162
Cdd:PRK07478  80 R-FGGLDIAFNNAGTLGEMGpVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARG--GGSLIFTSTFVGhTAGFPGMAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV---PEkVIDKITSIIPLGRMGEPAEVADACAFLASDDS 239
Cdd:PRK07478 157 YAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMgdtPE-ALAFVAGLHALKRMAQPEEIAQAALFLASDAA 235

                        250
                 ....*....|....*.
gi 148540050 240 RYITGVSIEVAGGLFI 255
Cdd:PRK07478 236 SFVTGTALLVDGGVSI 251
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 10-252 1.12e-40

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 139.72  E-value: 1.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTL--ELlprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRyF 87
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLkdEL---NALRNSAVLVQADLSDFAACADLVAAAFRA-F 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  88 QPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsAGSAKGSIITVGSIVGKVGNIGQVNYASSK 167
Cdd:cd05357   77 GRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRL--AGSRNGSIINIIDAMTDRPLTGYFAYCMSK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 168 AGVQGLTRTAAKELSKFgIRCNCVLPGFITTPMTDkvPEKVIDKITSIIPLGRMGEPAEVADACAFLAsdDSRYITGVSI 247
Cdd:cd05357  155 AALEGLTRSAALELAPN-IRVNGIAPGLILLPEDM--DAEYRENALRKVPLKRRPSAEEIADAVIFLL--DSNYITGQII 229


                 ....*
gi 148540050 248 EVAGG 252
Cdd:cd05357  230 KVDGG 234
PRK09730 PRK09730
SDR family oxidoreductase;
11-252 1.60e-40

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 139.99  E-value: 1.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  11 LTLVTGGGSGIGRAVCQRFATEGASVVVA-DRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQP 89
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVNyQQNLHAAQEVVNLI--TQAGGKAFVLQADISDENQVVAMFTAIDQH-DEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGIT-QDEFILKMEEDDFDKVIKVNLKGTFLVT-QAVSKALVSAGSAKGSIITVGSIVGKVGNIGQ-VNYASS 166
Cdd:PRK09730  80 LAALVNNAGILfTQCTVENLTAERINRVLSTNVTGYFLCCrEAVKRMALKHGGSGGAIVNVSSAASRLGAPGEyVDYAAS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM--TDKVPEKViDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK09730 160 KGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMhaSGGEPGRV-DRVKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTG 238


                 ....*...
gi 148540050 245 VSIEVAGG 252
Cdd:PRK09730 239 SFIDLAGG 246
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 7-252 2.21e-40

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 139.68  E-value: 2.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALGVDVSSKDSVEKLVTSIQRRy 86
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEI-----GPAACAISLDVTDQASIDRCVAALVDR- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:cd05363   75 WGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRG-GKIINMASQAGRRGEALVGVYCAT 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVID-----------KITSIIPLGRMGEPAEVADACAFLA 235
Cdd:cd05363  154 KAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKFARyenrprgekkrLVGEAVPFGRMGRAEDLTGMAIFLA 233

                        250
                 ....*....|....*..
gi 148540050 236 SDDSRYITGVSIEVAGG 252
Cdd:cd05363  234 STDADYIVAQTYNVDGG 250
fabG_rel TIGR01831
3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well ...
 13-253 2.72e-40

3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well conserved family of proteins closely related to the FabG family, TIGR01830, and possibly equal in function. In all completed genomes with a member of this family, a FabG in TIGR01830 is also found. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273825 [Multi-domain]  Cd Length: 239  Bit Score: 138.89  E-value: 2.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   13 LVTGGGSGIGRAVCQRFATEGASVVV-ADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQPPS 91
Cdd:TIGR01831   2 LVTGASRGIGRAIANQLAADGFNIGVhYHSDAAGAQETLNAI--VANGGNGRLLSFDVADRVACREVLEADIAQHGAYYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   92 VCVNAaGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:TIGR01831  80 VVLNA-GIARDAAFPALSEDDWDAVIHTNLDGFYNVIHPCIMPMIGARQG-GRIITLASVSGVMGNRGQVNYSAAKAGLI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  172 GLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPeKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAG 251
Cdd:TIGR01831 158 GATKALAIELAKRKITVNCIAPGLIDTGMIAMEE-SALKEALSMVPMKRMGQPEEVAGLASFLMSDIAGYVTRQVISVNG 236


                  ..
gi 148540050  252 GL 253
Cdd:TIGR01831 237 GM 238
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 13-252 2.75e-40

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 139.14  E-value: 2.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESAnqtlellprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRYfQPPSV 92
Cdd:cd05331    2 IVTGAAQGIGRAVARHLLQAGATVIALDLPFVLL---------LEYGDPLRLTPLDVADAAAVREVCSRLLAEH-GPIDA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:cd05331   72 LVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRT--GAIVTVASNAAHVPRISMAAYGASKAALAS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPM------TDKVPEKVI----DKITSIIPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:cd05331  150 LSKCLGLELAPYGVRCNVVSPGSTDTAMqrtlwhDEDGAAQVIagvpEQFRLGIPLGKIAQPADIANAVLFLASDQAGHI 229

                        250
                 ....*....|
gi 148540050 243 TGVSIEVAGG 252
Cdd:cd05331  230 TMHDLVVDGG 239
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-255 4.14e-40

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 138.94  E-value: 4.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVAD-RNEESANQTLELLPRehRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQ 88
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELRA--LGVEVIFFPADVADLSAHEAMLDAAQAA-WG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEF--ILKMEEDDFDKVIKVNLKGTFLVTQAVSKALV----SAGSAKGSIITVGSIVGKVGNIGQVN 162
Cdd:PRK12745  80 RIDCLVNNAGVGVKVRgdLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLaqpePEELPHRSIVFVSSVNAIMVSPNRGE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITS-IIPLGRMGEPAEVADACAFLASDDSRY 241
Cdd:PRK12745 160 YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAKYDALIAKgLVPMPRWGEPEDVARAVAALASGDLPY 239

                        250
                 ....*....|....
gi 148540050 242 ITGVSIEVAGGLFI 255
Cdd:PRK12745 240 STGQAIHVDGGLSI 253
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 13-252 8.15e-40

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 138.09  E-value: 8.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:cd05365    3 IVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQA--GGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:cd05365   81 VNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGG--GAILNISSMSSENKNVRIAAYGSSKAAVNH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFIttpMTDKVPEKVIDKITSII----PLGRMGEPAEVADACAFLASDDSRYITGVSIE 248
Cdd:cd05365  159 MTRNLAFDLGPKGIRVNAVAPGAV---KTDALASVLTPEIERAMlkhtPLGRLGEPEDIANAALFLCSPASAWVSGQVLT 235


                 ....
gi 148540050 249 VAGG 252
Cdd:cd05365  236 VSGG 239
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 7-253 8.16e-40

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 137.95  E-value: 8.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVV-----ADRNEESANQTlellprEHRGQEHMALGVDVSSKDSVEKLVTS 81
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVnyagsAAAADELVAEI------EAAGGRAIAVQADVADAAAVTRLFDA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  82 IQRRyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsagSAKGSIITVGSIVGKVGNIGQV 161
Cdd:PRK12937  77 AETA-FGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL----GQGGRIINLSTSVIALPLPGYG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 162 NYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM-TDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSR 240
Cdd:PRK12937 152 PYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATELfFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGA 231

                        250
                 ....*....|...
gi 148540050 241 YITGVSIEVAGGL 253
Cdd:PRK12937 232 WVNGQVLRVNGGF 244
PRK07069 PRK07069
short chain dehydrogenase; Validated
 13-253 1.01e-39

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 137.92  E-value: 1.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTL-ELLPREHRGQEHMALGVDVSSKDSVEKLVtSIQRRYFQPPS 91
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFaAEINAAHGEGVAFAAVQDVTDEAQWQALL-AQAADAMGGLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:PRK07069  82 VLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRA--SQPASIVNISSVAAFKAEPDYTAYNASKAAVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 172 GLTRTAAKELSKFG--IRCNCVLPGFITTPMTDKV-----PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK07069 160 SLTKSIALDCARRGldVRCNSIHPTFIRTGIVDPIfqrlgEEEATRKLARGVPLGRLGEPDDVAHAVLYLASDESRFVTG 239


                 ....*....
gi 148540050 245 VSIEVAGGL 253
Cdd:PRK07069 240 AELVIDGGI 248
PRK12743 PRK12743
SDR family oxidoreductase;
10-253 2.13e-39

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 137.09  E-value: 2.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASV-VVADRNEESANQTLELLPREHRGQE--HMALGVDVSSKDSVEKLVTSIQRRy 86
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKETAEEVRSHGVRAEirQLDLSDLPEGAQALDKLIQRLGRI- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 fqppSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK12743  82 ----DVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQG-GRIINITSVHEHTPLPGASAYTAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVS 246
Cdd:PRK12743 157 KHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQS 236


                 ....*..
gi 148540050 247 IEVAGGL 253
Cdd:PRK12743 237 LIVDGGF 243
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 1-256 3.54e-39

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 136.90  E-value: 3.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRnEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVT 80
Cdd:cd08933    1 MASGLRYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCAR-GEAAGQALESELNRAGPGSCKFVPCDVTKEEDIKTLIS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  81 SIQRRYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAvskALVSAGSAKGSIITVGSIVGKVGNIGQ 160
Cdd:cd08933   80 VTVERFGRIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKY---ALPHLRKSQGNIINLSSLVGSIGQKQA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 161 VNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV------PEKVIDKITSIIPLGRMGEPAEVADACAFL 234
Cdd:cd08933  157 APYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELaaqtpdTLATIKEGELAQLLGRMGTEAESGLAALFL 236

                        250       260
                 ....*....|....*....|..
gi 148540050 235 ASdDSRYITGVSIEVAGGLFIG 256
Cdd:cd08933  237 AA-EATFCTGIDLLLSGGAELG 257
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 10-252 5.42e-39

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 136.06  E-value: 5.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHrGQEHMALGVDVSSKDSVEKLVTSIQRRYFQP 89
Cdd:cd05322    3 QVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEY-GEKAYGFGADATNEQSVIALSKGVDEIFKRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 pSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSaKGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd05322   82 -DLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGI-QGRIIQINSKSGKVGSKHNSGYSAAKFG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPG-FITTPMTDK----------VPEKVIDKI-TSIIPLGRMGEPAEVADACAFLASD 237
Cdd:cd05322  160 GVGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQSllpqyakklgIKESEVEQYyIDKVPLKRGCDYQDVLNMLLFYASP 239

                        250
                 ....*....|....*
gi 148540050 238 DSRYITGVSIEVAGG 252
Cdd:cd05322  240 KASYCTGQSINITGG 254
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 14-254 5.56e-39

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 136.24  E-value: 5.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  14 VTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREHRGQEHMALGV--DVSSKDSVEKLVTSIQRRYFQPPS 91
Cdd:PRK07890  10 VSGVGPGLGRTLAVRAARAGADVVLAARTAER----LDEVAAEIDDLGRRALAVptDITDEDQCANLVALALERFGRVDA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsakGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:PRK07890  86 LVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG---GSIVMINSMVLRHSQPKYGAYKMAKGALL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFITTPMTD-----------KVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSR 240
Cdd:PRK07890 163 AASQSLATELGPQGIRVNSVAPGYIWGDPLKgyfrhqagkygVTVEQIYAETAANSDLKRLPTDDEVASAVLFLASDLAR 242

                        250
                 ....*....|....
gi 148540050 241 YITGVSIEVAGGLF 254
Cdd:PRK07890 243 AITGQTLDVNCGEY 256
PRK08628 PRK08628
SDR family oxidoreductase;
13-252 1.65e-38

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 135.09  E-value: 1.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEEsANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:PRK08628  11 IVTGGASGIGAAISLRLAEEGAIPVIFGRSAP-DDEFAEEL--RALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 cVNAAGItQDEFILKMEEDDFDKVIKVNLKGTFLVTQAvskALVSAGSAKGSIITVGSivgKVGNIGQVN---YASSKAG 169
Cdd:PRK08628  88 -VNNAGV-NDGVGLEAGREAFVASLERNLIHYYVMAHY---CLPHLKASRGAIVNISS---KTALTGQGGtsgYAAAKGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV------PEKVIDKITSIIPLG-RMGEPAEVADACAFLASDDSRYI 242
Cdd:PRK08628 160 QLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWiatfddPEAKLAAITAKIPLGhRMTTAEEIADTAVFLLSERSSHT 239

                        250
                 ....*....|
gi 148540050 243 TGVSIEVAGG 252
Cdd:PRK08628 240 TGQWLFVDGG 249
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 5-252 4.13e-38

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 133.98  E-value: 4.13e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   5 TRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:PRK08265   2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASL-----GERARFIATDITDDAAIERAVATVVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RyFQPPSVCVNAAGITQDEFiLKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsakGSIITVGSIVGKVGNIGQVNYA 164
Cdd:PRK08265  77 R-FGRVDILVNLACTYLDDG-LASSRADWLAALDVNLVSAAMLAQAAHPHLARGG---GAIVNFTSISAKFAQTGRWLYP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSII----PLGRMGEPAEVADACAFLASDDSR 240
Cdd:PRK08265 152 ASKAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSGGDRAKADRVAapfhLLGRVGDPEEVAQVVAFLCSDAAS 231

                        250
                 ....*....|..
gi 148540050 241 YITGVSIEVAGG 252
Cdd:PRK08265 232 FVTGADYAVDGG 243
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 10-252 4.72e-38

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 133.36  E-value: 4.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREHRGQEhmALGVDVSSKDSVEKLVTSIqrryfQP 89
Cdd:cd05351    8 KRALVTGAGKGIGRATVKALAKAGARVVAVSRTQAD----LDSLVRECPGIE--PVCVDLSDWDATEEALGSV-----GP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsAKGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd05351   77 VDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARG-VPGSIVNVSSQASQRALTNHTVYCSTKAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV---PEKViDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVS 246
Cdd:cd05351  156 LDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNwsdPEKA-KKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGST 234


                 ....*.
gi 148540050 247 IEVAGG 252
Cdd:cd05351  235 LPVDGG 240
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 6-252 4.81e-38

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 133.82  E-value: 4.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK06113   8 RLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEI--QQLGGQAFACRCDITSEQELSALADFALSK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YFQPPSVCVNAAGITQDEFILKMeeDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK06113  86 LGKVDILVNNAGGGGPKPFDMPM--ADFRRAYELNVFSFFHLSQLVAPEMEKNGG--GVILTITSMAAENKNINMTSYAS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV--PEkVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYIT 243
Cdd:PRK06113 162 SKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVitPE-IEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVS 240


                 ....*....
gi 148540050 244 GVSIEVAGG 252
Cdd:PRK06113 241 GQILTVSGG 249
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 13-252 4.93e-38

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 133.16  E-value: 4.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtlellprEHRGQEHmALGVDVSskDSVEKLVTSIQRryfqpPSV 92
Cdd:PRK06550   9 LITGAASGIGLAQARAFLAQGAQVYGVDKQDKP----------DLSGNFH-FLQLDLS--DDLEPLFDWVPS-----VDI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQD-EFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:PRK06550  71 LCNTAGILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKS--GIIINMCSIASFVAGGGGAAYTASKHALA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFITTPMT--DKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEV 249
Cdd:PRK06550 149 GFTKQLALDYAKDGIQVFGIAPGAVKTPMTaaDFEPGGLADWVARETPIKRWAEPEEVAELTLFLASGKADYMQGTIVPI 228


                 ...
gi 148540050 250 AGG 252
Cdd:PRK06550 229 DGG 231
PRK07856 PRK07856
SDR family oxidoreductase;
10-252 7.63e-38

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 133.14  E-value: 7.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNE-ESANQtlellprehRGQEHMALgvDVSSKDSVEKLVTSIQRRYFQ 88
Cdd:PRK07856   7 RVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRApETVDG---------RPAEFHAA--DVRDPDQVAALVDAIVERHGR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PpSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSkALVSAGSAKGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK07856  76 L-DVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAAN-AVMQQQPGGGSIVNIGSVSGRRPSPGTAAYGAAKA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKfGIRCNCVLPGFITTPMTDKV--PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVS 246
Cdd:PRK07856 154 GLLNLTRSLAVEWAP-KVRVNAVVVGLVRTEQSELHygDAEGIAAVAATVPLGRLATPADIAWACLFLASDLASYVSGAN 232


                 ....*.
gi 148540050 247 IEVAGG 252
Cdd:PRK07856 233 LEVHGG 238
PRK05867 PRK05867
SDR family oxidoreductase;
7-252 9.43e-38

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 132.85  E-value: 9.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRy 86
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTS--GGKVVPVCCDVSQHQQVTSMLDQVTAE- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQV--NYA 164
Cdd:PRK05867  84 LGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQG-GVIINTASMSGHIINVPQQvsHYC 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEkVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK05867 163 ASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTE-YQPLWEPKIPLGRLGRPEELAGLYLYLASEASSYMTG 241


                 ....*...
gi 148540050 245 VSIEVAGG 252
Cdd:PRK05867 242 SDIVIDGG 249
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 10-252 1.46e-37

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 133.26  E-value: 1.46e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVAD---------RNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVT 80
Cdd:PRK07791   7 RVVIVTGAGGGIGRAHALAFAAEGARVVVNDigvgldgsaSGGSAAQAVVDEI--VAAGGEAVANGDDIADWDGAANLVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  81 SiQRRYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQ---AVSKALVSAGSA-KGSIITVGSIVGKVG 156
Cdd:PRK07791  85 A-AVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRhaaAYWRAESKAGRAvDARIINTSSGAGLQG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 157 NIGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFIT--TP-----MTDKVPEKVIDkitsiiplgrMGEPAEVAD 229
Cdd:PRK07791 164 SVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAARTrmTEtvfaeMMAKPEEGEFD----------AMAPENVSP 233

                        250       260
                 ....*....|....*....|...
gi 148540050 230 ACAFLASDDSRYITGVSIEVAGG 252
Cdd:PRK07791 234 LVVWLGSAESRDVTGKVFEVEGG 256
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 10-252 1.86e-37

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 131.83  E-value: 1.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrgQEHMALGVDVSSKDSVEKLVTSIQRRYfQP 89
Cdd:cd08942    7 KIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAY---GECIAIPADLSSEEGIEALVARVAERS-DR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAK--GSIITVGSIVGKVGNIGQV-NYASS 166
Cdd:cd08942   83 LDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATAEnpARVINIGSIAGIVVSGLENySYGAS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE--KVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:cd08942  163 KAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNdpAALEAEEKSIPLGRWGRPEDMAGLAIMLASRAGAYLTG 242


                 ....*...
gi 148540050 245 VSIEVAGG 252
Cdd:cd08942  243 AVIPVDGG 250
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 1-256 2.49e-37

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 132.00  E-value: 2.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVT 80
Cdd:PRK07576   1 MTTMFDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQL--QQAGPEGLGVSADVRDYAAVEAAFA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  81 SIQRRYFQPPSVCVNAAGitqdEF---ILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsakGSIITVGSIVGKVGN 157
Cdd:PRK07576  79 QIADEFGPIDVLVSGAAG----NFpapAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG---ASIIQISAPQAFVPM 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 158 IGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFI--TTPMTDKVP-EKVIDKITSIIPLGRMGEPAEVADACAFL 234
Cdd:PRK07576 152 PMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIagTEGMARLAPsPELQAAVAQSVPLKRNGTKQDIANAALFL 231

                        250       260
                 ....*....|....*....|..
gi 148540050 235 ASDDSRYITGVSIEVAGGLFIG 256
Cdd:PRK07576 232 ASDMASYITGVVLPVDGGWSLG 253
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 7-252 1.52e-36

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 130.27  E-value: 1.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRY 86
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEI--TALGGRAIALAADVLDRASLERAREEIVAQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPpSVCVNAAG------ITQDEF--------ILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIV 152
Cdd:cd08935   81 GTV-DILINGAGgnhpdaTTDPEHyepeteqnFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQK--GGSIINISSMN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 153 GKVGNIGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM-------TDKVPEKVIDKITSIIPLGRMGEPA 225
Cdd:cd08935  158 AFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQnrkllinPDGSYTDRSNKILGRTPMGRFGKPE 237

                        250       260
                 ....*....|....*....|....*...
gi 148540050 226 EVADACAFLASDD-SRYITGVSIEVAGG 252
Cdd:cd08935  238 ELLGALLFLASEKaSSFVTGVVIPVDGG 265
PRK06123 PRK06123
SDR family oxidoreductase;
10-252 1.68e-36

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 129.51  E-value: 1.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVA-DRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQ 88
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLNyLRNRDAAEAVVQAI--RRQGGEALAVAADVADEADVLRLFEAVDRE-LG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFIL-KMEEDDFDKVIKVNLKGTFLVT-QAVSKALVSAGSAKGSIITVGSIVGKVGNIGQ-VNYAS 165
Cdd:PRK06123  80 RLDALVNNAGILEAQMRLeQMDAARLTRIFATNVVGSFLCArEAVKRMSTRHGGRGGAIVNVSSMAARLGSPGEyIDYAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM--TDKVPEKViDKITSIIPLGRMGEPAEVADACAFLASDDSRYIT 243
Cdd:PRK06123 160 SKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIhaSGGEPGRV-DRVKAGIPMGRGGTAEEVARAILWLLSDEASYTT 238


                 ....*....
gi 148540050 244 GVSIEVAGG 252
Cdd:PRK06123 239 GTFIDVSGG 247
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 13-255 3.45e-36

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 128.72  E-value: 3.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK08085  13 LITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQE--GIKAHAAPFNVTHKQEVEAAIEHIEKD-IGPIDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKgsIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:PRK08085  90 LINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGK--IINICSMQSELGRDTITPYAASKGAVKM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE--KVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVA 250
Cdd:PRK08085 168 LTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEdeAFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFVD 247


                 ....*
gi 148540050 251 GGLFI 255
Cdd:PRK08085 248 GGMLV 252
PLN02253 PLN02253
xanthoxin dehydrogenase
 4-252 3.65e-36

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 129.56  E-value: 3.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrgQEHMALGVDVSSKDSVEKLVTSIQ 83
Cdd:PLN02253  13 SQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGE---PNVCFFHCDVTVEDDVSRAVDFTV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  84 RRyFQPPSVCVNAAGITQDEF--ILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGSIVGKVGNIGQV 161
Cdd:PLN02253  90 DK-FGTLDIMVNNAGLTGPPCpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIP--LKKGSIVSLCSVASAIGGLGPH 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 162 NYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMT-DKVP--EKVIDKITSIIPL--------GRMGEPAEVADA 230
Cdd:PLN02253 167 AYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALAlAHLPedERTEDALAGFRAFagknanlkGVELTVDDVANA 246

                        250       260
                 ....*....|....*....|..
gi 148540050 231 CAFLASDDSRYITGVSIEVAGG 252
Cdd:PLN02253 247 VLFLASDEARYISGLNLMIDGG 268
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 13-252 5.00e-36

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 128.86  E-value: 5.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK08277  14 VITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAA--GGEALAVKADVLDKESLEQARQQILED-FGPCDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAG------ITQDEF---------ILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVG---- 153
Cdd:PRK08277  91 LINGAGgnhpkaTTDNEFhelieptktFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRK--GGNIINISSMNAftpl 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 154 -KVgnigqVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM-------TDKVPEKVIDKITSIIPLGRMGEPA 225
Cdd:PRK08277 169 tKV-----PAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQnrallfnEDGSLTERANKILAHTPMGRFGKPE 243

                        250       260
                 ....*....|....*....|....*...
gi 148540050 226 EVADACAFLASDD-SRYITGVSIEVAGG 252
Cdd:PRK08277 244 ELLGTLLWLADEKaSSFVTGVVLPVDGG 271
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 10-231 7.45e-36

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 127.37  E-value: 7.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHR--GQEHMALGVDVSSKDSVEKLVTSIQRRyF 87
Cdd:cd08939    2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANasGQKVSYISADLSDYEEVEQAFAQAVEK-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  88 QPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSK 167
Cdd:cd08939   81 GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQR--PGHIVFVSSQAALVGIYGYSAYCPSK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDkVPEKVIDKITSIIPLG-RMGEPAEVADAC 231
Cdd:cd08939  159 FALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFE-EENKTKPEETKAIEGSsGPITPEEAARII 222
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-252 1.04e-35

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 127.59  E-value: 1.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEEsaNQTLELlprEHRGQEhmALGVDVSSKDSVEKLVTSIQ 83
Cdd:PRK06463   2 SMRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAE--NEAKEL---REKGVF--TIKCDVGNRDQVKKSKEVVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  84 RRyFQPPSVCVNAAGITQ----DEFilkmEEDDFDKVIKVNLKGTFLVTQAVSKALvsAGSAKGSIITVGSIVGkVGN-- 157
Cdd:PRK06463  75 KE-FGRVDVLVNNAGIMYlmpfEEF----DEEKYNKMIKINLNGAIYTTYEFLPLL--KLSKNGAIVNIASNAG-IGTaa 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 158 IGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMT--DKVPE---KVIDKITSIIPLGRMGEPAEVADACA 232
Cdd:PRK06463 147 EGTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTlsGKSQEeaeKLRELFRNKTVLKTTGKPEDIANIVL 226

                        250       260
                 ....*....|....*....|
gi 148540050 233 FLASDDSRYITGVSIEVAGG 252
Cdd:PRK06463 227 FLASDDARYITGQVIVADGG 246
PRK07035 PRK07035
SDR family oxidoreductase;
7-255 1.35e-35

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 127.05  E-value: 1.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRRY 86
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAA--GGKAEALACHIGEMEQIDALFAHIRERH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK07035  84 GRLDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGG--GSIVNVASVNGVSPGDFQGIYSIT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV--PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK07035 162 KAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALfkNDAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTG 241

                        250
                 ....*....|.
gi 148540050 245 VSIEVAGGLFI 255
Cdd:PRK07035 242 ECLNVDGGYLS 252
PRK06128 PRK06128
SDR family oxidoreductase;
6-255 1.55e-35

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 128.44  E-value: 1.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEES--ANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQ 83
Cdd:PRK06128  52 RLQGRKALITGADSGIGRATAIAFAREGADIALNYLPEEEqdAAEVVQLI--QAEGRKAVALPGDLKDEAFCRQLVERAV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  84 RRyFQPPSVCVNAAGI-TQDEFILKMEEDDFDKVIKVNLKGTFLVTQAvSKALVSAGSakgSIITVGSIVGKVGNIGQVN 162
Cdd:PRK06128 130 KE-LGGLDILVNIAGKqTAVKDIADITTEQFDATFKTNVYAMFWLCKA-AIPHLPPGA---SIINTGSIQSYQPSPTLLD 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMT---DKVPEKVIDkITSIIPLGRMGEPAEVADACAFLASDDS 239
Cdd:PRK06128 205 YASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQpsgGQPPEKIPD-FGSETPMKRPGQPVEMAPLYVLLASQES 283

                        250
                 ....*....|....*.
gi 148540050 240 RYITGVSIEVAGGLFI 255
Cdd:PRK06128 284 SYVTGEVFGVTGGLLL 299
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
13-253 3.23e-35

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 132.66  E-value: 3.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRgqeHMALGVDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:PRK08324 426 LVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDR---ALGVACDVTDEAAVQAAFEEAALAFGGVDIV 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 cVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGS---IVGKVGNigqVNYASSKAG 169
Cdd:PRK08324 503 -VSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLG-GSIVFIASknaVNPGPNF---GAYGAAKAA 577

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPgfittpmtDKV-------PEKVIDK--ITSIIP-------------LGRMGEPAEV 227
Cdd:PRK08324 578 ELHLVRQLALELGPDGIRVNGVNP--------DAVvrgsgiwTGEWIEAraAAYGLSeeeleefyrarnlLKREVTPEDV 649

                        250       260
                 ....*....|....*....|....*.
gi 148540050 228 ADACAFLASDDSRYITGVSIEVAGGL 253
Cdd:PRK08324 650 AEAVVFLASGLLSKTTGAIITVDGGN 675
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 13-252 4.39e-35

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 126.02  E-value: 4.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:cd08940    6 LVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQ-FGGVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:cd08940   85 LVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGW--GRIINIASVHGLVASANKSAYVAAKHGVVG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDK------------ITSIIPLGRMGEPAEVADACAFLASDDSR 240
Cdd:cd08940  163 LTKVVALETAGTGVTCNAICPGWVLTPLVEKQISALAQKngvpqeqaarelLLEKQPSKQFVTPEQLGDTAVFLASDAAS 242

                        250
                 ....*....|..
gi 148540050 241 YITGVSIEVAGG 252
Cdd:cd08940  243 QITGTAVSVDGG 254
PRK07985 PRK07985
SDR family oxidoreductase;
4-256 4.78e-35

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 127.03  E-value: 4.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVA--DRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTS 81
Cdd:PRK07985  44 SGRLKDRKALVTGGDSGIGRAAAIAYAREGADVAISylPVEEEDAQDVKKII--EECGRKAVLLPGDLSDEKFARSLVHE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  82 IQRRYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAvSKALVSAGSakgSIITVGSIVGKVGNIGQV 161
Cdd:PRK07985 122 AHKALGGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQE-AIPLLPKGA---SIITTSSIQAYQPSPHLL 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 162 NYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM--TDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDS 239
Cdd:PRK07985 198 DYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALqiSGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQES 277

                        250
                 ....*....|....*..
gi 148540050 240 RYITGVSIEVAGGLFIG 256
Cdd:PRK07985 278 SYVTAEVHGVCGGEHLG 294
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-255 3.88e-34

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 124.89  E-value: 3.88e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVAD-RNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLV 79
Cdd:PRK07792   4 TTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDvASALDASDVLDEI--RAAGAKAVAVAGDISQRATADELV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  80 TSIQRryFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAV-----SKALVSAGSAKGSIITVGSIVGK 154
Cdd:PRK07792  82 ATAVG--LGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAaaywrAKAKAAGGPVYGRIVNTSSEAGL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 155 VGNIGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGfITTPMTDKV----PEKVIDKITsiiPLGrmgePAEVADA 230
Cdd:PRK07792 160 VGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICPR-ARTAMTADVfgdaPDVEAGGID---PLS----PEHVVPL 231

                        250       260
                 ....*....|....*....|....*
gi 148540050 231 CAFLASDdsryitgVSIEVAGGLFI 255
Cdd:PRK07792 232 VQFLASP-------AAAEVNGQVFI 249
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-252 7.46e-34

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 122.88  E-value: 7.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGG--GSGIGRAVCQRFATEGASVVV-------ADRNEESANQTLELLPREHRGQ----EHMalGVDVSSKDSVE 76
Cdd:PRK12748   6 KIALVTGAsrLNGIGAAVCRRLAAKGIDIFFtywspydKTMPWGMHDKEPVLLKEEIESYgvrcEHM--EIDLSQPYAPN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  77 KLVTSIQRRYFQPPSVCVNAAGITQDEFI-LKMEEddFDKVIKVNLKGTFLVTQAVSKALvsAGSAKGSII--TVGSIVG 153
Cdd:PRK12748  84 RVFYAVSERLGDPSILINNAAYSTHTRLEeLTAEQ--LDKHYAVNVRATMLLSSAFAKQY--DGKAGGRIInlTSGQSLG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 154 KVgnIGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFI-TTPMTDKVPEKVIDKItsiiPLGRMGEPAEVADACA 232
Cdd:PRK12748 160 PM--PDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTdTGWITEELKHHLVPKF----PQGRVGEPVDAARLIA 233

                        250       260
                 ....*....|....*....|
gi 148540050 233 FLASDDSRYITGVSIEVAGG 252
Cdd:PRK12748 234 FLVSEEAKWITGQVIHSEGG 253
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 1-252 9.58e-34

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 122.65  E-value: 9.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVT 80
Cdd:cd08936    2 VTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGE--GLSVTGTVCHVGKAEDRERLVA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  81 SIQRRYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQ 160
Cdd:cd08936   80 TAVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGG--GSVVIVSSVAAFHPFPGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 161 VNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMT-----DKVPEKVIDKITSIiplGRMGEPAEVADACAFLA 235
Cdd:cd08936  158 GPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSsalwmDKAVEESMKETLRI---RRLGQPEDCAGIVSFLC 234

                        250
                 ....*....|....*..
gi 148540050 236 SDDSRYITGVSIEVAGG 252
Cdd:cd08936  235 SEDASYITGETVVVGGG 251
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 5-254 2.24e-33

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 121.93  E-value: 2.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   5 TRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:PRK13394   3 SNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEI--NKAGGKAIGVAMDVTNEDAVNAGIDKVAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYA 164
Cdd:PRK13394  81 R-FGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRG-GVVIYMGSVHSHEASPLKSAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDK-VPEKVIDKITSI-----------IPLGRMGEPAEVADACA 232
Cdd:PRK13394 159 TAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKqIPEQAKELGISEeevvkkvmlgkTVDGVFTTVEDVAQTVL 238

                        250       260
                 ....*....|....*....|..
gi 148540050 233 FLASDDSRYITGVSIEVAGGLF 254
Cdd:PRK13394 239 FLSSFPSAALTGQSFVVSHGWF 260
PRK06124 PRK06124
SDR family oxidoreductase;
7-253 3.72e-33

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 120.97  E-value: 3.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPRehRGQEHMALGVDVSSKDSVEKLVTSIQRRY 86
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRA--AGGAAEALAFDIADEEAVAAAFARIDAEH 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPpSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK06124  87 GRL-DILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGY--GRIIAITSIAGQVARAGDAVYPAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPG-FITTPMTDKVP-EKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK06124 164 KQGLTGLMRALAAEFGPHGITSNAIAPGyFATETNAAMAAdPAVGPWLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNG 243


                 ....*....
gi 148540050 245 VSIEVAGGL 253
Cdd:PRK06124 244 HVLAVDGGY 252
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-252 5.73e-33

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 120.36  E-value: 5.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   4 STRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESanQTLELLprEHRGQEHMALGVDVSSKDS----VEKLV 79
Cdd:PRK08993   5 AFSLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPT--ETIEQV--TALGRRFLSLTADLRKIDGipalLERAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  80 TSiqrryFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIG 159
Cdd:PRK08993  81 AE-----FGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNG-GKIINIASMLSFQGGIR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 160 QVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTD--KVPEKVIDKITSIIPLGRMGEPAEVADACAFLASD 237
Cdd:PRK08993 155 VPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQqlRADEQRSAEILDRIPAGRWGLPSDLMGPVVFLASS 234

                        250
                 ....*....|....*
gi 148540050 238 DSRYITGVSIEVAGG 252
Cdd:PRK08993 235 ASDYINGYTIAVDGG 249
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 12-252 6.59e-33

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 120.10  E-value: 6.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  12 TLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTleLLPREHRGQEHMALGVDVSSKDSVEKLVTSIqRRYFQPPS 91
Cdd:cd05323    3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAA--ELQAINPKVKATFVQCDVTSWEQLAAAFKKA-IEKFGRVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGIT--QDEFILKMEEDDFDKVIKVNLKG----TFLVTQAVSKalvSAGSAKGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:cd05323   80 ILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGvintTYLALHYMDK---NKGGKGGVIVNIGSVAGLYPAPQFPVYSA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKEL-SKFGIRCNCVLPGFITTPM----TDKVPEKVIDKITSiiplgrmgEPAEVADACAFLASDDSR 240
Cdd:cd05323  157 SKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLlpdlVAKEAEMLPSAPTQ--------SPEVVAKAIVYLIEDDEK 228

                        250
                 ....*....|..
gi 148540050 241 yiTGVSIEVAGG 252
Cdd:cd05323  229 --NGAIWIVDGG 238
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 7-253 8.71e-33

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 119.87  E-value: 8.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEhmALGVDVSSKDSVEKLVTSIQRRy 86
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAH--ALAFDVTDHDAVRAAIDAFEAE- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK07523  85 IGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARG--AGKIINIASVQSALARPGIAPYTAT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMT-----DKVPEKVIDKITsiiPLGRMGEPAEVADACAFLASDDSRY 241
Cdd:PRK07523 163 KGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNaalvaDPEFSAWLEKRT---PAGRWGKVEELVGACVFLASDASSF 239

                        250
                 ....*....|..
gi 148540050 242 ITGVSIEVAGGL 253
Cdd:PRK07523 240 VNGHVLYVDGGI 251
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 13-256 8.75e-33

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 120.06  E-value: 8.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESAnQTLellpREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK06200  10 LITGGGSGIGRALVERFLAEGARVAVLERSAEKL-ASL----RQRFGDHVLVVEGDVTSYADNQRAVDQTVDA-FGKLDC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITqdEFILKMEEDD-------FDKVIKVNLKGTFLVTQAVSKALVSAGsakGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:PRK06200  84 FVGNAGIW--DYNTSLVDIPaetldtaFDEIFNVNVKGYLLGAKAALPALKASG---GSMIFTLSNSSFYPGGGGPLYTA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKfGIRCNCVLPGFITTPM------------TDKVPEkVIDKITSIIPLGRMGEPAEVADACAF 233
Cdd:PRK06200 159 SKHAVVGLVRQLAYELAP-KIRVNGVAPGGTVTDLrgpaslgqgetsISDSPG-LADMIAAITPLQFAPQPEDHTGPYVL 236

                        250       260
                 ....*....|....*....|....
gi 148540050 234 LASD-DSRYITGVSIEVAGGLFIG 256
Cdd:PRK06200 237 LASRrNSRALTGVVINADGGLGIR 260
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-252 1.42e-32

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 119.24  E-value: 1.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVAdrNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRY 86
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGV--GVAEAPETQAQV--EALGRKFHFITADLIQQKDIDSIVSQAVEVM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPpSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK12481  82 GHI-DILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNG-GKIINIASMLSFQGGIRVPSYTAS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTD--KVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK12481 160 KSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAalRADTARNEAILERIPASRWGTPDDLAGPAIFLSSSASDYVTG 239


                 ....*...
gi 148540050 245 VSIEVAGG 252
Cdd:PRK12481 240 YTLAVDGG 247
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 7-252 1.01e-31

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 117.10  E-value: 1.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVV--ADRNEESANQTLELlprEHRGQEHMALGVDVSSKDSVEKLVTSI-- 82
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIhyGNRKEEAEETVYEI---QSNGGSAFSIGANLESLHGVEALYSSLdn 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 --QRRYFQPP-SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsagSAKGSIITVGSIVGKVGNIG 159
Cdd:PRK12747  79 elQNRTGSTKfDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL----RDNSRIINISSAATRISLPD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 160 QVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDK--ITSIIPLGRMGEPAEVADACAFLASD 237
Cdd:PRK12747 155 FIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKqyATTISAFNRLGEVEDIADTAAFLASP 234

                        250
                 ....*....|....*
gi 148540050 238 DSRYITGVSIEVAGG 252
Cdd:PRK12747 235 DSRWVTGQLIDVSGG 249
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 13-244 1.24e-31

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 116.56  E-value: 1.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREHRGQ-EHMALgvDVSSKDSVEKLVTSIQRRyFQPPS 91
Cdd:cd05374    4 LITGCSSGIGLALALALAAQGYRVIATARNPDK----LESLGELLNDNlEVLEL--DVTDEESIKAAVKEVIER-FGRID 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:cd05374   77 VLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGS--GRIVNVSSVAGLVPTPFLGPYCASKAALE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP----------------EKVIDKITSIIPLGrmGEPAEVADA---CA 232
Cdd:cd05374  155 ALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAgsaledpeispyaperKEIKENAAGVGSNP--GDPEKVADVivkAL 232

                        250
                 ....*....|..
gi 148540050 233 FLASDDSRYITG 244
Cdd:cd05374  233 TSESPPLRYFLG 244
PRK06947 PRK06947
SDR family oxidoreductase;
9-252 1.32e-31

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 116.83  E-value: 1.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVA-DRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRYF 87
Cdd:PRK06947   2 RKVVLITGASRGIGRATAVLAAARGWSVGINyARDAAAAEETADAV--RAAGGRACVVAGDVANEADVIAMFDAVQSAFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  88 QPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSA-GSAKGSIITVGSIVGKVGNIGQ-VNYAS 165
Cdd:PRK06947  80 RLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrGGRGGAIVNVSSIASRLGSPNEyVDYAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM--TDKVPEKViDKITSIIPLGRMGEPAEVADACAFLASDDSRYIT 243
Cdd:PRK06947 160 SKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIhaSGGQPGRA-ARLGAQTPLGRAGEADEVAETIVWLLSDAASYVT 238


                 ....*....
gi 148540050 244 GVSIEVAGG 252
Cdd:PRK06947 239 GALLDVGGG 247
PRK12746 PRK12746
SDR family oxidoreductase;
7-253 1.44e-31

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 116.67  E-value: 1.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVA-DRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQ-- 83
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREI--ESNGGKAFLIEADLNSIDGVKKLVEQLKne 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  84 ---RRYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsagSAKGSIITVGSIVGKVGNIGQ 160
Cdd:PRK12746  82 lqiRVGTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL----RAEGRVINISSAEVRLGFTGS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 161 VNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV---PEkVIDKITSIIPLGRMGEPAEVADACAFLASD 237
Cdd:PRK12746 158 IAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLlddPE-IRNFATNSSVFGRIGQVEDIADAVAFLASS 236

                        250
                 ....*....|....*.
gi 148540050 238 DSRYITGVSIEVAGGL 253
Cdd:PRK12746 237 DSRWVTGQIIDVSGGF 252
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 6-252 3.60e-31

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 115.70  E-value: 3.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEesanQTLELL-PREHRGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:cd08937    1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSE----LVHEVLaEILAAGDAAHVHTADLETYAGAQGVVRAAVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVgkVGNIGQVNYA 164
Cdd:cd08937   77 RFGRVDVLINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQ--GVIVNVSSIA--TRGIYRIPYS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTP----------MTDKVPE---KVIDKITSIIPLGRMGEPAEVADAC 231
Cdd:cd08937  153 AAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPprkiprnaapMSEQEKVwyqRIVDQTLDSSLMGRYGTIDEQVRAI 232

                        250       260
                 ....*....|....*....|.
gi 148540050 232 AFLASDDSRYITGVSIEVAGG 252
Cdd:cd08937  233 LFLASDEASYITGTVLPVGGG 253
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 13-256 7.43e-31

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 115.14  E-value: 7.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREHrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:cd05348    8 LITGGGSGLGRALVERFVAEGAKVAVLDRSAEK----VAELRADF-GDAVVGVEGDVRSLADNERAVARCVER-FGKLDC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGI---------TQDEFIlkmeEDDFDKVIKVNLKGTFLVTQAVSKALVsagSAKGSIITVGSIVGKVGNIGQVNY 163
Cdd:cd05348   82 FIGNAGIwdystslvdIPEEKL----DEAFDELFHINVKGYILGAKAALPALY---ATEGSVIFTVSNAGFYPGGGGPLY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELSKFgIRCNCVLPGFITT----PMTDKVPEKVI------DKITSIIPLGRMGEPAEVADACAF 233
Cdd:cd05348  155 TASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTdlrgPASLGQGETSIstppldDMLKSILPLGFAPEPEDYTGAYVF 233

                        250       260
                 ....*....|....*....|....
gi 148540050 234 LAS-DDSRYITGVSIEVAGGLFIG 256
Cdd:cd05348  234 LASrGDNRPATGTVINYDGGMGVR 257
PRK09186 PRK09186
flagellin modification protein A; Provisional
 13-252 1.25e-30

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 114.32  E-value: 1.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:PRK09186   8 LITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLVELDITDQESLEEFLSKSAEKYGKIDGA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 cVNAAGITQDEFILKMEE---DDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGkVGN-----------I 158
Cdd:PRK09186  88 -VNCAYPRNKDYGKKFFDvslDDFNENLSLHLGSSFLFSQQFAKYFKKQG--GGNLVNISSIYG-VVApkfeiyegtsmT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 159 GQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFIttpmTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDD 238
Cdd:PRK09186 164 SPVEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGI----LDNQPEAFLNAYKKCCNGKGMLDPDDICGTLVFLLSDQ 239

                        250
                 ....*....|....
gi 148540050 239 SRYITGVSIEVAGG 252
Cdd:PRK09186 240 SKYITGQNIIVDDG 253
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 3-252 1.59e-30

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 114.27  E-value: 1.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   3 ASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPRehrGQEHMALGVDVSSKDSVEKLVTSI 82
Cdd:PRK12823   2 MNQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEVAAELRAA---GGEALALTADLETYAGAQAAMAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 QRRyFQPPSVCVNAAGIT-----QDEFilkmEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVgkVGN 157
Cdd:PRK12823  79 VEA-FGRIDVLINNVGGTiwakpFEEY----EEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGG--GAIVNVSSIA--TRG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 158 IGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPmTDKVP---------EK-----VIDKITSIIPLGRMGE 223
Cdd:PRK12823 150 INRVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAP-PRRVPrnaapqseqEKawyqqIVDQTLDSSLMKRYGT 228

                        250       260
                 ....*....|....*....|....*....
gi 148540050 224 PAEVADACAFLASDDSRYITGVSIEVAGG 252
Cdd:PRK12823 229 IDEQVAAILFLASDEASYITGTVLPVGGG 257
PRK05855 PRK05855
SDR family oxidoreductase;
10-202 2.36e-30

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 118.54  E-value: 2.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQEHmALGVDVSSKDSVEKLVTSIQRRYfQP 89
Cdd:PRK05855 316 KLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELI-RAAGAVAH-AYRVDVSDADAMEAFAEWVRAEH-GV 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:PRK05855 393 PDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTG-GHIVNVASAAAYAPSRSLPAYATSKAA 471

                        170       180       190
                 ....*....|....*....|....*....|...
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTD 202
Cdd:PRK05855 472 VLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
PRK07814 PRK07814
SDR family oxidoreductase;
6-253 2.66e-30

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 113.72  E-value: 2.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLV-TSIQR 84
Cdd:PRK07814   7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQI--RAAGRRAHVVAADLAHPEATAGLAgQAVEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 ryFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVsAGSAKGSIITVGSIVGKVGNIGQVNYA 164
Cdd:PRK07814  85 --FGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLML-EHSGGGSVINISSTMGRLAGRGFAAYG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 165 SSKAGVQGLTRTAAKELSKfGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYI 242
Cdd:PRK07814 162 TAKAALAHYTRLAALDLCP-RIRVNAIAPGSILTSALEVVAanDELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYL 240

                        250
                 ....*....|.
gi 148540050 243 TGVSIEVAGGL 253
Cdd:PRK07814 241 TGKTLEVDGGL 251
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 14-230 3.58e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 113.50  E-value: 3.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  14 VTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHrgqehmALGVDVSSKDSVEKLVTSIQRRyFQPPSVC 93
Cdd:PRK07825  10 ITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVV------GGPLDVTDPASFAAFLDAVEAD-LGPIDVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  94 VNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQGL 173
Cdd:PRK07825  83 VNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGR--GHVVNVASLAGKIPVPGMATYCASKHAVVGF 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148540050 174 TRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEkvidkitsiIPLGRMGEPAEVADA 230
Cdd:PRK07825 161 TDAARLELRGTGVHVSVVLPSFVNTELIAGTGG---------AKGFKNVEPEDVAAA 208
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 10-234 4.39e-30

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 112.07  E-value: 4.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLEllprehRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQP 89
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSA------SGGDVEAVPYDARDPEDARALVDALRDR-FGR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd08932   74 IDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGS--GRVVFLNSLSGKRVLAGNAGYSASKFA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKvidkitSIIPLGRMGEPAEVADACAFL 234
Cdd:cd08932  152 LRALAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLV------GAFPPEEMIQPKDIANLVRMV 210
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 10-253 5.39e-30

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 112.29  E-value: 5.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyfqp 89
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAE-GPNLFFVHGDVADETLVKFVVYAMLEKLGRI---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 pSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsakGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd09761   77 -DVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK---GRIINIASTRAFQSEPDSEAYAASKGG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFgIRCNCVLPGFI-TTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIE 248
Cdd:cd09761  153 LVALTHALAMSLGPD-IRVNCISPGWInTTEQQEFTAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFI 231


                 ....*
gi 148540050 249 VAGGL 253
Cdd:cd09761  232 VDGGM 236
PRK07062 PRK07062
SDR family oxidoreductase;
10-253 6.80e-30

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 112.44  E-value: 6.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQP 89
Cdd:PRK07062   9 RVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEAR-FGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGI--------TQDEFILKMEEDDFDKVIKvnlkgtflVTQAVSKALvsAGSAKGSIITVGSIVGKVGNIGQV 161
Cdd:PRK07062  88 VDMLVNNAGQgrvstfadTTDDAWRDELELKYFSVIN--------PTRAFLPLL--RASAAASIVCVNSLLALQPEPHMV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 162 NYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSI------------IPLGRMGEPAEVAD 229
Cdd:PRK07062 158 ATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVESGQWRRRYEARADPGQSWeawtaalarkkgIPLGRLGRPDEAAR 237

                        250       260
                 ....*....|....*....|....
gi 148540050 230 ACAFLASDDSRYITGVSIEVAGGL 253
Cdd:PRK07062 238 ALFFLASPLSSYTTGSHIDVSGGF 261
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 13-209 1.25e-29

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 111.32  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIqRRYFQPPSV 92
Cdd:PRK07666  11 LITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEV--EAYGVKVVIATADVSDYEEVTAAIEQL-KNELGSIDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:PRK07666  88 LINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQS--GDIINISSTAGQKGAAVTSAYSASKFGVLG 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPM------TDKVPEKVI 209
Cdd:PRK07666 166 LTESLMQEVRKHNIRVTALTPSTVATDMavdlglTDGNPDKVM 208
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 7-252 2.06e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 111.82  E-value: 2.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRY 86
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKGAGAVRYEPADVTDEDQVARAVDAATAWH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK05875  85 GRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGG--GSFVGISSIAASNTHRWFGAYGVT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE--KVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK05875 163 KSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITEspELSADYRACTPLPRVGEVEDVANLAMFLLSDAASWITG 242


                 ....*...
gi 148540050 245 VSIEVAGG 252
Cdd:PRK05875 243 QVINVDGG 250
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 1-252 5.33e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 109.99  E-value: 5.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNeesanqTLELLPRehrGQEHMAlgVDVSSKDSVEKLVT 80
Cdd:PRK06523   1 MSFFLELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARS------RPDDLPE---GVEFVA--ADLTTAEGCAAVAR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  81 SIQRRyFQPPSVCVNAAG--ITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKV-GN 157
Cdd:PRK06523  70 AVLER-LGGVDILVHVLGgsSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGS--GVIIHVTSIQRRLpLP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 158 IGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE--------------KVIDKITSIIPLGRMGE 223
Cdd:PRK06523 147 ESTTAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAErlaeaagtdyegakQIIMDSLGGIPLGRPAE 226

                        250       260
                 ....*....|....*....|....*....
gi 148540050 224 PAEVADACAFLASDDSRYITGVSIEVAGG 252
Cdd:PRK06523 227 PEEVAELIAFLASDRAASITGTEYVIDGG 255
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 7-248 5.50e-29

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 109.59  E-value: 5.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEH-MALGVDVSSKDSVEKLVTSIQRR 85
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQwFILDLLTCTSENCQQLAQRIAVN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGSIVGKVGNIGQVNYAS 165
Cdd:cd05340   82 YPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLK--SDAGSLVFTSSSVGRQGRANWGAYAV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM-TDKVPekviDKITSIIPlgrmgEPAEVADACAFLASDDSRYITG 244
Cdd:cd05340  160 SKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMrASAFP----TEDPQKLK-----TPADIMPLYLWLMGDDSRRKTG 230


                 ....
gi 148540050 245 VSIE 248
Cdd:cd05340  231 MTFD 234
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
13-253 6.17e-29

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 109.81  E-value: 6.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVA-DRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIqRRYFQPPS 91
Cdd:PRK08063   8 LVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEI--EALGRKALAVKANVGDVEKIKEMFAQI-DEEFGRLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIvgkvGNIGQV-NYAS---SK 167
Cdd:PRK08063  85 VFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGG--GKIISLSSL----GSIRYLeNYTTvgvSK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGV 245
Cdd:PRK08063 159 AALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPnrEELLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMIRGQ 238


                 ....*...
gi 148540050 246 SIEVAGGL 253
Cdd:PRK08063 239 TIIVDGGR 246
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 10-252 3.74e-28

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 107.86  E-value: 3.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLEllpREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQP 89
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAE---AAQGGPRALGVQCDVTSEAQVQSAFEQAVLE-FGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd08943   78 LDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIG-GNIVFNASKNAVAPGPNAAAYSAAKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTpmTDKVPEKVIDKITSIIP------------LGRMGEPAEVADACAFLASD 237
Cdd:cd08943  157 EAHLARCLALEGGEDGIRVNTVNPDAVFR--GSKIWEGVWRAARAKAYglleeeyrtrnlLKREVLPEDVAEAVVAMASE 234

                        250
                 ....*....|....*
gi 148540050 238 DSRYITGVSIEVAGG 252
Cdd:cd08943  235 DFGKTTGAIVTVDGG 249
PRK06949 PRK06949
SDR family oxidoreductase;
1-253 3.92e-28

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 107.93  E-value: 3.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANqtlELLPR-EHRGQEHMALGVDVSSKDSVEKLV 79
Cdd:PRK06949   1 MGRSINLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLK---ELRAEiEAEGGAAHVVSLDVTDYQSIKAAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  80 TSIQRRyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALV----SAGSAK--GSIITVGSIVG 153
Cdd:PRK06949  78 AHAETE-AGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIarakGAGNTKpgGRIINIASVAG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 154 -KV-GNIGQvnYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE-KVIDKITSIIPLGRMGEPAEVADA 230
Cdd:PRK06949 157 lRVlPQIGL--YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWEtEQGQKLVSMLPRKRVGKPEDLDGL 234

                        250       260
                 ....*....|....*....|...
gi 148540050 231 CAFLASDDSRYITGVSIEVAGGL 253
Cdd:PRK06949 235 LLLLAADESQFINGAIISADDGF 257
PRK07577 PRK07577
SDR family oxidoreductase;
9-252 7.28e-28

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 106.35  E-value: 7.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNeesanqTLELLPREhrgqehmALGVDVSSKDSVEKLVTSIQRRYfq 88
Cdd:PRK07577   3 SRTVLVTGATKGIGLALSLRLANLGHQVIGIARS------AIDDFPGE-------LFACDLADIEQTAATLAQINEIH-- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIvGKVGNIGQVNYASSKA 168
Cdd:PRK07577  68 PVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQ--GRIVNICSR-AIFGALDRTSYSAAKS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPM---TDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGV 245
Cdd:PRK07577 145 ALVGCTRTWALELAEYGITVNAVAPGPIETELfrqTRPVGSEEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQ 224


                 ....*..
gi 148540050 246 SIEVAGG 252
Cdd:PRK07577 225 VLGVDGG 231
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 10-211 8.20e-28

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 106.17  E-value: 8.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGA-SVVVADRNEESANQTLELLPREHRGQEHMALgvDVSSKDSVEKLVTSIQRRYfQ 88
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQL--DVTDDASIEAAADFVEEKY-G 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKME-EDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKgsIITVGSIVGKVgnigQVNYASSK 167
Cdd:cd05324   78 GLDILVNNAGIAFKGFDDSTPtREQARETMKTNFFGTVDVTQALLPLLKKSPAGR--IVNVSSGLGSL----TSAYGVSK 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDK 211
Cdd:cd05324  152 AALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAPKTPEE 195
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 13-252 1.86e-27

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 105.96  E-value: 1.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVV-ADRNEESANQTLELLpREHRGQEHMALGvDVSSKDSVEKLVTSIQRRYFQpPS 91
Cdd:PRK06077  10 VVTGSGRGIGRAIAVRLAKEGSLVVVnAKKRAEEMNETLKMV-KENGGEGIGVLA-DVSTREGCETLAKATIDRYGV-AD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQdeFILKMEEDD--FDKVIKVNLKGTFLVTQAVSKALvsagSAKGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:PRK06077  87 ILVNNAGLGL--FSPFLNVDDklIDKHISTDFKSVIYCSQELAKEM----REGGAIVNIASVAGIRPAYGLSIYGAMKAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKfGIRCNCVLPGFITTPMTDKVP------EKVIDKITSIipLGRMGEPAEVADACAFLASDDSryIT 243
Cdd:PRK06077 161 VINLTKYLALELAP-KIRVNAIAPGFVKTKLGESLFkvlgmsEKEFAEKFTL--MGKILDPEEVAEFVAAILKIES--IT 235


                 ....*....
gi 148540050 244 GVSIEVAGG 252
Cdd:PRK06077 236 GQVFVLDSG 244
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-252 2.44e-27

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 105.64  E-value: 2.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGG--SGIGRAVCQRFATEGASVVVA-----DRNEESANQTLE--LLPREHR--GQEHMALGVDVSSKDS 74
Cdd:PRK12859   3 QLKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTywtayDKEMPWGVDQDEqiQLQEELLknGVKVSSMELDLTQNDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  75 VEKLVTSIQRRyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsAGSAKGSIITVGSIVGK 154
Cdd:PRK12859  83 PKELLNKVTEQ-LGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGF--DKKSGGRIINMTSGQFQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 155 VGNIGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTP-MTDKVPEKVIDKItsiiPLGRMGEPAEVADACAF 233
Cdd:PRK12859 160 GPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGwMTEEIKQGLLPMF----PFGRIGEPKDAARLIKF 235

                        250
                 ....*....|....*....
gi 148540050 234 LASDDSRYITGVSIEVAGG 252
Cdd:PRK12859 236 LASEEAEWITGQIIHSEGG 254
PRK05650 PRK05650
SDR family oxidoreductase;
13-202 6.46e-27

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 104.74  E-value: 6.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQEHMaLGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLL-REAGGDGFY-QRCDVRDYSQLTALAQACEEK-WGGIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:PRK05650  81 IVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKS--GRIVNIASMAGLMQGPAMSSYNVAKAGVVA 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTD 202
Cdd:PRK05650 159 LSETLLVELADDEIGVHVVCPSFFQTNLLD 188
PRK09135 PRK09135
pteridine reductase; Provisional
 9-252 6.59e-27

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 104.24  E-value: 6.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQ 88
Cdd:PRK09135   6 AKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADALAAELNALRPGSAAALQADLLDPDALPELVAACVAA-FG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsaGSAKGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK09135  85 RLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQL---RKQRGAIVNITDIHAERPLKGYPVYCAAKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKfGIRCNCVLPGFITTPMTDK-VPEKVIDKITSIIPLGRMGEPAEVADACAFLAsDDSRYITGVSI 247
Cdd:PRK09135 162 ALEMLTRSLALELAP-EVRVNAVAPGAILWPEDGNsFDEEARQAILARTPLKRIGTPEDIAEAVRFLL-ADASFITGQIL 239


                 ....*
gi 148540050 248 EVAGG 252
Cdd:PRK09135 240 AVDGG 244
PRK07326 PRK07326
SDR family oxidoreductase;
13-205 2.00e-26

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 102.78  E-value: 2.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRgqehmALGV--DVSSKDSVEKLVTSIQRRyFQPP 90
Cdd:PRK07326  10 LITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGN-----VLGLaaDVRDEADVQRAVDAIVAA-FGGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsakGSIITVGSIVGKVGNIGQVNYASSKAGV 170
Cdd:PRK07326  84 DVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG---GYIINISSLAGTNFFAGGAAYNASKFGL 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 148540050 171 QGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP 205
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTP 195
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 13-198 1.18e-24

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 98.51  E-value: 1.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHmALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:cd05346    4 LITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVL-PLQLDVSDRESIEAALENLPEE-FRDIDI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQD-EFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKV----GNIgqvnYASSK 167
Cdd:cd05346   82 LVNNAGLALGlDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQ--GHIINLGSIAGRYpyagGNV----YCATK 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITT 198
Cdd:cd05346  156 AAVRQFSLNLRKDLIGTGIRVTNIEPGLVET 186
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 14-235 1.21e-24

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 97.84  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  14 VTGGGSGIGRAVCQRFATEGASVVVADRNEEsanqTLELLPREHRGQEHMALGV--DVSSKDSVEKLVTSIQRRyFQPPS 91
Cdd:cd05360    5 ITGASSGIGRATALAFAERGAKVVLAARSAE----ALHELAREVRELGGEAIAVvaDVADAAQVERAADTAVER-FGRID 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:cd05360   80 TWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGG--GALINVGSLLGYRSAPLQAAYSASKHAVR 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148540050 172 GLTRTAAKELSKFG--IRCNCVLPGFITTPMTDKVPEKViDKITSiiPLGRMGEPAEVADACAFLA 235
Cdd:cd05360  158 GFTESLRAELAHDGapISVTLVQPTAMNTPFFGHARSYM-GKKPK--PPPPIYQPERVAEAIVRAA 220
PRK07832 PRK07832
SDR family oxidoreductase;
13-211 1.68e-24

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 98.58  E-value: 1.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQEHMALGVDVSSKDSVEKLVTSIQRRYfQPPSV 92
Cdd:PRK07832   4 FVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADA-RALGGTVPEHRALDISDYDAVAAFAADIHAAH-GSMDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:PRK07832  82 VMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRG-GHLVNVSSAAGLVALPWHAAYSASKFGLRG 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDK 211
Cdd:PRK07832 161 LSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEIAGVDR 199
PRK09072 PRK09072
SDR family oxidoreductase;
6-230 2.56e-24

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 97.70  E-value: 2.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREHRGQE-HMALGVDVSSKDSVEKLVTSIQR 84
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEK----LEALAARLPYPGrHRWVVADLTSEAGREAVLARARE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 ryFQPPSVCVNAAGITQdeFIL--KMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKgsIITVGSIVGKVGNIGQVN 162
Cdd:PRK09072  78 --MGGINVLINNAGVNH--FALleDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAM--VVNVGSTFGSIGYPGYAS 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKitsiipLG-RMGEPAEVADA 230
Cdd:PRK09072 152 YCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAMNSEAVQALNRA------LGnAMDDPEDVAAA 214
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 13-244 4.32e-24

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 96.69  E-value: 4.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESAN--------QTLELLPREHR--GQEHMALGVDVSSKDSVEKLVTSI 82
Cdd:cd05338    7 FVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDngsakslpGTIEETAEEIEaaGGQALPIVVDVRDEDQVRALVEAT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 qRRYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVN 162
Cdd:cd05338   87 -VDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAG--QGHILNISPPLSLRPARGDVA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPG-FITTP-MTDKVPEKVIDKITSiiplgrmgePAEVADACAFLASDDSR 240
Cdd:cd05338  164 YAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStAIETPaATELSGGSDPARARS---------PEILSDAVLAILSRPAA 234


                 ....
gi 148540050 241 YITG 244
Cdd:cd05338  235 ERTG 238
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 6-253 4.42e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 97.04  E-value: 4.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQEHMALGVDVSSKDSVEKLVTSIqrr 85
Cdd:PRK06125   4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADL-RAAHGVDVAVHALDLSSPEAREQLAAEA--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yfQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakgsiitvGSIVGKVGNIGQ---VN 162
Cdd:PRK06125  80 --GDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGS--------GVIVNVIGAAGEnpdAD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 Y---ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV----------PEKVIDKITSIIPLGRMGEPAEVAD 229
Cdd:PRK06125 150 YicgSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLlkgraraelgDESRWQELLAGLPLGRPATPEEVAD 229

                        250       260
                 ....*....|....*....|....
gi 148540050 230 ACAFLASDDSRYITGVSIEVAGGL 253
Cdd:PRK06125 230 LVAFLASPRSGYTSGTVVTVDGGI 253
PRK06181 PRK06181
SDR family oxidoreductase;
10-198 5.32e-24

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 96.97  E-value: 5.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREHRGQEHMALGV--DVSSKDSVEKLVTSIQRRyF 87
Cdd:PRK06181   2 KVVIITGASEGIGRALAVRLARAGAQLVLAARNETR----LASLAQELADHGGEALVVptDVSDAEACERLIEAAVAR-F 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  88 QPPSVCVNAAGITQDEFILKMEEDD-FDKVIKVNLKGTFLVTQAvskALVSAGSAKGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK06181  77 GGIDILVNNAGITMWSRFDELTDLSvFERVMRVNYLGAVYCTHA---ALPHLKASRGQIVVVSSLAGLTGVPTRSGYAAS 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITT 198
Cdd:PRK06181 154 KHALHGFFDSLRIELADDGVAVTVVCPGFVAT 185
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 13-234 6.55e-24

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 96.30  E-value: 6.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESAnqtLELLPREHRGQEHMALGV--DVSSKDSVEKLVTSIqRRYFQPP 90
Cdd:cd05373    3 AVVGAGDGLGAAIARRFAAEGFSVALAARREAKL---EALLVDIIRDAGGSAKAVptDARDEDEVIALFDLI-EEEIGPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKAGV 170
Cdd:cd05373   79 EVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARG--RGTIIFTGATASLRGRAGFAAFAGAKFAL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 171 QGLTRTAAKELSKFGIRCNCVL------PGFITTPMTDKVPEKVIDKITsiiplgrmgEPAEVADACAFL 234
Cdd:cd05373  157 RALAQSMARELGPKGIHVAHVIidggidTDFIRERFPKRDERKEEDGIL---------DPDAIAEAYWQL 217
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 12-213 6.82e-24

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 96.13  E-value: 6.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  12 TLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHrGQEHMALGVDVSSKDSV-EKLVTSIQRRyfqPP 90
Cdd:cd05356    4 AVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKY-GVETKTIAADFSAGDDIyERIEKELEGL---DI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAAGITQD--EFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGN-IGQVnYASSK 167
Cdd:cd05356   80 GILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRK--KGAIVNISSFAGLIPTpLLAT-YSASK 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTdKVPEKVIDKIT 213
Cdd:cd05356  157 AFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMS-KIRKSSLFVPS 201
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 13-235 1.13e-23

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 94.12  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVAdrneesanqtlellprehrgqehmalgvdVSSKDSVeklvtsiqrryfqppsv 92
Cdd:cd02266    2 LVTGGSGGIGGAIARWLASRGSPKVLV-----------------------------VSRRDVV----------------- 35

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 cVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:cd02266   36 -VHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKR--LGRFILISSVAGLFGAPGLGGYAASKAALDG 112

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLA 235
Cdd:cd02266  113 LAQQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARALLNAL 175
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 7-252 1.30e-23

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 96.08  E-value: 1.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGvDVSSKDSVEKLVTSIQRry 86
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVA-DLTKREDLERTVKELKN-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKGSIITVGSIVGKVGNIGQVNYAss 166
Cdd:PRK08339  83 IGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVV-- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTD-----------KVPEKVIDKITSIIPLGRMGEPAEVADACAFLA 235
Cdd:PRK08339 161 RISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIqlaqdrakregKSVEEALQEYAKPIPLGRLGEPEEIGYLVAFLA 240

                        250
                 ....*....|....*..
gi 148540050 236 SDDSRYITGVSIEVAGG 252
Cdd:PRK08339 241 SDLGSYINGAMIPVDGG 257
PRK08267 PRK08267
SDR family oxidoreductase;
13-230 1.40e-23

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 95.78  E-value: 1.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHmalgVDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAWTGA----LDVTDRAAWDAALADFAAATGGRLDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAvskAL----VSAGSAkgsIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK08267  81 LFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHA---ALpylkATPGAR---VINTSSASAIYGQPGLAVYSATKF 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVidKITSIIPLGRMGEPAEVADA 230
Cdd:PRK08267 155 AVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEV--DAGSTKRLGVRLTPEDVAEA 214
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 13-253 4.85e-23

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 94.10  E-value: 4.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANqtlellprehrgqehmalgVDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHTVIGIDLREADVI-------------------ADLSTPEGRAAAIADVLARCSGVLDG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFIlkmeeddfDKVIKVNLKGTFLVTQAVSKALvsAGSAKGSIITVGSIVG------------------- 153
Cdd:cd05328   64 LVNCAGVGGTTVA--------GLVLKVNYFGLRALMEALLPRL--RKGHGPAAVVVSSIAGagwaqdklelakalaagte 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 154 --------KVGNIGQVNYASSKAGVQGLTRTAAKE-LSKFGIRCNCVLPGFITTPMT-----DKVPEKVIDKITSiiPLG 219
Cdd:cd05328  134 aravalaeHAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILqaflqDPRGGESVDAFVT--PMG 211

                        250       260       270
                 ....*....|....*....|....*....|....
gi 148540050 220 RMGEPAEVADACAFLASDDSRYITGVSIEVAGGL 253
Cdd:cd05328  212 RRAEPDEIAPVIAFLASDAASWINGANLFVDGGL 245
PRK08416 PRK08416
enoyl-ACP reductase;
12-252 7.50e-23

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 93.68  E-value: 7.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  12 TLVTGGGS-GIGRAVCQRFATEGASVVVA-DRNEESANQTLELLPREHrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQP 89
Cdd:PRK08416  10 TLVISGGTrGIGKAIVYEFAQSGVNIAFTyNSNVEEANKIAEDLEQKY-GIKAKAYPLNILEPETYKELFKKIDED-FDR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFIlkmeeDDFDKVIKVNLKG----------TFLV-TQAVSKALVSAGSakGSIITVGSivgkVGNI 158
Cdd:PRK08416  88 VDFFISNAIISGRAVV-----GGYTKFMRLKPKGlnniytatvnAFVVgAQEAAKRMEKVGG--GSIISLSS----TGNL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 159 GQV-NYA---SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLGRMGEPAEVADACA 232
Cdd:PRK08416 157 VYIeNYAghgTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTnyEEVKAKTEELSPLNRMGQPEDLAGACL 236

                        250       260
                 ....*....|....*....|
gi 148540050 233 FLASDDSRYITGVSIEVAGG 252
Cdd:PRK08416 237 FLCSEKASWLTGQTIVVDGG 256
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 13-254 8.74e-23

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 93.83  E-value: 8.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQ--EHMALgvDVSSKDSVEKLVTSIQRRyFQPP 90
Cdd:cd05327    5 VITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAkvEVIQL--DLSSLASVRQFAEEFLAR-FPRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAAGITQDEFilKMEEDDFDKVIKVNLKGTFLVTQAVSKALVsaGSAKGSIITVGSIVGKVGNIGQVN-------- 162
Cdd:cd05327   82 DILINNAGIMAPPR--RLTKDGFELQFAVNYLGHFLLTNLLLPVLK--ASAPSRIVNVSSIAHRAGPIDFNDldlennke 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 ------YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKItsIIPLGRMGEPAEVADACAFLAS 236
Cdd:cd05327  158 yspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFLLYK--LLRPFLKKSPEQGAQTALYAAT 235

                        250
                 ....*....|....*...
gi 148540050 237 DDSryITGVSievaGGLF 254
Cdd:cd05327  236 SPE--LEGVS----GKYF 247
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 13-226 3.10e-22

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 91.88  E-value: 3.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGvDVSSKDSVEKLVTSIQRRYFQpPSV 92
Cdd:cd05332    7 IITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPL-DMSDLEDAEQVVEEALKLFGG-LDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:cd05332   85 LINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERS--QGSIVVVSSIAGKIGVPFRTAYAASKHALQG 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAE 226
Cdd:cd05332  163 FFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGSMSAKMDDTTANGMSPE 216
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-252 4.11e-22

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 91.36  E-value: 4.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGvDVSSKDSVEKLVTSIQRR 85
Cdd:PRK05786   2 RLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTL--SKYGNIHYVVG-DVSSTESARNVIEKAAKV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YFQPPSVCVNAAGITQDefilKMEE-DDFDKVIKVNLKGTFLVTQAVSKALvsagsAKGSIITVGSIVGKVGNIG--QVN 162
Cdd:PRK05786  79 LNAIDGLVVTVGGYVED----TVEEfSGLEEMLTNHIKIPLYAVNASLRFL-----KEGSSIVLVSSMSGIYKASpdQLS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFIttpMTDKVPEKVIDKITsiiPLGR-MGEPAEVADACAFLASDDSRY 241
Cdd:PRK05786 150 YAVAKAGLAKAVEILASELLGRGIRVNGIAPTTI---SGDFEPERNWKKLR---KLGDdMAPPEDFAKVIIWLLTDEADW 223

                        250
                 ....*....|.
gi 148540050 242 ITGVSIEVAGG 252
Cdd:PRK05786 224 VDGVVIPVDGG 234
PRK12742 PRK12742
SDR family oxidoreductase;
9-252 4.43e-22

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 91.36  E-value: 4.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTlelLPREHRGQehmALGVDVSSKDSVEKLVtsiqrRYFQ 88
Cdd:PRK12742   6 GKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAER---LAQETGAT---AVQTDSADRDAVIDVV-----RKSG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsagSAKGSIITVGSIVG-KVGNIGQVNYASSK 167
Cdd:PRK12742  75 ALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQM----PEGGRIIIIGSVNGdRMPVAGMAAYAASK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTdkvPEK--VIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGV 245
Cdd:PRK12742 151 SALQGMARGLARDFGPRGITINVVQPGPIDTDAN---PANgpMKDMMHSFMAIKRHGRPEEVAGMVAWLAGPEASFVTGA 227


                 ....*..
gi 148540050 246 SIEVAGG 252
Cdd:PRK12742 228 MHTIDGA 234
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 13-234 4.52e-22

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 91.03  E-value: 4.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREHRGQEHMALGvDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:cd08929    4 LVTGASRGIGEATARLLHAEGYRVGICARDEAR----LAAAAAQELEGVLGLAG-DVRDEADVRRAVDAMEEA-FGGLDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVT-QAVSKALVSAGsakGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:cd08929   78 LVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIhKAAPALLRRGG---GTIVNVGSLAGKNAFKGGAAYNASKFGLL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPekvidkitsiiPLGRMGEPAEVADACAFL 234
Cdd:cd08929  155 GLSEAAMLDLREANIRVVNVMPGSVDTGFAGSPE-----------GQAWKLAPEDVAQAVLFA 206
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 13-205 5.11e-22

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 90.82  E-value: 5.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVAD-RNEESANQTLELLPREHRGQehmALGVDVSS--KDSVEKLVTSIQrryFQP 89
Cdd:cd05325    2 LITGASRGIGLELVRQLLARGNNTVIATcRDPSAATELAALGASHSRLH---ILELDVTDeiAESAEAVAERLG---DAG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGI-TQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKgsIITVGSIVGKVGNI---GQVNYAS 165
Cdd:cd05325   76 LDVLINNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAK--IINISSRVGSIGDNtsgGWYSYRA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP 205
Cdd:cd05325  154 SKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFA 193
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 13-204 2.73e-21

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 89.31  E-value: 2.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPRE-HRGQEHMALG-VDVSSKDSVEKLVTSIQRRYFQPP 90
Cdd:cd05350    2 LITGASSGIGRALAREFAKAGYNVALAARRTDR----LDELKAElLNPNPSVEVEiLDVTDEERNQLVIAELEAELGGLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAA-GITQDEFILKMEedDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd05350   78 LVIINAGvGKGTSLGDLSFK--AFRETIDTNLLGAAAILEAALPQFRAKGR--GHLVLISSVAALRGLPGAAAYSASKAA 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV 204
Cdd:cd05350  154 LSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANM 188
PRK07454 PRK07454
SDR family oxidoreductase;
9-235 2.93e-21

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 89.25  E-value: 2.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEEsanqTLELLPRE--HRGQEHMALGVDVSSKDSVEKLVTSIQRRy 86
Cdd:PRK07454   6 MPRALITGASSGIGKATALAFAKAGWDLALVARSQD----ALEALAAElrSTGVKAAAYSIDLSNPEAIAPGIAELLEQ- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK07454  81 FGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGG--GLIINVSSIAARNAFPQWGAYCVS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKvpekviDKITSIIPLGRMGEPAEVADACAFLA 235
Cdd:PRK07454 159 KAALAAFTKCLAEEERSHGIRVCTITLGAVNTPLWDT------ETVQADFDRSAMLSPEQVAQTILHLA 221
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 7-248 4.42e-21

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 88.78  E-value: 4.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEH-MALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAiIPLDLLTATPQNYQQLADTIEEQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YFQPPSVCVNaAGITQDefILKMEE---DDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGSIVGKVGNIGQVN 162
Cdd:PRK08945  90 FGRLDGVLHN-AGLLGE--LGPMEQqdpEVWQDVMQVNVNATFMLTQALLPLLLK--SPAASLVFTSSSVGRQGRANWGA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITT-----------PMTDKVPEkvidkitSIIPLgrmgepaevadaC 231
Cdd:PRK08945 165 YAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTamrasafpgedPQKLKTPE-------DIMPL------------Y 225

                        250
                 ....*....|....*..
gi 148540050 232 AFLASDDSRYITGVSIE 248
Cdd:PRK08945 226 LYLMGDDSRRKNGQSFD 242
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 13-252 7.37e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 88.92  E-value: 7.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGsGIGRAVCQRFATeGASVVVADRNEESANQTLELLPREhrGQEHMALGVDVSSKDSVEKLVTSIQRryFQPPSV 92
Cdd:PRK06940   6 VVIGAG-GIGQAIARRVGA-GKKVLLADYNEENLEAAAKTLREA--GFDVSTQEVDVSSRESVKALAATAQT--LGPVTG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQdefilkmEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkgsiITVGSIVG------------------- 153
Cdd:PRK06940  80 LVHTAGVSP-------SQASPEAILKVDLYGTALVLEEFGKVIAPGGAG----VVIASQSGhrlpaltaeqeralattpt 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 154 ---------KVGNIGQ--VNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMT-DKVPEKVIDKITSII---PL 218
Cdd:PRK06940 149 eellslpflQPDAIEDslHAYQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAqDELNGPRGDGYRNMFaksPA 228

                        250       260       270
                 ....*....|....*....|....*....|....
gi 148540050 219 GRMGEPAEVADACAFLASDDSRYITGVSIEVAGG 252
Cdd:PRK06940 229 GRPGTPDEIAALAEFLMGPRGSFITGSDFLVDGG 262
PRK07041 PRK07041
SDR family oxidoreductase;
13-252 1.04e-20

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 87.40  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPrEHRGQEHMALgvDVSSKDSVEKLVtsiqRRYFQPPSV 92
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALG-GGAPVRTAAL--DITDEAAVDAFF----AEAGPFDHV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEfILKMEEDDFDKVIKVNLKGTFLVTQAvskALVSAGsakGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:PRK07041  74 VITAADTPGGP-VRALPLAAAQAAMDSKFWGAYRVARA---ARIAPG---GSLTFVSGFAAVRPSASGVLQGAINAALEA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 173 LTRTAAKELSKfgIRCNCVLPGFITTPMTDKVP----EKVIDKITSIIPLGRMGEPAEVADACAFLASddSRYITGVSIE 248
Cdd:PRK07041 147 LARGLALELAP--VRVNTVSPGLVDTPLWSKLAgdarEAMFAAAAERLPARRVGQPEDVANAILFLAA--NGFTTGSTVL 222


                 ....
gi 148540050 249 VAGG 252
Cdd:PRK07041 223 VDGG 226
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 1-201 1.22e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 88.49  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRgqeHMALGVDVSSKDSVEKLVT 80
Cdd:PRK05872   1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDR---VLTVVADVTDLAAMQAAAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  81 SIQRRyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVsagSAKGSIITVGSIVGKVGNIGQ 160
Cdd:PRK05872  78 EAVER-FGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALI---ERRGYVLQVSSLAAFAAAPGM 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 148540050 161 VNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMT 201
Cdd:PRK05872 154 AAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLV 194
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 13-253 1.38e-20

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 88.06  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSK----DSVEKLVTSIqRRYFQ 88
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARRPNSAVTCQADLSNSatlfSRCEAIIDAC-FRAFG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   89 PPSVCVNAAGITQDEFILKMEEDDFD-----------KVIKVNLKGTFLVTQAVSKALVSAGSA-KGSIITVGSIVGKVG 156
Cdd:TIGR02685  84 RCDVLVNNASAFYPTPLLRGDAGEGVgdkkslevqvaELFGSNAIAPYFLIKAFAQRQAGTRAEqRSTNLSIVNLCDAMT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  157 N---IGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPmtDKVPEKVIDKITSIIPLGRMGEPAE-VADACA 232
Cdd:TIGR02685 164 DqplLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLP--DAMPFEVQEDYRRKVPLGQREASAEqIADVVI 241

                         250       260
                  ....*....|....*....|.
gi 148540050  233 FLASDDSRYITGVSIEVAGGL 253
Cdd:TIGR02685 242 FLVSPKAKYITGTCIKVDGGL 262
PRK09134 PRK09134
SDR family oxidoreductase;
1-252 2.09e-20

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 87.29  E-value: 2.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVV-ADRNEESANQTLELLPRehRGQEHMALGVDVSSKDSVEKLV 79
Cdd:PRK09134   1 SPPMSMAAPRAALVTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAAEIRA--LGRRAVALQADLADEAEVRALV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  80 TSIqRRYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAgsAKGSIITVgsIVGKVGNIG 159
Cdd:PRK09134  79 ARA-SAALGPITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPAD--ARGLVVNM--IDQRVWNLN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 160 Q--VNYASSKAGVQGLTRTAAKELSKfGIRCNCVLPGfITTPMTDKVPEKvIDKITSIIPLGRMGEPAEVADACAFLAsd 237
Cdd:PRK09134 154 PdfLSYTLSKAALWTATRTLAQALAP-RIRVNAIGPG-PTLPSGRQSPED-FARQHAATPLGRGSTPEEIAAAVRYLL-- 228

                        250
                 ....*....|....*
gi 148540050 238 DSRYITGVSIEVAGG 252
Cdd:PRK09134 229 DAPSVTGQMIAVDGG 243
PRK12744 PRK12744
SDR family oxidoreductase;
1-252 2.41e-20

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 87.10  E-value: 2.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTrLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEES----ANQTLELLprEHRGQEHMALGVDVSSKDSVE 76
Cdd:PRK12744   1 MADHS-LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAAskadAEETVAAV--KAAGAKAVAFQADLTTAAAVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  77 KL-VTSIQRryFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsagSAKGSIIT-VGSIVGK 154
Cdd:PRK12744  78 KLfDDAKAA--FGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL----NDNGKIVTlVTSLLGA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 155 VGNiGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM--TDKVPEKV----------------IDKITSII 216
Cdd:PRK12744 152 FTP-FYSAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFfyPQEGAEAVayhktaaalspfsktgLTDIEDIV 230

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148540050 217 PLGRmgepaevadacaFLASdDSRYITGVSIEVAGG 252
Cdd:PRK12744 231 PFIR------------FLVT-DGWWITGQTILINGG 253
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 7-233 4.19e-20

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 86.05  E-value: 4.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPRE--HRGQEHMALGVDVSSK----DSVEKLVT 80
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDR----LEALADEleAEGGKALVLELDVTDEqqvdAAVERTVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  81 SIQRRyfqppSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQ 160
Cdd:cd08934   77 ALGRL-----DILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRN--KGTIVNISSVAGRVAVRNS 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148540050 161 VNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKV-----IDKITSIIPLgrmgEPAEVADACAF 233
Cdd:cd08934  150 AVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTItkeayEERISTIRKL----QAEDIAAAVRY 223
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 9-251 8.31e-20

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 84.68  E-value: 8.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNE-ESANQTLELLPrehrgqehmaLGVDVSSKDSVEKLVTSIQRRYf 87
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAEnEEADASIIVLD----------SDSFTEQAKQVVASVARLSGKV- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  88 qppSVCVNAAGITQDEfilKMEEDDF----DKVIKVNLKGTFLVTQAVSKALVSAgsakGSIITVGSIVGKVGNIGQVNY 163
Cdd:cd05334   70 ---DALICVAGGWAGG---SAKSKSFvknwDLMWKQNLWTSFIASHLATKHLLSG----GLLVLTGAKAALEPTPGMIGY 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELS--KFGIRCNCVLPGFITTPMTDK-VPEKVIDKITSiiplgrmgePAEVADACAFLASDDSR 240
Cdd:cd05334  140 GAAKAAVHQLTQSLAAENSglPAGSTANAILPVTLDTPANRKaMPDADFSSWTP---------LEFIAELILFWASGAAR 210

                        250
                 ....*....|.
gi 148540050 241 YITGVSIEVAG 251
Cdd:cd05334  211 PKSGSLIPVVT 221
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 14-199 3.20e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 84.97  E-value: 3.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  14 VTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSVC 93
Cdd:PRK07109  13 ITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEI--RAAGGEALAVVADVADAEAVQAAADRAEEE-LGPIDTW 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  94 VNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKAGVQGL 173
Cdd:PRK07109  90 VNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRD--RGAIIQVGSALAYRSIPLQSAYCAAKHAIRGF 167

                        170       180
                 ....*....|....*....|....*...
gi 148540050 174 TRTAAKEL--SKFGIRCNCVLPGFITTP 199
Cdd:PRK07109 168 TDSLRCELlhDGSPVSVTMVQPPAVNTP 195
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 10-252 5.04e-19

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 83.01  E-value: 5.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADrneESANQTLELLPREHRGQEHMALgvdvsSKDSVEKLVTSIQRRYFQP 89
Cdd:cd05361    2 SIALVTHARHFAGPASAEALTEDGYTVVCHD---ASFADAAERQAFESENPGTKAL-----SEQKPEELVDAVLQAGGAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:cd05361   74 DVLVSNDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGG--GSIIFITSAVPKKPLAYNSLYGPARAA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTP------MTDKVPEKViDKITSIIPLGRMGEPAEVADACAFLASDDSRYIT 243
Cdd:cd05361  152 AVALAESLAKELSRDNILVYAIGPNFFNSPtyfptsDWENNPELR-ERVKRDVPLGRLGRPDEMGALVAFLASRRADPIT 230


                 ....*....
gi 148540050 244 GVSIEVAGG 252
Cdd:cd05361  231 GQFFAFAGG 239
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 13-206 6.09e-19

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 83.48  E-value: 6.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTlELlpREHRGQEHMALGVDVSSKDSVEKlVTSIQRRYFQPPSV 92
Cdd:cd09805    4 LITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNGPGAK-EL--RRVCSDRLRTLQLDVTKPEQIKR-AAQWVKEHVGEKGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 --CVNAAGIT---QDEFILKMeeDDFDKVIKVNLKGTFLVTQAVskaLVSAGSAKGSIITVGSIVGKVGNIGQVNYASSK 167
Cdd:cd09805   80 wgLVNNAGILgfgGDEELLPM--DDYRKCMEVNLFGTVEVTKAF---LPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASK 154

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE 206
Cdd:cd09805  155 AAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSEL 193
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 13-215 8.33e-19

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 82.35  E-value: 8.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQehmalgVDVSSKDSVEKLVTSIQRRYfqpPS- 91
Cdd:cd05370    9 LITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNIHTIV------LDVGDAESVEALAEALLSEY---PNl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 -VCVNAAGITQDEFILKMEE--DDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:cd05370   80 dILINNAGIQRPIDLRDPASdlDKADTEIDTNLIGPIRLIKAFLPHLKK--QPEATIVNVSSGLAFVPMAANPVYCATKA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSI 215
Cdd:cd05370  158 ALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKM 204
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 6-230 1.45e-18

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 82.18  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREHRGQEH---MALGVDVSSKDSVEKLVTSI 82
Cdd:cd05343    3 RWRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDK----IEALAAECQSAGYptlFPYQCDLSNEEQILSMFSAI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 qRRYFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKGSIITVGSIVGKvgNIGQVN 162
Cdd:cd05343   79 -RTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDGHIININSMSGH--RVPPVS 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148540050 163 ----YASSKAGVQGLTRTAAKEL--SKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIPLGRMGEPAEVADA 230
Cdd:cd05343  156 vfhfYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVANA 229
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 13-164 1.81e-18

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 80.22  E-value: 1.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050    13 LVTGGGSGIGRAVCQRFATEGA-SVVVADRNEESANQTLELLPR-EHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPP 90
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAElEAAGARVTVVACDVADRDALAAVLAAIPAV-EGPL 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148540050    91 SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAgsakgsIITVGSIVGKVGNIGQVNYA 164
Cdd:smart00822  83 TGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDF------FVLFSSIAGVLGSPGQANYA 150
PRK06194 PRK06194
hypothetical protein; Provisional
 5-202 1.83e-18

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 82.37  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   5 TRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQR 84
Cdd:PRK06194   2 KDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAEL--RAQGAEVLGVRTDVSDAAQVEALADAALE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RYFQPPSVCvNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSA----KGSIITVGSIVGKVGNIGQ 160
Cdd:PRK06194  80 RFGAVHLLF-NNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEKdpayEGHIVNTASMAGLLAPPAM 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148540050 161 VNYASSKAGVQGLTRTAAKELSKFG--IRCNCVLPGFITTPMTD 202
Cdd:PRK06194 159 GIYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPTGIWQ 202
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 13-164 2.79e-18

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 83.19  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFA-TEGASVVVADR-----NEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRY 86
Cdd:cd08953  209 LVTGGAGGIGRALARALArRYGARLVLLGRsplppEEEWKAQTLAAL--EALGARVLYISADVTDAAAVRRLLEKVRERY 286

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148540050  87 fQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVskalvsAGSAKGSIITVGSIVGKVGNIGQVNYA 164
Cdd:cd08953  287 -GAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQAL------ADEPLDFFVLFSSVSAFFGGAGQADYA 357
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 13-164 3.88e-18

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 79.14  E-value: 3.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   13 LVTGGGSGIGRAVCQRFATEGAS-VVVADRNEESANQTLELLPR-EHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPP 90
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAQALIAElEARGVEVVVVACDVSDPDAVAALLAEIKAE-GPPI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148540050   91 SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAgsakgsIITVGSIVGKVGNIGQVNYA 164
Cdd:pfam08659  83 RGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDF------FVLFSSIAGLLGSPGQANYA 150
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 13-239 1.65e-17

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 78.87  E-value: 1.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGAS--VVVADRNEESANQTLELLPREHRGQEHMAlgvDVSSKDSVEKLVTSIQRRYFQPP 90
Cdd:cd05367    3 ILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEELRPGLRVTTVKA---DLSDAAGVEQLLEAIRKLDGERD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSaKGSIITVGSIVGKVGNIGQVNYASSKAGV 170
Cdd:cd05367   80 LLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGL-KKTVVNVSSGAAVNPFKGWGLYCSSKAAR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148540050 171 QGLTRTAAKELSkfGIRCNCVLPGFITTPMTDKV-----PEKVIDKITSIIPLGRMGEPAEVADACAFLASDDS 239
Cdd:cd05367  159 DMFFRVLAAEEP--DVRVLSYAPGVVDTDMQREIretsaDPETRSRFRSLKEKGELLDPEQSAEKLANLLEKDK 230
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 10-198 2.06e-17

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 79.23  E-value: 2.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehRGQEHMALGV--DVSSKDSVEKLVTSIQRRYF 87
Cdd:PRK05876   7 RGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHL----RAEGFDVHGVmcDVRHREEVTHLADEAFRLLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  88 QPPSVCVNaAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGSIVGKVGNIGQVNYASSK 167
Cdd:PRK05876  83 HVDVVFSN-AGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTG-GHVVFTASFAGLVPNAGLGAYGVAK 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITT 198
Cdd:PRK05876 161 YGVVGLAETLAREVTADGIGVSVLCPMVVET 191
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 14-200 2.14e-17

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 78.26  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  14 VTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALG-VDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:cd08931    5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAEL-----GAENVVAGaLDVTDRAAWAAALADFAAATGGRLDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKgsIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:cd08931   80 LFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGAR--VINTASSSAIYGQPDLAVYSATKFAVRG 157

                        170       180
                 ....*....|....*....|....*...
gi 148540050 173 LTRTAAKELSKFGIRCNCVLPGFITTPM 200
Cdd:cd08931  158 LTEALDVEWARHGIRVADVWPWFVDTPI 185
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 13-216 6.78e-17

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 77.51  E-value: 6.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEEsanqTLELLPREHRGQEHMALgvDVSSKDSVEKLVTSIQRRYfqpPS- 91
Cdd:COG3967    9 LITGGTSGIGLALAKRLHARGNTVIITGRREE----KLEEAAAANPGLHTIVL--DVADPASIAALAEQVTAEF---PDl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 -VCVNAAGITQDEfILKMEEDDFDKV---IKVNLKGTFLVTQAVSKALVSAGSAkgSIITVGSIVGKVGNIGQVNYASSK 167
Cdd:COG3967   80 nVLINNAGIMRAE-DLLDEAEDLADAereITTNLLGPIRLTAAFLPHLKAQPEA--AIVNVSSGLAFVPLAVTPTYSATK 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV--------PEKVIDKITSII 216
Cdd:COG3967  157 AALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQggdprampLDEFADEVMAGL 213
PRK05717 PRK05717
SDR family oxidoreductase;
10-253 7.52e-17

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 77.62  E-value: 7.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALGVDVSSKDSVEKLVTSIQRRYFQP 89
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKAL-----GENAWFIAMDVADEAQVAAGVAEVLGQFGRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAgiTQDEFILKMEEDD---FDKVIKVNLKGTFLVTQAVSKALVSAGsakGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK05717  86 DALVCNAA--IADPHNTTLESLSlahWNRVLAVNLTGPMLLAKHCAPYLRAHN---GAIVNLASTRARQSEPDTEAYAAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKfGIRCNCVLPGFITT-PMTDKVPEKVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGV 245
Cdd:PRK05717 161 KGGLLALTHALAISLGP-EIRVNAVSPGWIDArDPSQRRAEPLSEADHAQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQ 239


                 ....*...
gi 148540050 246 SIEVAGGL 253
Cdd:PRK05717 240 EFVVDGGM 247
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 9-230 7.70e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 77.64  E-value: 7.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESAN--QTLELLPrehrgqehmalgVDVSSKDSVEKLVTSIQRRy 86
Cdd:PRK06179   4 SKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAApiPGVELLE------------LDVTDDASVQAAVDEVIAR- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITqdeFILKMEEDDFD---KVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNY 163
Cdd:PRK06179  71 AGRIDVLVNNAGVG---LAGAAEESSIAqaqALFDTNVFGILRMTRAVLPHMRAQGS--GRIINISSVLGFLPAPYMALY 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITT-------------PMTDKVPEKVIDKITSIIPLGRmgEPAEVADA 230
Cdd:PRK06179 146 AASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTnfdanapepdsplAEYDRERAVVSKAVAKAVKKAD--APEVVADT 223
PRK07775 PRK07775
SDR family oxidoreductase;
10-236 9.40e-17

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 77.49  E-value: 9.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQP 89
Cdd:PRK07775  11 RPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKI--RADGGEAVAFPLDVTDPDSVKSFVAQAEEA-LGE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:PRK07775  88 IEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIE--RRRGDLIFVGSDVALRQRPHMGAYGAAKAG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 170 VQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIdkitsiiplGRMGE---------------PAEVADACAFL 234
Cdd:PRK07775 166 LEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWSLPAEVI---------GPMLEdwakwgqarhdyflrASDLARAITFV 236


                 ..
gi 148540050 235 AS 236
Cdd:PRK07775 237 AE 238
PRK06914 PRK06914
SDR family oxidoreductase;
10-244 1.79e-16

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 76.60  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQEHMAL-GVDVSSKDSVEKLVTSIQRryFQ 88
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQA-TQLNLQQNIKVqQLDVTDQNSIHNFQLVLKE--IG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKgsIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGK--IINISSISGRVGFPGLSPYVSSKY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITT-------------PMTDKVPEKVIDKITSIIPLG--RMGEPAEVADACAF 233
Cdd:PRK06914 159 ALEGFSESLRLELKPFGIDVALIEPGSYNTniwevgkqlaenqSETTSPYKEYMKKIQKHINSGsdTFGNPIDVANLIVE 238

                        250
                 ....*....|....
gi 148540050 234 LASDDS---RYITG 244
Cdd:PRK06914 239 IAESKRpklRYPIG 252
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 9-201 5.36e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 75.46  E-value: 5.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEEsanqTLELLPREHrGQEHMALGVDVSSKDSVEKLVTSIQRRyFQ 88
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTA----TLADLAEKY-GDRLLPLALDVTDRAAVFAAVETAVEH-FG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK08263  77 RLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRS--GHIIQISSIGGISAFPMSGIYHASKW 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPG-----FITTPMT 201
Cdd:PRK08263 155 ALEGMSEALAQEVAEFGIKVTLVEPGgystdWAGTSAK 192
PRK07024 PRK07024
SDR family oxidoreductase;
9-205 1.50e-15

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 73.81  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASV-VVADRNEEsanqtLELLPREHRGQE-HMALGVDVSSKDSVEKLVTS-IQRr 85
Cdd:PRK07024   2 PLKVFITGASSGIGQALAREYARQGATLgLVARRTDA-----LQAFAARLPKAArVSVYAADVRDADALAAAAADfIAA- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAGITQDefILKMEEDD---FDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVN 162
Cdd:PRK07024  76 -HGLPDVVIANAGISVG--TLTEEREDlavFREVMDTNYFGMVATFQPFIAPMRAARR--GTLVGIASVAGVRGLPGAGA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148540050 163 YASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP 205
Cdd:PRK07024 151 YSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMTAHNP 193
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 13-200 2.32e-15

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 72.23  E-value: 2.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEEsanqtlellprehrgqehmALGVDVSSKDSVEKLVTSIqrryfQPPSV 92
Cdd:cd11731    2 IVIGATGTIGLAVAQLLSAHGHEVITAGRSSG-------------------DYQVDITDEASIKALFEKV-----GHFDA 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsagSAKGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:cd11731   58 IVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL----NDGGSITLTSGILAQRPIPGGAAAATVNGALEG 133

                        170       180
                 ....*....|....*....|....*...
gi 148540050 173 LTRTAAKELSKfGIRCNCVLPGFITTPM 200
Cdd:cd11731  134 FVRAAAIELPR-GIRINAVSPGVVEESL 160
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
33-253 2.50e-15

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 73.11  E-value: 2.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  33 GASVVVADRNEESAnqTLELLprehrgqehmaLGVDVSSKDSVEKLVTSIQRRYfqppSVCVNAAGITQDEfilkmeedD 112
Cdd:PRK12428   9 GARVIGVDRREPGM--TLDGF-----------IQADLGDPASIDAAVAALPGRI----DALFNIAGVPGTA--------P 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 113 FDKVIKVNlkgtFLVTQAVSKALVSAGSAKGSIITVGSIVGK--VGNI----GQVNYASSKAGVQGLTRTA--------- 177
Cdd:PRK12428  64 VELVARVN----FLGLRHLTEALLPRMAPGGAIVNVASLAGAewPQRLelhkALAATASFDEGAAWLAAHPvalatgyql 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 178 AKE-------------LSKFGIRCNCVLPGFITTPMTDK----VPEKVIDKITSiiPLGRMGEPAEVADACAFLASDDSR 240
Cdd:PRK12428 140 SKEalilwtmrqaqpwFGARGIRVNCVAPGPVFTPILGDfrsmLGQERVDSDAK--RMGRPATADEQAAVLVFLCSDAAR 217

                        250
                 ....*....|...
gi 148540050 241 YITGVSIEVAGGL 253
Cdd:PRK12428 218 WINGVNLPVDGGL 230
PRK08264 PRK08264
SDR family oxidoreductase;
13-230 3.01e-15

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 72.61  E-value: 3.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGAS-VVVADRNEESANqtlELLPREHrgqehmALGVDVSSKDSVEKLVTSIQrryfqPPS 91
Cdd:PRK08264  10 LVTGANRGIGRAFVEQLLARGAAkVYAAARDPESVT---DLGPRVV------PLQLDVTDPASVAAAAEAAS-----DVT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQ-DEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVG--KVGNIGqvNYASSKA 168
Cdd:PRK08264  76 ILVNNAGIFRtGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGG--GAIVNVLSVLSwvNFPNLG--TYSASKA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPekvIDKITsiiplgrmgePAEVADA 230
Cdd:PRK08264 152 AAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGLD---APKAS----------PADVARQ 200
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 13-194 1.12e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 71.87  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPrehrgqeHMALGV--DVSSKDSVEKLVTSIQRRyFQPP 90
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHP-------DRALARllDVTDFDAIDAVVADAEAT-FGPI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKAGV 170
Cdd:PRK06180  80 DVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRR--GHIVNITSMGGLITMPGIGYYCGSKFAL 157

                        170       180
                 ....*....|....*....|....
gi 148540050 171 QGLTRTAAKELSKFGIRCNCVLPG 194
Cdd:PRK06180 158 EGISESLAKEVAPFGIHVTAVEPG 181
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 1-194 2.54e-14

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 72.26  E-value: 2.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   1 MAASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprehrGQEHMALGVDVSSKDSVEKLVT 80
Cdd:COG3347  417 MPKPKPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAEL-----GGGYGADAVDATDVDVTAEAAV 491

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  81 SIQRRYFqppsvCV----------NAAGITQDEFILKMEEDDFDKViKVNLKGTFLVTQAVSKALVSAGSAkGSIITVGS 150
Cdd:COG3347  492 AAAFGFA-----GLdiggsdigvaNAGIASSSPEEETRLSFWLNNF-AHLSTGQFLVARAAFQGTGGQGLG-GSSVFAVS 564

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148540050 151 IVGKVGNIGQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPG 194
Cdd:COG3347  565 KNAAAAAYGAAAAATAKAAAQHLLRALAAEGGANGINANRVNPD 608
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 13-255 3.78e-14

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 69.92  E-value: 3.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGS--GIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLvtsiqrryfqpp 90
Cdd:cd05372    5 LITGIANdrSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLA--ERLGESALVLPCDVSNDEEIKEL------------ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 svcvnAAGITQD----EFILK----MEEDDFDK-VIKVNLKGtFLVTQ--------AVSKALVSAGSAKGSIITVgSIVG 153
Cdd:cd05372   71 -----FAEVKKDwgklDGLVHsiafAPKVQLKGpFLDTSRKG-FLKALdisayslvSLAKAALPIMNPGGSIVTL-SYLG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 154 KVGNIGQVNY-ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLGRMGEPAEVADA 230
Cdd:cd05372  144 SERVVPGYNVmGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAASGITgfDKMLEYSEQRAPLGRNVTAEEVGNT 223

                        250       260
                 ....*....|....*....|....*
gi 148540050 231 CAFLASDDSRYITGVSIEVAGGLFI 255
Cdd:cd05372  224 AAFLLSDLSSGITGEIIYVDGGYHI 248
PRK05866 PRK05866
SDR family oxidoreductase;
13-200 4.91e-14

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 70.16  E-value: 4.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPRehRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK05866  44 LLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITR--AGGDAMAVPCDLSDLDAVDALVADVEKR-IGGVDI 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITqdefILKMEED------DFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVN-YAS 165
Cdd:PRK05866 121 LINNAGRS----IRRPLAEsldrwhDVERTMVLNYYAPLRLIRGLAPGMLERGD--GHIINVATWGVLSEASPLFSvYNA 194

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPM 200
Cdd:PRK05866 195 SKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229
PRK07201 PRK07201
SDR family oxidoreductase;
6-217 5.56e-14

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 71.14  E-value: 5.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLpREHRGQEHmALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK07201 368 PLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEI-RAKGGTAH-AYTCDLTDSAAVDHTVKDILAE 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 yFQPPSVCVNAAG--------ITQDEFilkmeeDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIvGKVGN 157
Cdd:PRK07201 446 -HGHVDYLVNNAGrsirrsveNSTDRF------HDYERTMAVNYFGAVRLILGLLPHMRERR--FGHVVNVSSI-GVQTN 515

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148540050 158 IGQVN-YASSKAGVQGLTRTAAKELSKFGIR-CNCVLPgFITTPMTdkVPEKVIDKITSIIP 217
Cdd:PRK07201 516 APRFSaYVASKAALDAFSDVAASETLSDGITfTTIHMP-LVRTPMI--APTKRYNNVPTISP 574
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 10-210 6.05e-14

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 69.41  E-value: 6.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASV--VVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRYf 87
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASDPSKRfkVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERH- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  88 qpPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSK 167
Cdd:cd09806   80 --VDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGS--GRILVTSSVGGLQGLPFNDVYCASK 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVID 210
Cdd:cd09806  156 FALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEE 198
PRK06101 PRK06101
SDR family oxidoreductase;
13-203 7.16e-14

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 69.13  E-value: 7.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEEsanqTLELLPREHRGQEHMALgvDVSSKDSVEKLVTSIQrryFQPPSV 92
Cdd:PRK06101   5 LITGATSGIGKQLALDYAKQGWQVIACGRNQS----VLDELHTQSANIFTLAF--DVTDHPGTKAALSQLP---FIPELW 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGItqdEFIL--KMEEDDFDKVIKVNLKGTFLVTQAVSKALvsagSAKGSIITVGSIVGKVGNIGQVNYASSKAGV 170
Cdd:PRK06101  76 IFNAGDC---EYMDdgKVDATLMARVFNVNVLGVANCIEGIQPHL----SCGHRVVIVGSIASELALPRAEAYGASKAAV 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 148540050 171 QGLTRTAAKELSKFGIRCNCVLPGFITTPMTDK 203
Cdd:PRK06101 149 AYFARTLQLDLRPKGIEVVTVFPGFVATPLTDK 181
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 13-252 1.69e-13

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 68.13  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTG--GGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrgQEHMALGVDVSSKDSVEKLVTSIQRRYfqpp 90
Cdd:COG0623    9 LITGvaNDRSIAWGIAKALHEEGAELAFTYQGEALKKRVEPLAEEL---GSALVLPCDVTDDEQIDALFDEIKEKW---- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 svcvnaagitqdefilkmeeDDFDKVI-------KVNLKGTFLVT--QAVSKAL-VSAGS----AK---------GSIIT 147
Cdd:COG0623   82 --------------------GKLDFLVhsiafapKEELGGRFLDTsrEGFLLAMdISAYSlvalAKaaeplmnegGSIVT 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 148 VgSIVGkvgniGQV---NY---ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLG 219
Cdd:COG0623  142 L-TYLG-----AERvvpNYnvmGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKTLAASGIPgfDKLLDYAEERAPLG 215

                        250       260       270
                 ....*....|....*....|....*....|...
gi 148540050 220 RMGEPAEVADACAFLASDDSRYITGVSIEVAGG 252
Cdd:COG0623  216 RNVTIEEVGNAAAFLLSDLASGITGEIIYVDGG 248
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 13-212 1.77e-13

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 67.82  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGAS-VVVADRNEESANQTLEL-LPREHrgqehmALGVDVSSKDSVEKLVTSIQRryfqpP 90
Cdd:cd05354    7 LVTGANRGIGKAFVESLLAHGAKkVYAAVRDPGSAAHLVAKyGDKVV------PLRLDVTDPESIKAAAAQAKD-----V 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAAGITQDEFIlkMEEDDFDKV---IKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSK 167
Cdd:cd05354   76 DVVINNAGVLKPATL--LEEGALEALkqeMDVNVFGLLRLAQAFAPVLKANG--GGAIVNLNSVASLKNFPAMGTYSASK 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148540050 168 AGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV------PEKVIDKI 212
Cdd:cd05354  152 SAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAggpkesPETVAEAV 202
PRK07102 PRK07102
SDR family oxidoreductase;
13-230 2.42e-13

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 67.64  E-value: 2.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGV-DVSSKDSVEKLVTSIQRRyfqpPS 91
Cdd:PRK07102   5 LIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDL--RARGAVAVSTHElDILDTASHAAFLDSLPAL----PD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQDEfilKMEEDDFD---KVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK07102  79 IVLIAVGTLGDQ---AACEADPAlalREFRTNFEGPIALLTLLANRFEARGS--GTIVGISSVAGDRGRASNYVYGSAKA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148540050 169 GV----QGLTrtaaKELSKFGIRCNCVLPGFITTPMTDKVPEKviDKITSiiplgrmgEPAEVADA 230
Cdd:PRK07102 154 ALtaflSGLR----NRLFKSGVHVLTVKPGFVRTPMTAGLKLP--GPLTA--------QPEEVAKD 205
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 13-252 5.76e-13

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 66.49  E-value: 5.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLellprehRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:PRK06483   6 LITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGL-------RQAGAQCIQADFSTNAGIMAFIDELKQHTDGLRAI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAgITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKGSIITVGSIVGKVGNIGQVNYASSKAGVQG 172
Cdd:PRK06483  79 IHNAS-DWLAEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHAASDIIHITDYVVEKGSDKHIAYAASKAALDN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 173 LTRTAAKELSKfGIRCNCVLPGFITTPMTD--KVPEKVIDKitSIIPLgrmgEP--AEVADACAFLAsdDSRYITGVSIE 248
Cdd:PRK06483 158 MTLSFAAKLAP-EVKVNSIAPALILFNEGDdaAYRQKALAK--SLLKI----EPgeEEIIDLVDYLL--TSCYVTGRSLP 228


                 ....
gi 148540050 249 VAGG 252
Cdd:PRK06483 229 VDGG 232
PRK06139 PRK06139
SDR family oxidoreductase;
3-199 1.22e-12

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 66.28  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   3 ASTRLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSI 82
Cdd:PRK06139   1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEEC--RALGAEVLVVPTDVTDADQVKALATQA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 QrRYFQPPSVCVNAAGITQdefILKMEE---DDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIG 159
Cdd:PRK06139  79 A-SFGGRIDVWVNNVGVGA---VGRFEEtpiEAHEQVIQTNLIGYMRDAHAALPIFKKQGH--GIFINMISLGGFAAQPY 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 148540050 160 QVNYASSKAGVQGLTRTAAKELSKF-GIRCNCVLPGFITTP 199
Cdd:PRK06139 153 AAAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDTP 193
PRK08219 PRK08219
SDR family oxidoreductase;
10-233 1.89e-12

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 64.57  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFAtEGASVVVADRNEESANQTLELLPREHrgqehmALGVDVSSKDSVEKLVTSIQRRyfqp 89
Cdd:PRK08219   4 PTALITGASRGIGAAIARELA-PTHTLLLGGRPAERLDELAAELPGAT------PFPVDLTDPEAIAAAVEQLGRL---- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 pSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsaGSAKGSIITVGSIVGKVGNIGQVNYASSKAG 169
Cdd:PRK08219  73 -DVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPAL---RAAHGHVVFINSGAGLRANPGWGSYAASKFA 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148540050 170 VQGLTrTAAKELSKFGIRCNCVLPGFITTPMTDKV---------PEKVIDkitsiiplgrmgePAEVADACAF 233
Cdd:PRK08219 149 LRALA-DALREEEPGNVRVTSVHPGRTDTDMQRGLvaqeggeydPERYLR-------------PETVAKAVRF 207
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
21-255 5.33e-12

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 63.98  E-value: 5.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  21 IGRAVCQRFATEGASVVVADRNEESANQTLELLPrEHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQPPSV--CVNAAG 98
Cdd:PRK08594  21 IAWGIARSLHNAGAKLVFTYAGERLEKEVRELAD-TLEGQESLLLPCDVTSDEEITACFETIKEEVGVIHGVahCIAFAN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  99 ItqdefilkmeEDDFDKVIKVNLKGtFLVTQ--------AVSKALVSAGSAKGSIITV----GSIVGKVGNIGQVNYASS 166
Cdd:PRK08594 100 K----------EDLRGEFLETSRDG-FLLAQnisaysltAVAREAKKLMTEGGSIVTLtylgGERVVQNYNVMGVAKASL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLtrtaAKELSKFGIRCNCVLPGFITTPMTDKVPE--KVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK08594 169 EASVKYL----ANDLGKDGIRVNAISAGPIRTLSAKGVGGfnSILKEIEERAPLRRTTTQEEVGDTAAFLFSDLSRGVTG 244

                        250
                 ....*....|.
gi 148540050 245 VSIEVAGGLFI 255
Cdd:PRK08594 245 ENIHVDSGYHI 255
PRK08862 PRK08862
SDR family oxidoreductase;
13-193 9.28e-12

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 62.82  E-value: 9.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDvsSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:PRK08862   9 LITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVYSFQLKDF--SQESIRHLFDAIEQQFNRAPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNA----------AGITQDEFILKMEEddfdkvikvnLKGTFLVTQAVSKALVSAGSAKGSIITVGSiVGKVGNIGQVN 162
Cdd:PRK08862  87 LVNNwtssplpslfDEQPSESFIQQLSS----------LASTLFTYGQVAAERMRKRNKKGVIVNVIS-HDDHQDLTGVE 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 148540050 163 yaSSKAGVQGLTRTAAKELSKFGIRCNCVLP 193
Cdd:PRK08862 156 --SSNALVSGFTHSWAKELTPFNIRVGGVVP 184
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 2-196 1.47e-11

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 63.56  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   2 AASTRLISRLTLVTGGGSGIGRAVCQRFATEGA-SVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVT 80
Cdd:cd05274  143 AAAPGGLDGTYLITGGLGGLGLLVARWLAARGArHLVLLSRRGPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLA 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  81 SIQRryFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAvskalvSAGSAKGSIITVGSIVGKVGNIGQ 160
Cdd:cd05274  223 ELAA--GGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHEL------TPDLPLDFFVLFSSVAALLGGAGQ 294

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148540050 161 VNYASSKAGVQGLtrtaAKELSKFGIRCNCVLPGFI 196
Cdd:cd05274  295 AAYAAANAFLDAL----AAQRRRRGLPATSVQWGAW 326
PRK08703 PRK08703
SDR family oxidoreductase;
7-203 2.03e-11

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 61.87  E-value: 2.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPrEHRGQEHMALGVDV--SSKDSVEKLVTSIQR 84
Cdd:PRK08703   4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIV-EAGHPEPFAIRFDLmsAEEKEFEQFAATIAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  85 RYFQPPSVCVNAAGitqdeFILKMEEDDFDKV------IKVNLKGTFLVTQAVSKALVSAGSAkgSIITVGSIVGKVGNI 158
Cdd:PRK08703  83 ATQGKLDGIVHCAG-----YFYALSPLDFQTVaewvnqYRINTVAPMGLTRALFPLLKQSPDA--SVIFVGESHGETPKA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 148540050 159 GQVNYASSKAGVQGLTRTAAKELSKFG-IRCNCVLPGFITTPMTDK 203
Cdd:PRK08703 156 YWGGFGASKAALNYLCKVAADEWERFGnLRANVLVPGPINSPQRIK 201
PRK09291 PRK09291
SDR family oxidoreductase;
13-230 2.50e-11

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 61.94  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVAdrnEESANQTLELlpREhrgqEHMALGVDVSskdsVEKL-VTS---IQRRYFQ 88
Cdd:PRK09291   6 LITGAGSGFGREVALRLARKGHNVIAG---VQIAPQVTAL--RA----EAARRGLALR----VEKLdLTDaidRAQAAEW 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVG--KVGNIGQvnYASS 166
Cdd:PRK09291  73 DVDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARG--KGKVVFTSSMAGliTGPFTGA--YCAS 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGF----------------------------ITTPMTDKVPEKVIDKITSIIP- 217
Cdd:PRK09291 149 KHALEAIAEAMHAELKPFGIQVATVNPGPyltgfndtmaetpkrwydparnftdpedLAFPLEQFDPQEMIDAMVEVIPa 228

                        250
                 ....*....|....*.
gi 148540050 218 ---LGRMGEPAEVADA 230
Cdd:PRK09291 229 dtgLFRNLLPAAIEDM 244
PRK05693 PRK05693
SDR family oxidoreductase;
13-198 3.53e-11

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 61.73  E-value: 3.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESAnqtlellprEHRGQEHM-ALGVDVSSKDSVEKLVTSIQRRYfQPPS 91
Cdd:PRK05693   5 LITGCSSGIGRALADAFKAAGYEVWATARKAEDV---------EALAAAGFtAVQLDVNDGAALARLAEELEAEH-GGLD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsaGSAKGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:PRK05693  75 VLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLL---RRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVH 151

                        170       180
                 ....*....|....*....|....*..
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFITT 198
Cdd:PRK05693 152 ALSDALRLELAPFGVQVMEVQPGAIAS 178
PRK08278 PRK08278
SDR family oxidoreductase;
14-244 4.03e-11

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 61.46  E-value: 4.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  14 VTGGGSGIGRAVCQRFATEGASVVVADRNEE----------SANQTLellprEHRGQEHMALGVDVSSKDSVEKLV-TSI 82
Cdd:PRK08278  11 ITGASRGIGLAIALRAARDGANIVIAAKTAEphpklpgtihTAAEEI-----EAAGGQALPLVGDVRDEDQVAAAVaKAV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  83 QRryFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsAGSAKGSIITVGSIVgkvgNI---- 158
Cdd:PRK08278  86 ER--FGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHL--KKSENPHILTLSPPL----NLdpkw 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 159 --GQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPgfITTPMTDKVpeKVIDKITSIIPLGRmgEPAEVADACAFLAS 236
Cdd:PRK08278 158 faPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP--RTTIATAAV--RNLLGGDEAMRRSR--TPEIMADAAYEILS 231


                 ....*...
gi 148540050 237 DDSRYITG 244
Cdd:PRK08278 232 RPAREFTG 239
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 7-244 9.41e-11

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 60.54  E-value: 9.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEE-SANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEI--EARGGKCIPVRCDHSDDDEVEALFERVARE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YFQPPSVCVNAA-------GITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKGSIItvgSIVGKVGNI 158
Cdd:cd09763   79 QQGRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVII---SSTGGLEYL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 159 GQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDKITSIIP-LGRMGEPAEVADAC-AFLAS 236
Cdd:cd09763  156 FNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEGSWHAKERdAFLNGETTEYSGRCvVALAA 235


                 ....*....
gi 148540050 237 D-DSRYITG 244
Cdd:cd09763  236 DpDLMELSG 244
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 10-238 1.80e-10

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 59.79  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQp 89
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDR- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDEFILKmeEDDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGSIVGKVGNIG---------- 159
Cdd:cd09807   81 LDVLINNAGVMRCPYSKT--EDGFEMQFGVNHLGHFLLTNLLLDLLKK--SAPSRIVNVSSLAHKAGKINfddlnseksy 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 160 --QVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKV--PEKVIDKITSIIPLGRMGEPAEVADACAFLA 235
Cdd:cd09807  157 ntGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHTgiHHLFLSTLLNPLFWPFVKTPREGAQTSIYLA 236


                 ...
gi 148540050 236 SDD 238
Cdd:cd09807  237 LAE 239
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 13-201 2.31e-10

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 59.88  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSS--KDSVEKLVTSIQRryfQPP 90
Cdd:PLN02780  57 LVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTVVVDFSGdiDEGVKRIKETIEG---LDV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAAGITQD--EFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGS---IVGKVGNIGQVnYAS 165
Cdd:PLN02780 134 GVLINNVGVSYPyaRFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLK--RKKGAIINIGSgaaIVIPSDPLYAV-YAA 210

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMT 201
Cdd:PLN02780 211 TKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMA 246
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 13-196 3.05e-10

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 58.61  E-value: 3.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtLELLPREhRGQEHMALGVDVSSKDSVEKLVTSIQRRyFQPPSV 92
Cdd:PRK10538   4 LVTGATAGFGECITRRFIQQGHKVIATGRRQER----LQELKDE-LGDNLYIAQLDVRNRAAIEEMLASLPAE-WRNIDV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQD-EFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:PRK10538  78 LVNNAGLALGlEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERN--HGHIINIGSTAGSWPYAGGNVYGATKAFVR 155

                        170       180
                 ....*....|....*....|....*
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFI 196
Cdd:PRK10538 156 QFSLNLRTDLHGTAVRVTDIEPGLV 180
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
10-200 3.06e-10

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 58.93  E-value: 3.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRneeSANQTLELLPREHRGQ--EHMALGVDVSSKDS-VEKLVTSIQRRY 86
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISR---TENKELTKLAEQYNSNltFHSLDLQDVHELETnFNEILSSIQEDN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 FQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAgSAKGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK06924  79 VSSIHLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDW-KVDKRVINISSGAAKNPYFGWSAYCSS 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148540050 167 KAGVQGLTRTAA--KELSKFGIRCNCVLPGFITTPM 200
Cdd:PRK06924 158 KAGLDMFTQTVAteQEEEEYPVKIVAFSPGVMDTNM 193
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 12-200 4.83e-10

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 57.53  E-value: 4.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  12 TLVTGGGSGIGRAVCQRFATEGASVVVADRNEesanQTLELLPREhRGQehMALGVDVSSKDSVEKLVTSIQrryfqPPS 91
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDA----GALAGLAAE-VGA--LARPADVAAELEVWALAQELG-----PLD 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAvSKALVSAGsakGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:cd11730   69 LLVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKH-ALALLAAG---ARLVFLGAYPELVMLPGLSAYAAAKAALE 144

                        170       180
                 ....*....|....*....|....*....
gi 148540050 172 GLTRTAAKELSkfGIRCNCVLPGFITTPM 200
Cdd:cd11730  145 AYVEVARKEVR--GLRLTLVRPPAVDTGL 171
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 13-201 9.12e-10

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 57.78  E-value: 9.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRF-----ATEGASVVVADRN----EESANQTLELLPREHRGQEHmaLGVDVSSKDSVEKLVTSIQ 83
Cdd:cd08941    5 LVTGANSGLGLAICERLlaeddENPELTLILACRNlqraEAACRALLASHPDARVVFDY--VLVDLSNMVSVFAAAKELK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  84 RRYFQPPSVCVNAA-----GI-----------------------TQDEFIL----KMEEDDFDKVIKVNLKGTFLVTQAV 131
Cdd:cd08941   83 KRYPRLDYLYLNAGimpnpGIdwigaikevltnplfavtnptykIQAEGLLsqgdKATEDGLGEVFQTNVFGHYYLIREL 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148540050 132 sKALVSAGSAKGSIITVGSIVGKVGNI---------GQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMT 201
Cdd:cd08941  163 -EPLLCRSDGGSQIIWTSSLNASPKYFslediqhlkGPAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTTNLT 240
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 10-194 9.38e-10

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 57.61  E-value: 9.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQP 89
Cdd:cd09809    2 KVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSPL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 PSVCVNAAGITQDefiLKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSagSAKGSIITVGS-------IVGKVGNI---- 158
Cdd:cd09809   82 HVLVCNAAVFALP---WTLTEDGLETTFQVNHLGHFYLVQLLEDVLRR--SAPARVIVVSSeshrftdLPDSCGNLdfsl 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 148540050 159 ---------GQVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPG 194
Cdd:cd09809  157 lsppkkkywSMLAYNRAKLCNILFSNELHRRLSPRGITSNSLHPG 201
PRK08340 PRK08340
SDR family oxidoreductase;
13-253 1.16e-09

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 57.12  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREhrGQEHmALGVDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEY--GEVY-AVKADLSDKDDLKNLVKEAWELLGGIDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEFILkmEEDDFDKVIKVNLKGT----FLVTQAVSKALvsAGSAKGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK08340  81 VWNAGNVRCEPCML--HEAGYSDWLEAALLHLvapgYLTTLLIQAWL--EKKMKGVLVYLSSVSVKEPMPPLVLADVTRA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTP-----------MTDKVPEKVIDK-ITSIIPLGRMGEPAEVADACAFLAS 236
Cdd:PRK08340 157 GLVQLAKGVSRTYGGKGIRAYTVLLGSFDTPgarenlariaeERGVSFEETWEReVLERTPLKRTGRWEELGSLIAFLLS 236

                        250
                 ....*....|....*..
gi 148540050 237 DDSRYITGVSIEVAGGL 253
Cdd:PRK08340 237 ENAEYMLGSTIVFDGAM 253
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
13-212 2.04e-09

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 56.91  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPRE-HRGqehmalgvDVSSKDSVEKLvtsiqrryFQPPS 91
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEfVRG--------DLRDPEALAAA--------LAGVD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  92 VCVNAAGITQDefilkmEEDDFDKVIKVNLKGTFLVTQAVSKA----LVSAGSAK-----GSIITVGSIVGKVGnigqvN 162
Cdd:COG0451   67 AVVHLAAPAGV------GEEDPDETLEVNVEGTLNLLEAARAAgvkrFVYASSSSvygdgEGPIDEDTPLRPVS-----P 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 148540050 163 YASSKAGVQGLTRTAAKElskFGIRCNCVLPGFITTPMTDKVPEKVIDKI 212
Cdd:COG0451  136 YGASKLAAELLARAYARR---YGLPVTILRPGNVYGPGDRGVLPRLIRRA 182
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
167-255 5.71e-09

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 55.33  E-value: 5.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE--KVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITG 244
Cdd:PRK07533 166 KAALESSVRYLAAELGPKGIRVHAISPGPLKTRAASGIDDfdALLEDAAERAPLRRLVDIDDVGAVAAFLASDAARRLTG 245

                         90
                 ....*....|.
gi 148540050 245 VSIEVAGGLFI 255
Cdd:PRK07533 246 NTLYIDGGYHI 256
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
 13-173 1.95e-08

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 54.21  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGA-SVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRyfQPP- 90
Cdd:cd08955  153 LITGGLGGLGLLVAEWLVERGArHLVLTGRRAPSAAARQAIAALEEAGAEVVVLAADVSDRDALAAALAQIRAS--LPPl 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 -SVcVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSK------ALVSagsakgsiitvgSIVGKVGNIGQVNY 163
Cdd:cd08955  231 rGV-IHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTQDlpldffVLFS------------SVASLLGSPGQANY 297

                        170
                 ....*....|
gi 148540050 164 ASSKAGVQGL 173
Cdd:cd08955  298 AAANAFLDAL 307
PRK06182 PRK06182
short chain dehydrogenase; Validated
 9-199 3.23e-08

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 53.04  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEEsanqtlellprehRGQEHMALGV-----DVSSKDSVEKLVTSIQ 83
Cdd:PRK06182   3 KKVALVTGASSGIGKATARRLAAQGYTVYGAARRVD-------------KMEDLASLGVhplslDVTDEASIKAAVDTII 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  84 RRYFQpPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNY 163
Cdd:PRK06182  70 AEEGR-IDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRS--GRIINISSMGGKIYTPLGAWY 146

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148540050 164 ASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTP 199
Cdd:PRK06182 147 HATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTE 182
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 9-199 3.94e-08

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 52.60  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRYfQ 88
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQNIFLHIVDMSDPKQVWEFVEEFKEEG-K 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVCVNAAGITQDEfiLKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKgsIITVGS---IVGK--VGNI----- 158
Cdd:cd09808   80 KLHVLINNAGCMVNK--RELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPR--VITVSSggmLVQKlnTNNLqsert 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 148540050 159 ---GQVNYASSKAGVQGLTRTAAKelSKFGIRCNCVLPGFITTP 199
Cdd:cd09808  156 afdGTMVYAQNKRQQVIMTEQWAK--KHPEIHFSVMHPGWADTP 197
PRK06196 PRK06196
oxidoreductase; Provisional
 7-205 5.12e-08

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 52.76  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLellpREHRGQEHMALgvDVSSKDSVEKLVTSIQRRY 86
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREAL----AGIDGVEVVML--DLADLESVRAFAERFLDSG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  87 fQPPSVCVNAAGITQDEfiLKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKgsIITVGSIVGKVGNI--GQVNYA 164
Cdd:PRK06196  98 -RRIDILINNAGVMACP--ETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGAR--VVALSSAGHRRSPIrwDDPHFT 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148540050 165 S--SKAGVQGLTRTA----AKELSK----FGIRCNCVLPGFITTPMTDKVP 205
Cdd:PRK06196 173 RgyDKWLAYGQSKTAnalfAVHLDKlgkdQGVRAFSVHPGGILTPLQRHLP 223
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 13-200 1.15e-07

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 51.34  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPrehrGQEHMALGvDVSSKDSVEKL---VTSIQRRyfqp 89
Cdd:cd08951   11 FITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACP----GAAGVLIG-DLSSLAETRKLadqVNAIGRF---- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  90 pSVCVNAAGITQDEFILKMEEDDfDKVIKVNLKGTFLVTQAVS--KALV--SAGSAKGSIITVGSIV-GKVGNIGQVNYA 164
Cdd:cd08951   82 -DAVIHNAGILSGPNRKTPDTGI-PAMVAVNVLAPYVLTALIRrpKRLIylSSGMHRGGNASLDDIDwFNRGENDSPAYS 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148540050 165 SSKAGVQGLTRTAAKELSKfgIRCNCVLPGFITTPM 200
Cdd:cd08951  160 DSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPTKM 193
PRK08017 PRK08017
SDR family oxidoreductase;
13-211 2.32e-07

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 50.47  E-value: 2.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELlprehrGQEHMALgvDVSSKDSVEKLVTSIQR----RYFQ 88
Cdd:PRK08017   6 LITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMNSL------GFTGILL--DLDDPESVERAADEVIAltdnRLYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 ppsvCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGsaKGSIITVGSIVGKVGNIGQVNYASSKA 168
Cdd:PRK08017  78 ----LFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHG--EGRIVMTSSVMGLISTPGRGAYAASKY 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 148540050 169 GVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVIDK 211
Cdd:PRK08017 152 ALEAWSDALRMELRHSGIKVSLIEPGPIRTRFTDNVNQTQSDK 194
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 13-133 2.78e-07

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 50.31  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGAS-VVVADRNEESANQ-TLELLPREHRGQEHMALGvDVSSKDSVEKLVTsiqrryFQPP 90
Cdd:cd05237    6 LVTGGAGSIGSELVRQILKFGPKkLIVFDRDENKLHElVRELRSRFPHDKLRFIIG-DVRDKERLRRAFK------ERGP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 148540050  91 SVCVNAAGITQdefiLKMEEDDFDKVIKVNLKGTFLVTQAVSK 133
Cdd:cd05237   79 DIVFHAAALKH----VPSMEDNPEEAIKTNVLGTKNVIDAAIE 117
PRK08251 PRK08251
SDR family oxidoreductase;
13-205 5.68e-07

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 49.16  E-value: 5.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRYFQPPSV 92
Cdd:PRK08251   6 LITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELGGLDRV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAaGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVN-YASSKAGVQ 171
Cdd:PRK08251  86 IVNA-GIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGS--GHLVLISSVSAVRGLPGVKAaYAASKAGVA 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP 205
Cdd:PRK08251 163 SLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAK 196
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
20-255 8.48e-07

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 48.81  E-value: 8.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  20 GIGRAvCQRFATEGASVVVADRNEESANQTLELLPREhrgqehMALGVDVSSKDSVEKLVTSIQRRYFQPPSVcVNAAGI 99
Cdd:PRK08690  23 GIAKA-CREQGAELAFTYVVDKLEERVRKMAAELDSE------LVFRCDVASDDEINQVFADLGKHWDGLDGL-VHSIGF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 100 TQDEfilKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSA-----KGSIITVgSIVGKVGNIGQVNYAS-SKAGVQGL 173
Cdd:PRK08690  95 APKE---ALSGDFLDSISREAFNTAHEISAYSLPALAKAARPmmrgrNSAIVAL-SYLGAVRAIPNYNVMGmAKASLEAG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 174 TRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE--KVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAG 251
Cdd:PRK08690 171 IRFTAACLGKEGIRCNGISAGPIKTLAASGIADfgKLLGHVAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDG 250


                 ....
gi 148540050 252 GLFI 255
Cdd:PRK08690 251 GYSI 254
PRK05854 PRK05854
SDR family oxidoreductase;
7-99 9.87e-07

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 48.91  E-value: 9.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIqRRY 86
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVPDAKLSLRALDLSSLASVAALGEQL-RAE 90

                         90
                 ....*....|...
gi 148540050  87 FQPPSVCVNAAGI 99
Cdd:PRK05854  91 GRPIHLLINNAGV 103
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
13-130 1.35e-06

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 48.20  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEesanqtlellprehrgqehmalgVDVSSKDSVEKLVTSIQrryfqpPSV 92
Cdd:COG1091    3 LVTGANGQLGRALVRLLAERGYEVVALDRSE-----------------------LDITDPEAVAALLEEVR------PDV 53

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 148540050  93 CVNAAGITQ-DEfilkmEEDDFDKVIKVNLKGTFLVTQA 130
Cdd:COG1091   54 VINAAAYTAvDK-----AESEPELAYAVNATGPANLAEA 87
PRK06482 PRK06482
SDR family oxidoreductase;
9-194 2.29e-06

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 47.42  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   9 SRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEesanQTLELLPREHRGQEHMALgVDVSSKDSVEKLVtsiQRRYFQ 88
Cdd:PRK06482   2 SKTWFITGASSGFGRGMTERLLARGDRVAATVRRP----DALDDLKARYGDRLWVLQ-LDVTDSAAVRAVV---DRAFAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PP--SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYASS 166
Cdd:PRK06482  74 LGriDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGG--GRIVQVSSEGGQIAYPGFSLYHAT 151

                        170       180
                 ....*....|....*....|....*...
gi 148540050 167 KAGVQGLTRTAAKELSKFGIRCNCVLPG 194
Cdd:PRK06482 152 KWGIEGFVEAVAQEVAPFGIEFTIVEPG 179
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 14-130 2.37e-06

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 47.44  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  14 VTGGGSGIGRAVCQRFATEGASVVVADRNEE----------SANQTLELLprehrGQEHMALGVDVSSKDSVEKLVTSIQ 83
Cdd:cd09762    8 ITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgtiyTAAEEIEAA-----GGKALPCIVDIRDEDQVRAAVEKAV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148540050  84 RRyFQPPSVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQA 130
Cdd:cd09762   83 EK-FGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKA 128
PRK07806 PRK07806
SDR family oxidoreductase;
7-98 2.71e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 47.02  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   7 LISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRN-EESANQTLELLprEHRGQEHMALGVDVSSKDSVEKLVTSIQRR 85
Cdd:PRK07806   4 LPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkAPRANKVVAEI--EAAGGRASAVGADLTDEESVAALMDTAREE 81

                         90
                 ....*....|...
gi 148540050  86 YFQPPSVCVNAAG 98
Cdd:PRK07806  82 FGGLDALVLNASG 94
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 13-124 4.39e-06

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 46.85  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESanqtlellprehrgqehmALGVDVSSKDSVEKLVTSIQrryfqpPSV 92
Cdd:cd05254    3 LITGATGMLGRALVRLLKERGYEVIGTGRSRAS------------------LFKLDLTDPDAVEEAIRDYK------PDV 58

                         90       100       110
                 ....*....|....*....|....*....|...
gi 148540050  93 CVNAAGIT-QDEFilkmeEDDFDKVIKVNLKGT 124
Cdd:cd05254   59 IINCAAYTrVDKC-----ESDPELAYRVNVLAP 86
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
132-255 7.06e-06

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 45.86  E-value: 7.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 132 SKALVSAGsakGSIITVgSIVGKVGNIGQVNYAS-SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE--KV 208
Cdd:PRK07370 133 AKPLMSEG---GSIVTL-TYLGGVRAIPNYNVMGvAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLASSAVGGilDM 208

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148540050 209 IDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAGGLFI 255
Cdd:PRK07370 209 IHHVEEKAPLRRTVTQTEVGNTAAFLLSDLASGITGQTIYVDAGYCI 255
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 10-86 9.70e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 45.79  E-value: 9.70e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148540050  10 RLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEKLVTSIQRRY 86
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASVRAAADALRAAY 93
PRK06720 PRK06720
hypothetical protein; Provisional
 6-51 1.44e-05

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 44.19  E-value: 1.44e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 148540050   6 RLISRLTLVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLE 51
Cdd:PRK06720  13 KLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVE 58
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 12-116 2.01e-05

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 45.24  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  12 TLVTGGGSGIGRAVCQRFATEGA-SVVVADRNEESANQTLELLprehrgQEHMALGV-------DVSSKDSVEKLVTSIQ 83
Cdd:cd08952  233 VLVTGGTGALGAHVARWLARRGAeHLVLTSRRGPDAPGAAELV------AELTALGArvtvaacDVADRDALAALLAALP 306

                         90       100       110
                 ....*....|....*....|....*....|...
gi 148540050  84 RRYfqPPSVCVNAAGITQDEFILKMEEDDFDKV 116
Cdd:cd08952  307 AGH--PLTAVVHAAGVLDDGPLDDLTPERLAEV 337
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 13-153 3.41e-05

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 44.05  E-value: 3.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGA-SVVVADRNEESANQTLELLPREHrgQEHMALGVDVSSKDSVEKLVTSIqRRYFQPPS 91
Cdd:cd09810    5 VITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGMPK--DSYSVLHCDLASLDSVRQFVDNF-RRTGRPLD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148540050  92 VCVNAAGItqdEFILKME----EDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKGSIITVGSIVG 153
Cdd:cd09810   82 ALVCNAAV---YLPTAKEprftADGFELTVGVNHLGHFLLTNLLLEDLQRSENASPRIVIVGSITH 144
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 17-200 4.67e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 43.26  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  17 GGSG-IGRAVCQRFATEgASVVVADRNeesanqtlellprehRGQEHmalgVDVSSKDSVEKLvtsiqrrYFQPPSV--C 93
Cdd:PRK07578   7 GASGtIGRAVVAELSKR-HEVITAGRS---------------SGDVQ----VDITDPASIRAL-------FEKVGKVdaV 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  94 VNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALvsagSAKGSIITVGSIVGKVGNIGQVNYASSKAGVQGL 173
Cdd:PRK07578  60 VSAAGKVHFAPLAEMTDEDFNVGLQSKLMGQVNLVLIGQHYL----NDGGSFTLTSGILSDEPIPGGASAATVNGALEGF 135

                        170       180
                 ....*....|....*....|....*..
gi 148540050 174 TRTAAKELSKfGIRCNCVLPGFITTPM 200
Cdd:PRK07578 136 VKAAALELPR-GIRINVVSPTVLTESL 161
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 13-160 7.72e-05

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 42.67  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGqehmalgvDVSSKDSVEKLVTSIQrryfqpPSV 92
Cdd:pfam01370   2 LVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLRFVEG--------DLTDRDALEKLLADVR------PDA 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148540050   93 CVNAAGITQDEFilkmEEDDFDKVIKVNLKGTFLVTQAVSKA----LVSAGSAkgsiitvgSIVGKVGNIGQ 160
Cdd:pfam01370  68 VIHLAAVGGVGA----SIEDPEDFIEANVLGTLNLLEAARKAgvkrFLFASSS--------EVYGDGAEIPQ 127
PRK09009 PRK09009
SDR family oxidoreductase;
13-237 1.15e-04

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 42.36  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATE--GASVVVADRNEESANQTLELLprEHRgqehmalgVDVSSKDSVEKLvtsiqRRYFQPP 90
Cdd:PRK09009   4 LIVGGSGGIGKAMVKQLLERypDATVHATYRHHKPDFQHDNVQ--WHA--------LDVTDEAEIKQL-----SEQFTQL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  91 SVCVNAAGI--TQD---EFILKMEEDD-FDKVIKVNLKGTFLVTQAVSKALVSAGSAKGSIITvgsivGKVGNI------ 158
Cdd:PRK09009  69 DWLINCVGMlhTQDkgpEKSLQALDADfFLQNITLNTLPSLLLAKHFTPKLKQSESAKFAVIS-----AKVGSIsdnrlg 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 159 GQVNYASSKAGVQGLTRTAAKELSKFGIRCnCVL---PGFITTPMT---------DKV--PEKVIDKITSIIplgrmgEP 224
Cdd:PRK09009 144 GWYSYRASKAALNMFLKTLSIEWQRSLKHG-VVLalhPGTTDTALSkpfqqnvpkGKLftPEYVAQCLLGII------AN 216

                        250
                 ....*....|...
gi 148540050 225 AEVADACAFLASD 237
Cdd:PRK09009 217 ATPAQSGSFLAYD 229
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 11-210 1.56e-04

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 41.82  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   11 LTLVTGGGSGIGRAVCQRFA----TEGASVVVADRNEESANQTLELLPREHRGQEHMALGVDVSSKDSVEK----LVTSI 82
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAkclkSPGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEQllkaLRELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   83 QRRYFQPPSVcVNAAGITQDEFILKMEEDDFDKVIK---VNLKGTFLVTQAVSKALVSAGSAKGSIITVGSIVGKVGNIG 159
Cdd:TIGR01500  82 RPKGLQRLLL-INNAGTLGDVSKGFVDLSDSTQVQNywaLNLTSMLCLTSSVLKAFKDSPGLNRTVVNISSLCAIQPFKG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 148540050  160 QVNYASSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPEKVID 210
Cdd:TIGR01500 161 WALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQVREESVD 211
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
13-206 5.46e-04

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 40.46  E-value: 5.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEG-ASVVVADRNEEsanqtlellPREHRGQEHM----ALGVDVSSKDSV--EKLVTSIQRR 85
Cdd:PRK07904  12 LLLGGTSEIGLAICERYLKNApARVVLAALPDD---------PRRDAAVAQMkaagASSVEVIDFDALdtDSHPKVIDAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  86 YFQPP-SVCVNAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSakGSIITVGSIVGKVGNIGQVNYA 164
Cdd:PRK07904  83 FAGGDvDVAIVAFGLLGDAEELWQNQRKAVQIAEINYTAAVSVGVLLGEKMRAQGF--GQIIAMSSVAGERVRRSNFVYG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 148540050 165 SSKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE 206
Cdd:PRK07904 161 STKAGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMSAHAKE 202
SDR_a8 cd05242
atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. ...
 12-100 6.40e-04

atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187553 [Multi-domain]  Cd Length: 296  Bit Score: 40.29  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  12 TLVTGGGSG-IGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMAL-GVDV-------------------- 69
Cdd:cd05242    1 KIVITGGTGfIGRALTRRLTAAGHEVVVLSRRPGKAEGLAEVITWDGLSLGPWELpGADAvinlagepiacrrwteankk 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 148540050  70 ---SSK-DSVEKLVTSIQRRYfQPPSVCVNAAGIT 100
Cdd:cd05242   81 eilSSRiESTRVLVEAIANAP-APPKVLISASAVG 114
PRK07984 PRK07984
enoyl-ACP reductase FabI;
166-255 7.30e-04

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 39.88  E-value: 7.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE--KVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYIT 243
Cdd:PRK07984 162 AKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDfrKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGIS 241

                         90
                 ....*....|..
gi 148540050 244 GVSIEVAGGLFI 255
Cdd:PRK07984 242 GEVVHVDGGFSI 253
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
 164-253 7.71e-04

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 40.14  E-value: 7.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 164 ASSKAGVQGLTRTAAKELS-KFGIRCNCVLPGfittPMTDKVP------EKVIDKITSIIPLGRMGEPAEVADACAFLAS 236
Cdd:PLN02730 194 SSAKAALESDTRVLAFEAGrKYKIRVNTISAG----PLGSRAAkaigfiDDMIEYSYANAPLQKELTADEVGNAAAFLAS 269

                         90
                 ....*....|....*..
gi 148540050 237 DDSRYITGVSIEVAGGL 253
Cdd:PLN02730 270 PLASAITGATIYVDNGL 286
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
166-252 1.12e-03

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 39.54  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 166 SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVP--EKVIDKITSIIPLG-RMGEPAEVADACAFLASDDSRYI 242
Cdd:PRK07889 161 AKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKAIPgfELLEEGWDERAPLGwDVKDPTPVARAVVALLSDWFPAT 240

                         90
                 ....*....|
gi 148540050 243 TGVSIEVAGG 252
Cdd:PRK07889 241 TGEIVHVDGG 250
PRK05599 PRK05599
SDR family oxidoreductase;
13-214 1.87e-03

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 38.71  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATeGASVVVADRNEESANQTLELLPREHRGQEHMaLGVDVSSKDSVEKLVTSIQRrYFQPPSV 92
Cdd:PRK05599   4 LILGGTSDIAGEIATLLCH-GEDVVLAARRPEAAQGLASDLRQRGATSVHV-LSFDAQDLDTHRELVKQTQE-LAGEISL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  93 CVNAAGITQDEfiLKMEEDDFDKVIKVNLKGTFLVTQ-AVSKALVSAGSAKGSIITVGSIVGKVGNIGQVNYASSKAGVQ 171
Cdd:PRK05599  81 AVVAFGILGDQ--ERAETDEAHAVEIATVDYTAQVSMlTVLADELRAQTAPAAIVAFSSIAGWRARRANYVYGSTKAGLD 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148540050 172 GLTRTAAKELSKFGIRCNCVLPGFITTPMTD------------KVPEKVIDKITS 214
Cdd:PRK05599 159 AFCQGLADSLHGSHVRLIIARPGFVIGSMTTgmkpapmsvyprDVAAAVVSAITS 213
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
27-252 1.88e-03

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 38.55  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  27 QRFATEGASVVVADRNEESANQTLELLPREHRGQEhmalgVDVSSKDSVEKLVTSIQRRYFQPPSVcVNAagitqdefIL 106
Cdd:PRK06079  27 QAIKDQGATVIYTYQNDRMKKSLQKLVDEEDLLVE-----CDVASDESIERAFATIKERVGKIDGI-VHA--------IA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 107 KMEEDDFD-KVIKVNLKGtFLVTQ--------AVSKALVSAGSAKGSIITVgSIVGKVGNIGQVNYAS-SKAGVQGLTRT 176
Cdd:PRK06079  93 YAKKEELGgNVTDTSRDG-YALAQdisaysliAVAKYARPLLNPGASIVTL-TYFGSERAIPNYNVMGiAKAALESSVRY 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148540050 177 AAKELSKFGIRCNCVLPGFITTPMTDKVPE--KVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAGG 252
Cdd:PRK06079 171 LARDLGKKGIRVNAISAGAVKTLAVTGIKGhkDLLKESDSRTVDGVGVTIEEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
 13-175 1.91e-03

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 38.97  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGA--SVVVADRNeeSANQTLELLPREHRGQEHMA--LGVDVSSKDSVEKlvtsIQRRYFQ 88
Cdd:cd08954  222 LITGGSGGLGLEILKWLVKRGAveNIIILSRS--GMKWELELLIREWKSQNIKFhfVSVDVSDVSSLEK----AINLILN 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  89 PPSVcVNAAGITQDEFILKmeeddfDKVIKVNLKGTFlvtqavskalVSAGSAK--GSI----------------ITVGS 150
Cdd:cd08954  296 APKI-GPIGGIFHLAFVLI------DKVLEIDTESLF----------ISVNKAKvmGAInlhnqsikrcwkldyfVLFSS 358

                        170       180
                 ....*....|....*....|....*
gi 148540050 151 IVGKVGNIGQVNYASSKAGVQGLTR 175
Cdd:cd08954  359 VSSIRGSAGQCNYVCANSVLDSLSR 383
PLN00015 PLN00015
protochlorophyllide reductase
 13-161 2.00e-03

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 38.92  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGA-SVVVADRNEESANQTLELLPREHRGQEHMALgvDVSSKDSVEKLVTSIqRRYFQPPS 91
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKwHVVMACRDFLKAERAAKSAGMPKDSYTVMHL--DLASLDSVRQFVDNF-RRSGRPLD 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148540050  92 VCV-NAAGITQDEFILKMEEDDFDKVIKVNLKGTFLVTQAVSKALVSAGSAKGSIITVGSIVGKVGNI-GQV 161
Cdd:PLN00015  78 VLVcNAAVYLPTAKEPTFTADGFELSVGTNHLGHFLLSRLLLDDLKKSDYPSKRLIIVGSITGNTNTLaGNV 149
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 13-48 2.55e-03

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 37.90  E-value: 2.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 148540050  13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQ 48
Cdd:COG0702    3 LVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAA 38
yfcH TIGR01777
TIGR01777 family protein; This model represents a clade of proteins of unknown function ...
 13-113 3.39e-03

TIGR01777 family protein; This model represents a clade of proteins of unknown function including the E. coli yfcH protein. [Hypothetical proteins, Conserved]


Pssm-ID: 273800 [Multi-domain]  Cd Length: 291  Bit Score: 38.00  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   13 LVTGGGSGIGRAVCQRFATEGASVVVADRNEESANQTLELLPREHRGQEHMAL-GVDV---------------------- 69
Cdd:TIGR01777   2 LITGGTGFIGRALTQRLTKRGHEVTILTRSPPPGANTKWEGYKPWAGEDADSLeGADAvinlagepiadkrwteerkqei 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 148540050   70 --SSKDSVEKLVTSIQRRYfQPPSVCVNAAGI----TQDEFILKMEE----DDF 113
Cdd:TIGR01777  82 rdSRIDTTRLLVEAIAAAE-QKPKVFISASAVgyygPSEDREYTEEDspagDDF 134
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
130-252 5.10e-03

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 37.49  E-value: 5.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050 130 AVSKALVSAGSAKGSIITVgSIVGKVGNIGQVNYAS-SKAGVQGLTRTAAKELSKFGIRCNCVLPGFITTPMTDKVPE-- 206
Cdd:PRK06997 126 ALAKAALPMLSDDASLLTL-SYLGAERVVPNYNTMGlAKASLEASVRYLAVSLGPKGIRANGISAGPIKTLAASGIKDfg 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 148540050 207 KVIDKITSIIPLGRMGEPAEVADACAFLASDDSRYITGVSIEVAGG 252
Cdd:PRK06997 205 KILDFVESNAPLRRNVTIEEVGNVAAFLLSDLASGVTGEITHVDSG 250
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
 13-136 6.06e-03

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 37.35  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148540050   13 LVTGGGSGIGRAVCQRFATEGA--SVVVADRNEESanQTLELLPREHRGQEHMalgVDVSSKDSVEKLVTSIqrryfqpp 90
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGElkEVRVFDLRESP--ELLEDFSKSNVIKYIQ---GDVTDKDDLDNALEGV-------- 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 148540050   91 SVCVNAAGITQdefilKMEEDDFDKVIKVNLKGTFLVTQAVSKALV 136
Cdd:pfam01073  68 DVVIHTASAVD-----VFGKYTFDEIMKVNVKGTQNVLEACVKAGV 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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