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Conserved domains on  [gi|15239327|ref|NP_196225|]
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NAD(P)-binding Rossmann-fold superfamily protein [Arabidopsis thaliana]

Protein Classification

tropinone reductase I/II( domain architecture ID 10143184)

tropinone reductase I/II catalyzes the stereospecific reduction of tropinone to tropine/pseudotropine respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 6-256 7.51e-154

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: 428.41  E-value: 7.51e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   6 RWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSA 85
Cdd:cd05329   1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  86 FSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATK 165
Cdd:cd05329  81 FGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 166 GALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQ 245
Cdd:cd05329 161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQ 240

                       250
                ....*....|.
gi 15239327 246 VISVDGGFTVN 256
Cdd:cd05329 241 IIAVDGGLTAN 251
 
Name Accession Description Interval E-value
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 6-256 7.51e-154

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: 428.41  E-value: 7.51e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   6 RWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSA 85
Cdd:cd05329   1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  86 FSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATK 165
Cdd:cd05329  81 FGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 166 GALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQ 245
Cdd:cd05329 161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQ 240

                       250
                ....*....|.
gi 15239327 246 VISVDGGFTVN 256
Cdd:cd05329 241 IIAVDGGLTAN 251
PRK09242 PRK09242
SDR family oxidoreductase;
3-258 2.28e-116

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 334.02  E-value: 2.28e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    3 TDKRWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKA--NGLVVSGSVCDASVRDQREKLIq 80
Cdd:PRK09242   1 TQHRWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEefPEREVHGLAADVSDDEDRRAIL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   81 EASSAFSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSI 160
Cdd:PRK09242  80 DWVEDHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  161 YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:PRK09242 160 YGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPAAS 239

                        250
                 ....*....|....*...
gi 15239327  241 YITGQVISVDGGFTVNGF 258
Cdd:PRK09242 240 YITGQCIAVDGGFLRYGF 257
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 8-255 2.03e-95

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: 280.52  E-value: 2.03e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:COG1028  82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVI 247
Cdd:COG1028 162 VVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVL 241


                ....*...
gi 15239327 248 SVDGGFTV 255
Cdd:COG1028 242 AVDGGLTA 249
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 21-254 5.05e-68

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: 210.36  E-value: 5.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    21 RGIGRAVVEELAKFGAKVHTCSRNqEELNACLNDWKA--NGLVVsgsVCDASVRDQREKLIQEASSAFsGKLNILINNVG 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLN-EALAKRVEELAEelGAAVL---PCDVTDEEQVEALVAAAVEKF-GRLDILVNNAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    99 --TNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLVHLSSGSIYGATKGALNQLTRNLA 176
Cdd:pfam13561  81 faPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGG--SIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239327   177 CEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVDGGFT 254
Cdd:pfam13561 159 VELGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGYT 236
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 12-256 5.66e-47

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 156.84  E-value: 5.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLN 91
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETAKEINQAGGKAVAYKLDVSDKDQVFSAIDQAAEKF-GGFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYGATKGALNQ 170
Cdd:TIGR02415  80 VMVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKIINAASIAGHEGNPILSAYSSTKFAVRG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   171 LTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK---------KEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:TIGR02415 160 LTQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEEtseiagkpiGEGFEEFSSEIALGRPSEPEDVAGLVSFLASEDSDY 239

                         250
                  ....*....|....*
gi 15239327   242 ITGQVISVDGGFTVN 256
Cdd:TIGR02415 240 ITGQSILVDGGMVYN 254
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 12-153 1.19e-09

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: 55.95  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327     12 KTALVTGGTRGIGRAVVEELAKFGA-KVHTCSRN---QEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLSRSgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVE- 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239327     88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLsqiaHPLLKASGVGSIVFISSVAGLV 153
Cdd:smart00822  80 GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNL----HELTADLPLDFFVLFSSIAGVL 141
 
Name Accession Description Interval E-value
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 6-256 7.51e-154

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: 428.41  E-value: 7.51e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   6 RWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSA 85
Cdd:cd05329   1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  86 FSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATK 165
Cdd:cd05329  81 FGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 166 GALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQ 245
Cdd:cd05329 161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQ 240

                       250
                ....*....|.
gi 15239327 246 VISVDGGFTVN 256
Cdd:cd05329 241 IIAVDGGLTAN 251
PRK09242 PRK09242
SDR family oxidoreductase;
3-258 2.28e-116

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 334.02  E-value: 2.28e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    3 TDKRWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKA--NGLVVSGSVCDASVRDQREKLIq 80
Cdd:PRK09242   1 TQHRWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEefPEREVHGLAADVSDDEDRRAIL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   81 EASSAFSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSI 160
Cdd:PRK09242  80 DWVEDHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  161 YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:PRK09242 160 YGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPAAS 239

                        250
                 ....*....|....*...
gi 15239327  241 YITGQVISVDGGFTVNGF 258
Cdd:PRK09242 240 YITGQCIAVDGGFLRYGF 257
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 8-255 2.03e-95

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: 280.52  E-value: 2.03e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:COG1028  82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVI 247
Cdd:COG1028 162 VVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVL 241


                ....*...
gi 15239327 248 SVDGGFTV 255
Cdd:COG1028 242 AVDGGLTA 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 14-250 2.32e-80

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: 241.80  E-value: 2.32e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLnDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLNIL 93
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA-AIEALGGNAVAVQADVSDEEDVEALVEEALEEF-GRLDIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  94 INNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQLTR 173
Cdd:cd05233  79 VNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239327 174 NLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEaVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVD 250
Cdd:cd05233 159 SLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKE-LAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
8-252 3.76e-76

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 231.20  E-value: 3.76e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAF- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVhlssGSI----YGA 163
Cdd:PRK05653  81 GALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVT----GNPgqtnYSA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEfvEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK05653 157 AKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVK--AEILKEIPLGRLGQPEEVANAVAFLASDAASYIT 234


                 ....*....
gi 15239327  244 GQVISVDGG 252
Cdd:PRK05653 235 GQVIPVNGG 243
FabG-like PRK07231
SDR family oxidoreductase;
9-256 2.03e-73

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 224.71  E-value: 2.03e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVsGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGGRAI-AVAADVSDEADVEAAVAAALERF-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVR-KPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVhlSSGSI--YGATK 165
Cdd:PRK07231  81 SVDILVNNAGTTHRnGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLR--PRPGLgwYNASK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  166 GALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLE--KKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK07231 159 GAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGepTPENRAKFLATIPLGRLGTPEDIANAALFLASDEASWIT 238

                        250
                 ....*....|...
gi 15239327  244 GQVISVDGGFTVN 256
Cdd:PRK07231 239 GVTLVVDGGRCVG 251
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-255 7.86e-71

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 217.81  E-value: 7.86e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVH-TCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVvHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK12825  83 -GRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEkkEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQV 246
Cdd:PRK12825 162 GLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIE--EAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQV 239


                 ....*....
gi 15239327  247 ISVDGGFTV 255
Cdd:PRK12825 240 IEVTGGVDV 248
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-255 1.98e-69

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 214.32  E-value: 1.98e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKV--HTcSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVviAY-DINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK05565  82 -GKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFveAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQV 246
Cdd:PRK05565 161 AVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKE--GLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQI 238


                 ....*....
gi 15239327  247 ISVDGGFTV 255
Cdd:PRK05565 239 ITVDGGWTC 247
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 8-256 6.56e-69

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 212.75  E-value: 6.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVH-TCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVViNYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK05557  82 -GGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEkkEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQV 246
Cdd:PRK05557 161 GVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPE--DVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQT 238

                        250
                 ....*....|
gi 15239327  247 ISVDGGFTVN 256
Cdd:PRK05557 239 LHVNGGMVMG 248
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 21-254 5.05e-68

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: 210.36  E-value: 5.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    21 RGIGRAVVEELAKFGAKVHTCSRNqEELNACLNDWKA--NGLVVsgsVCDASVRDQREKLIQEASSAFsGKLNILINNVG 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLN-EALAKRVEELAEelGAAVL---PCDVTDEEQVEALVAAAVEKF-GRLDILVNNAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    99 --TNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLVHLSSGSIYGATKGALNQLTRNLA 176
Cdd:pfam13561  81 faPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGG--SIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239327   177 CEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVDGGFT 254
Cdd:pfam13561 159 VELGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGYT 236
PRK12826 PRK12826
SDR family oxidoreductase;
8-256 5.33e-67

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 208.23  E-value: 5.33e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDF- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSI-YGATKG 166
Cdd:PRK12826  82 GRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVGYPGLAhYAASKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEkKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQV 246
Cdd:PRK12826 162 GLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGD-AQWAEAIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQT 240

                        250
                 ....*....|
gi 15239327  247 ISVDGGFTVN 256
Cdd:PRK12826 241 LPVDGGATLP 250
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 9-255 5.24e-65

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 203.25  E-value: 5.24e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERF-G 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ-IAHPLLKASGVGSIVFISSVAGLVHLSSGSI----YGA 163
Cdd:PRK08213  89 HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQaVAKRSMIPRGYGRIINVASVAGLGGNPPEVMdtiaYNT 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEfvEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK08213 169 SKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERLG--EDLLAHTPLGRLGDDEDLKGAALLLASDASKHIT 246

                        250
                 ....*....|..
gi 15239327  244 GQVISVDGGFTV 255
Cdd:PRK08213 247 GQILAVDGGVSA 258
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 12-252 2.42e-64

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: 200.85  E-value: 2.42e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLN 91
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEF-GPVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ-IAHPLLKAsGVGSIVFISSVAGLVhlssGSI----YGATKG 166
Cdd:cd05333  80 ILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQaVIRAMIKR-RSGRIINISSVVGLI----GNPgqanYAASKA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEfvEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQV 246
Cdd:cd05333 155 GVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVK--EKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQV 232


                ....*.
gi 15239327 247 ISVDGG 252
Cdd:cd05333 233 LHVNGG 238
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 8-255 3.47e-64

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: 201.05  E-value: 3.47e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:cd05347   2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDF- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:cd05347  81 GKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVI 247
Cdd:cd05347 161 VAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQII 240


                ....*...
gi 15239327 248 SVDGGFTV 255
Cdd:cd05347 241 FVDGGWLA 248
PRK06124 PRK06124
SDR family oxidoreductase;
1-255 1.08e-62

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 197.24  E-value: 1.08e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    1 METDKRWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQ 80
Cdd:PRK06124   1 MSILQRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   81 EASsAFSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSI 160
Cdd:PRK06124  81 RID-AEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  161 YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:PRK06124 160 YPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPAVGPWLAQRTPLGRWGRPEEIAGAAVFLASPAAS 239

                        250
                 ....*....|....*
gi 15239327  241 YITGQVISVDGGFTV 255
Cdd:PRK06124 240 YVNGHVLAVDGGYSV 254
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 12-205 6.73e-61

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 190.52  E-value: 6.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLN 91
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERL-GRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQL 171
Cdd:pfam00106  80 ILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGF 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 15239327   172 TRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK 205
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTDMTKELRED 193
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-253 8.28e-61

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 192.97  E-value: 8.28e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    1 METDKRWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDwkANGLVVSGSVCDASVRDQREKLIQ 80
Cdd:PRK12829   1 SAIDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAAR--LPGAKVTATVADVADPAQVERVFD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   81 EASSAFsGKLNILINNVGTNVRKPTVE-YSSEEYAKIMSTNLESAFHLSQIAHPLLKASG-VGSIVFISSVAGLVHLSSG 158
Cdd:PRK12829  79 TAVERF-GGLDVLVNNAGIAGPTGGIDeITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhGGVIIALSSVAGRLGYPGR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  159 SIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKK---------EFVEAVVSRTPLGRVGEPEEVSS 229
Cdd:PRK12829 158 TPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARaqqlgigldEMEQEYLEKISLGRMVEPEDIAA 237

                        250       260
                 ....*....|....*....|....
gi 15239327  230 LVAFLCLPASSYITGQVISVDGGF 253
Cdd:PRK12829 238 TALFLASPAARYITGQAISVDGNV 261
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 11-254 4.48e-59

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: 187.87  E-value: 4.48e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKL 90
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAF-GRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQ 170
Cdd:cd05344  80 DILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 171 LTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK---------KEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:cd05344 160 LVKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEAraekegisvEEAEKEVASQIPLGRVGKPEELAALIAFLASEKASY 239

                       250
                ....*....|...
gi 15239327 242 ITGQVISVDGGFT 254
Cdd:cd05344 240 ITGQAILVDGGLT 252
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 9-254 9.18e-59

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: 186.71  E-value: 9.18e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKV----HTCSRNQEELNACLNDWKANGLVVSGSVCDASvrdQREKLIQEASS 84
Cdd:cd05362   1 LAGKVALVTGASRGIGRAIAKRLARDGASVvvnyASSKAAAEEVVAEIEAAGGKAIAVQADVSDPS---QVARLFDAAEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  85 AFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLVHLSSGSIYGAT 164
Cdd:cd05362  78 AF-GGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGG--RIINISSSLTAAYTPNYGAYAGS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 165 KGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLlEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITG 244
Cdd:cd05362 155 KAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAG-KTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNG 233

                       250
                ....*....|
gi 15239327 245 QVISVDGGFT 254
Cdd:cd05362 234 QVIRANGGYV 243
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 8-255 1.03e-57

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: 184.46  E-value: 1.03e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKV-------HTCSRNQEELNaclndwKANGLVVSGSVCDASVRDQREKLIQ 80
Cdd:cd05352   5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVaiiynsaPRAEEKAEELA------KKYGVKTKAYKCDVSSQESVEKTFK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  81 EASSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLV-----HL 155
Cdd:cd05352  79 QIQKDF-GKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIvnrpqPQ 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 156 SSgsiYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLveTLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLC 235
Cdd:cd05352 158 AA---YNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDL--TDFVDKELRKKWESYIPLKRIALPEELVGAYLYLA 232

                       250       260
                ....*....|....*....|
gi 15239327 236 LPASSYITGQVISVDGGFTV 255
Cdd:cd05352 233 SDASSYTTGSDLIIDGGYTC 252
PRK07814 PRK07814
SDR family oxidoreductase;
6-254 3.20e-55

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 178.43  E-value: 3.20e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    6 RWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANG---LVVsgsVCDASVRDQREKLIQEA 82
Cdd:PRK07814   5 RFRLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGrraHVV---AADLAHPEATAGLAGQA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   83 SSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPL-LKASGVGSIVFISSVAGLVHLSSGSIY 161
Cdd:PRK07814  82 VEAF-GRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLmLEHSGGGSVINISSTMGRLAGRGFAAY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  162 GATKGALNQLTRNLACEWASdNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:PRK07814 161 GTAKAALAHYTRLAALDLCP-RIRVNAIAPGSILTSALEVVAANDELRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSY 239

                        250
                 ....*....|...
gi 15239327  242 ITGQVISVDGGFT 254
Cdd:PRK07814 240 LTGKTLEVDGGLT 252
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 9-252 6.86e-55

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: 177.01  E-value: 6.86e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGL-VVSGSVCDasVRD--QREKLIQEASSA 85
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGgRAHPIQCD--VRDpeAVEAAVDETLKE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  86 FsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHP-LLKASGVGSIVFISS------VAGLVHLssg 158
Cdd:cd05369  79 F-GKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKrLIEAKHGGSILNISAtyaytgSPFQVHS--- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 159 siyGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSL-VETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLP 237
Cdd:cd05369 155 ---AAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEgMERLAPSGKSEKKMIERVPLGRLGTPEEIANLALFLLSD 231

                       250
                ....*....|....*
gi 15239327 238 ASSYITGQVISVDGG 252
Cdd:cd05369 232 AASYINGTTLVVDGG 246
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 5-252 8.63e-55

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: 177.35  E-value: 8.63e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   5 KRWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASS 84
Cdd:cd08936   4 RRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  85 AFSGkLNILINNVGTNVRKPTVEYSSEE-YAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:cd08936  84 LHGG-VDILVSNAAVNPFFGNILDSTEEvWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:cd08936 163 SKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASYIT 242


                ....*....
gi 15239327 244 GQVISVDGG 252
Cdd:cd08936 243 GETVVVGGG 251
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
8-200 2.22e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 175.83  E-value: 2.22e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARF- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:COG0300  81 GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAA 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 15239327 168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVE 200
Cdd:COG0300 161 LEGFSESLRAELAPTGVRVTAVCPGPVDTPFTA 193
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 14-255 2.26e-54

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: 175.62  E-value: 2.26e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  14 ALVTGGTRGIGRAVVEELAKFGAKVH-TCSRNQEELNACLNDWKANG---LVVSGSVCDAsvrDQREKLIQEASSAFsGK 89
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVViNYRKSKDAAAEVAAEIEELGgkaVVVRADVSQP---QDVEEMFAAVKERF-GR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  90 LNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:cd05359  77 LDVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALE 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 170 QLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISV 249
Cdd:cd05359 157 ALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVV 236


                ....*.
gi 15239327 250 DGGFTV 255
Cdd:cd05359 237 DGGLSI 242
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 7-252 2.73e-54

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: 175.75  E-value: 2.73e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   7 WSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEelnACLNdwKANGLVVSGSV----CDASVRDQREKLIQEA 82
Cdd:cd08942   2 FSVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAE---ACAD--AAEELSAYGECiaipADLSSEEGIEALVARV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  83 SSAfSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV----GSIVFISSVAGLVHLSSG 158
Cdd:cd08942  77 AER-SDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIVVSGLE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 159 SI-YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLP 237
Cdd:cd08942 156 NYsYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNDPAALEAEEKSIPLGRWGRPEDMAGLAIMLASR 235

                       250
                ....*....|....*
gi 15239327 238 ASSYITGQVISVDGG 252
Cdd:cd08942 236 AGAYLTGAVIPVDGG 250
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 8-256 3.32e-54

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 175.55  E-value: 3.32e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK12939   4 NLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAAL- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK12939  83 GGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETlLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVI 247
Cdd:PRK12939 163 VIGMTRSLARELGGRGITVNAIAPGLTATEATAY-VPADERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLL 241


                 ....*....
gi 15239327  248 SVDGGFTVN 256
Cdd:PRK12939 242 PVNGGFVMN 250
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 8-252 8.16e-54

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 174.87  E-value: 8.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK07097   7 SLKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEV- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK07097  86 GVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKE------FVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:PRK07097 166 LKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLRELQAdgsrhpFDQFIIAKTPAARWGDPEDLAGPAVFLASDASNF 245

                        250
                 ....*....|.
gi 15239327  242 ITGQVISVDGG 252
Cdd:PRK07097 246 VNGHILYVDGG 256
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 7-253 8.56e-54

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 174.52  E-value: 8.56e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    7 WSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHT----CSRNQEELNACLNDWKANGLVVSGSVCDasVRDQ---REKLi 79
Cdd:PRK12827   2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVldihPMRGRAEADAVAAGIEAAGGKALGLAFD--VRDFaatRAAL- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   80 qEASSAFSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIA-HPLLKASGVGSIVFISSVAGLVHLSSG 158
Cdd:PRK12827  79 -DAGVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAAlPPMIRARRGGRIVNIASVAGVRGNRGQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  159 SIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSlvetLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:PRK12827 158 VNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTP----MADNAAPTEHLLNPVPVQRLGEPDEVAALVAFLVSDA 233

                        250
                 ....*....|....*
gi 15239327  239 SSYITGQVISVDGGF 253
Cdd:PRK12827 234 ASYVTGQVIPVDGGF 248
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 14-252 2.03e-53

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: 173.14  E-value: 2.03e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLNIL 93
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQF-GGITIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  94 INNVGTNVRKP-TVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQLT 172
Cdd:cd05365  81 VNNAGGGGPKPfDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 173 RNLACEWASDNIRTNCVAPWYIKTSLVETLLeKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVDGG 252
Cdd:cd05365 161 RNLAFDLGPKGIRVNAVAPGAVKTDALASVL-TPEIERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSGG 239
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 8-247 5.01e-53

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: 171.90  E-value: 5.01e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVsgsVCDASVRDQREKLIQEASSAFs 87
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAV---PLDVTDEAAVEAAVAAAVAEF- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:COG4221  78 GRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLL--EKKEFVEAVVSRTPLgrvgEPEEVSSLVAFLC-LPASSYITG 244
Cdd:COG4221 158 VRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFdgDAEAAAAVYEGLEPL----TPEDVAEAVLFALtQPAHVNVNE 233


                ...
gi 15239327 245 QVI 247
Cdd:COG4221 234 LVL 236
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 8-256 5.75e-52

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: 169.49  E-value: 5.75e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSgsvCDASVRDQREKLIQEASSAFs 87
Cdd:cd05341   2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFH---LDVTDEDGWTAVVDTAREAF- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:cd05341  78 GRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 168 LNQLTRNLA--CEWASDNIRTNCVAPWYIKTSLVETLLEKKEfVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQ 245
Cdd:cd05341 158 VRGLTKSAAleCATQGYGIRVNSVHPGYIYTPMTDELLIAQG-EMGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVTGS 236

                       250
                ....*....|.
gi 15239327 246 VISVDGGFTVN 256
Cdd:cd05341 237 ELVVDGGYTAG 247
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 9-252 6.56e-52

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 169.64  E-value: 6.56e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKL-G 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPtVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:PRK06113  88 KVDILVNNAGGGGPKP-FDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  169 NQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLeKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVIS 248
Cdd:PRK06113 167 SHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVI-TPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILT 245


                 ....
gi 15239327  249 VDGG 252
Cdd:PRK06113 246 VSGG 249
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-255 9.48e-52

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 169.53  E-value: 9.48e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAK--VHTCSRNQEELNACLNdwKANGLVVSGSVcDASVRDQREKLIQEASSA 85
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADiiITTHGTNWDETRRLIE--KEGRKVTFVQV-DLTKPESAEKVVKEALEE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVaglvhLS-SGSI---- 160
Cdd:PRK06935  89 F-GKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASM-----LSfQGGKfvpa 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  161 YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:PRK06935 163 YTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNRNDEILKRIPAGRWGEPDDLMGAAVFLASRASD 242

                        250
                 ....*....|....*
gi 15239327  241 YITGQVISVDGGFTV 255
Cdd:PRK06935 243 YVNGHILAVDGGWLV 257
PRK06172 PRK06172
SDR family oxidoreductase;
9-254 1.11e-51

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 169.16  E-value: 1.11e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQ---EELNACLNDWKANGLVVSgsvCDASVRDQREKLIQEASSA 85
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAaggEETVALIREAGGEALFVA---CDVTRDAEVKALVEQTIAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FsGKLNILINNVGTNVRKPTV-EYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGAT 164
Cdd:PRK06172  82 Y-GRLDYAFNNAGIEIEQGRLaEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  165 KGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLE----KKEFVEAVvsrTPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:PRK06172 161 KHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEadprKAEFAAAM---HPVGRIGKVEEVASAVLYLCSDGAS 237

                        250
                 ....*....|....
gi 15239327  241 YITGQVISVDGGFT 254
Cdd:PRK06172 238 FTTGHALMVDGGAT 251
PRK06484 PRK06484
short chain dehydrogenase; Validated
 4-257 1.15e-50

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 173.50  E-value: 1.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    4 DKRWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSgsvCDASVRDQREKLIQEAS 83
Cdd:PRK06484 262 PSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQ---ADITDEAAVESAFAQIQ 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 SAFsGKLNILINNVGTN-VRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVgsIVFISSVAGLVHLSSGSIYG 162
Cdd:PRK06484 339 ARW-GRLDVLVNNAGIAeVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQGGV--IVNLGSIASLLALPPRNAYC 415

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  163 ATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEF-VEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:PRK06484 416 ASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLALKASGRAdFDSIRRRIPLGRLGDPEEVAEAIAFLASPAASY 495

                        250
                 ....*....|....*.
gi 15239327  242 ITGQVISVDGGFTVNG 257
Cdd:PRK06484 496 VNGATLTVDGGWTAFG 511
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 9-252 3.47e-50

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: 165.28  E-value: 3.47e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELN----ACL--NDWKANGLVVSGSVCDAsvrDQREKLIQEA 82
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEetrqSCLqaGVSEKKILLVVADLTEE---EGQDRIISTT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  83 SSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYG 162
Cdd:cd05364  78 LAKF-GRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYC 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 163 ATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTS------LVETllEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCL 236
Cdd:cd05364 156 ISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGfhrrmgMPEE--QYIKFLSRAKETHPLGRPGTVDEVAEAIAFLAS 233

                       250
                ....*....|....*.
gi 15239327 237 PASSYITGQVISVDGG 252
Cdd:cd05364 234 DASSFITGQLLPVDGG 249
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 9-256 5.83e-50

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 164.67  E-value: 5.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETF-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:PRK12429  81 GVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  169 NQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK--KEF---VEAVVSR-----TPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:PRK12429 161 IGLTKVVALEGATHGVTVNAICPGYVDTPLVRKQIPDlaKERgisEEEVLEDvllplVPQKRFTTVEEIADYALFLASFA 240

                        250
                 ....*....|....*...
gi 15239327  239 SSYITGQVISVDGGFTVN 256
Cdd:PRK12429 241 AKGVTGQAWVVDGGWTAQ 258
PRK07856 PRK07856
SDR family oxidoreductase;
8-252 8.62e-50

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 164.34  E-value: 8.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEElnaclndwKANGLVVSGSVCDasVRD--QREKLIQEASSA 85
Cdd:PRK07856   3 DLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPE--------TVDGRPAEFHAAD--VRDpdQVAALVDAIVER 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKA-SGVGSIVFISSVAGLvHLSSGS-IYGA 163
Cdd:PRK07856  73 H-GRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSVSGR-RPSPGTaAYGA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDnIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK07856 151 AKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQSELHYGDAEGIAAVAATVPLGRLATPADIAWACLFLASDLASYVS 229


                 ....*....
gi 15239327  244 GQVISVDGG 252
Cdd:PRK07856 230 GANLEVHGG 238
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 9-257 1.07e-49

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 165.21  E-value: 1.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTC----SRNQEELNACLNDWKANGLVVSGSVCDasvRDQREKLIQEASS 84
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVyldeHEDANETKQRVEKEGVKCLLIPGDVSD---EAFCKDAVEETVR 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   85 AFsGKLNILINNVGTNVRKPTVEY-SSEEYAKIMSTNLESAFHLSQIAHPLLKaSGvGSIVFISSVAGLvhLSSGSI--Y 161
Cdd:PRK06701 121 EL-GRLDILVNNAAFQYPQQSLEDiTAEQLDKTFKTNIYSYFHMTKAALPHLK-QG-SAIINTGSITGY--EGNETLidY 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  162 GATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEfVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:PRK06701 196 SATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPSDFDEEK-VSQFGSNTPMQRPGQPEELAPAYVFLASPDSSY 274

                        250
                 ....*....|....*.
gi 15239327  242 ITGQVISVDGGFTVNG 257
Cdd:PRK06701 275 ITGQMLHVNGGVIVNG 290
PRK06484 PRK06484
short chain dehydrogenase; Validated
 11-257 1.11e-49

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 170.80  E-value: 1.11e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEelnACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKL 90
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVE---RARERADSLGPDHHALAMDVSDEAQIREGFEQLHREF-GRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVR--KPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVG-SIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK06484  81 DVLVNNAGVTDPtmTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGaAIVNVASGAGLVALPKRTAYSASKAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEF-VEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQV 246
Cdd:PRK06484 161 VISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERAGKLdPSAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGST 240

                        250
                 ....*....|.
gi 15239327  247 ISVDGGFTVNG 257
Cdd:PRK06484 241 LVVDGGWTVYG 251
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
12-256 1.82e-49

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 163.01  E-value: 1.82e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQeelNACLNDW-------KANGLVVSGSVCD-ASVRDQREKLIQEas 83
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSG---NDCAKDWfeeygftEDQVRLKELDVTDtEECAEALAEIEEE-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 safSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:PRK12824  78 ---EGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLleKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK12824 155 AKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQM--GPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFIT 232

                        250
                 ....*....|...
gi 15239327  244 GQVISVDGGFTVN 256
Cdd:PRK12824 233 GETISINGGLYMH 245
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 9-254 2.26e-49

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: 163.32  E-value: 2.26e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEE-LNACLNDWKANG---LVVSGsvcDASVRDQREKLIQEASS 84
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDaAEEVVEEIKAVGgkaIAVQA---DVSKEEDVVALFQSAIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  85 AFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIA-HPLLKASGVGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:cd05358  78 EF-GTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAiKRFRKSKIKGKIINMSSVHEKIPWPGHVNYAA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:cd05358 157 SKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVT 236

                       250
                ....*....|.
gi 15239327 244 GQVISVDGGFT 254
Cdd:cd05358 237 GTTLFVDGGMT 247
PRK07035 PRK07035
SDR family oxidoreductase;
8-255 9.91e-49

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 161.34  E-value: 9.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK07035   5 DLTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERH- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVR-KPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK07035  84 GRLDILVNNAAANPYfGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQV 246
Cdd:PRK07035 164 AVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTGEC 243


                 ....*....
gi 15239327  247 ISVDGGFTV 255
Cdd:PRK07035 244 LNVDGGYLS 252
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 7-255 1.34e-48

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 161.09  E-value: 1.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    7 WSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIqEASSAF 86
Cdd:PRK07523   6 FDLTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAI-DAFEAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 SGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK07523  85 IGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQV 246
Cdd:PRK07523 165 AVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALVADPEFSAWLEKRTPAGRWGKVEELVGACVFLASDASSFVNGHV 244


                 ....*....
gi 15239327  247 ISVDGGFTV 255
Cdd:PRK07523 245 LYVDGGITA 253
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 6-254 2.80e-48

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 160.27  E-value: 2.80e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    6 RWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSvCDASVRdqrekliqeASSA 85
Cdd:PRK07060   4 AFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRLDVG-DDAAIR---------AALA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ-IAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGAT 164
Cdd:PRK07060  74 AAGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARhVARAMIAAGRGGSIVNVSSQAALVGLPDHLAYCAS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  165 KGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITG 244
Cdd:PRK07060 154 KAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSG 233

                        250
                 ....*....|
gi 15239327  245 QVISVDGGFT 254
Cdd:PRK07060 234 VSLPVDGGYT 243
PRK08589 PRK08589
SDR family oxidoreductase;
9-252 1.84e-47

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 158.79  E-value: 1.84e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVhTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYV-LAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQF-G 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTV-EYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK08589  82 RVDVLFNNAGVDNAAGRIhEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQG-GSIINTSSFSGQAADLYRSGYNAAKGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKE------FVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:PRK08589 161 VINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSEdeagktFRENQKWMTPLGRLGKPEEVAKLVVFLASDDSSF 240

                        250
                 ....*....|.
gi 15239327  242 ITGQVISVDGG 252
Cdd:PRK08589 241 ITGETIRIDGG 251
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 8-257 4.75e-47

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 157.48  E-value: 4.75e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSgsvCDASVRDQREKLIQEASSAFs 87
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIA---TDITDDAAIERAVATVVARF- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVrKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK08265  79 GRVDILVNLACTYL-DDGLASSRADWLAALDVNLVSAAMLAQAAHPHLARGG-GAIVNFTSISAKFAQTGRWLYPASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLE-KKEFVEAVVSRT-PLGRVGEPEEVSSLVAFLCLPASSYITGQ 245
Cdd:PRK08265 157 IRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSGgDRAKADRVAAPFhLLGRVGDPEEVAQVVAFLCSDAASFVTGA 236

                        250
                 ....*....|..
gi 15239327  246 VISVDGGFTVNG 257
Cdd:PRK08265 237 DYAVDGGYSALG 248
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 12-256 5.66e-47

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 156.84  E-value: 5.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLN 91
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETAKEINQAGGKAVAYKLDVSDKDQVFSAIDQAAEKF-GGFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYGATKGALNQ 170
Cdd:TIGR02415  80 VMVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKIINAASIAGHEGNPILSAYSSTKFAVRG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   171 LTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK---------KEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:TIGR02415 160 LTQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEEtseiagkpiGEGFEEFSSEIALGRPSEPEDVAGLVSFLASEDSDY 239

                         250
                  ....*....|....*
gi 15239327   242 ITGQVISVDGGFTVN 256
Cdd:TIGR02415 240 ITGQSILVDGGMVYN 254
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-252 8.43e-47

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 156.48  E-value: 8.43e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEElnaclndwKANGLVVSGSV---CDASVRDQREKLIQEASSA 85
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN--------EAKELREKGVFtikCDVGNRDQVKKSKEVVEKE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSG-SIYGAT 164
Cdd:PRK06463  77 F-GRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEGtTFYAIT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  165 KGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLV---ETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTlsgKSQEEAEKLRELFRNKTVLKTTGKPEDIANIVLFLASDDARY 235

                        250
                 ....*....|.
gi 15239327  242 ITGQVISVDGG 252
Cdd:PRK06463 236 ITGQVIVADGG 246
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 11-252 1.47e-46

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: 156.00  E-value: 1.47e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAC----LNDWKANGLVVsgsVCDASVRDQREKLIQEASSAF 86
Cdd:cd05366   2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKStiqeISEAGYNAVAV---GADVTDKDDVEALIDQAVEKF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYGATK 165
Cdd:cd05366  79 -GSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHgGKIINASSIAGVQGFPNLGAYSASK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 166 GALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK---------KEFVEAVVSRTPLGRVGEPEEVSSLVAFLCL 236
Cdd:cd05366 158 FAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEvgeiagkpeGEGFAEFSSSIPLGRLSEPEDVAGLVSFLAS 237

                       250
                ....*....|....*.
gi 15239327 237 PASSYITGQVISVDGG 252
Cdd:cd05366 238 EDSDYITGQTILVDGG 253
PRK07774 PRK07774
SDR family oxidoreductase;
9-255 2.46e-46

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 155.29  E-value: 2.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAF-G 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNV---GTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHlssGSIYGATK 165
Cdd:PRK07774  83 GIDYLVNNAaiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLY---SNFYGLAK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  166 GALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLeKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQ 245
Cdd:PRK07774 160 VGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVT-PKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWITGQ 238

                        250
                 ....*....|
gi 15239327  246 VISVDGGFTV 255
Cdd:PRK07774 239 IFNVDGGQII 248
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 1-255 5.54e-46

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 154.43  E-value: 5.54e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    1 METDKRWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQ--EELNACLNDWKANGLVvsgsvCDASVRDQREKL 78
Cdd:PRK06841   5 KQFDLAFDLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEdvAEVAAQLLGGNAKGLV-----CDVSDSQSVEAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   79 IQEASSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSG 158
Cdd:PRK06841  80 VAAVISAF-GRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  159 SIYGATKGALNQLTRNLACEWASDNIRTNCVAPwyiktSLVETLLEKK----EFVEAVVSRTPLGRVGEPEEVSSLVAFL 234
Cdd:PRK06841 159 VAYCASKAGVVGMTKVLALEWGPYGITVNAISP-----TVVLTELGKKawagEKGERAKKLIPAGRFAYPEEIAAAALFL 233

                        250       260
                 ....*....|....*....|.
gi 15239327  235 CLPASSYITGQVISVDGGFTV 255
Cdd:PRK06841 234 ASDAAAMITGENLVIDGGYTI 254
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 8-253 1.34e-44

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: 151.46  E-value: 1.34e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:cd08935   2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQF- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 GKLNILINNVGTNVRKPTV--------------EYSSEEYAKIMSTNLESAFHLSQI-AHPLLKASGvGSIVFISSVAGL 152
Cdd:cd08935  81 GTVDILINGAGGNHPDATTdpehyepeteqnffDLDEEGWEFVFDLNLNGSFLPSQVfGKDMLEQKG-GSIINISSMNAF 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 153 VHLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKE-----FVEAVVSRTPLGRVGEPEEV 227
Cdd:cd08935 160 SPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINPDgsytdRSNKILGRTPMGRFGKPEEL 239

                       250       260
                ....*....|....*....|....*..
gi 15239327 228 SSLVAFLC-LPASSYITGQVISVDGGF 253
Cdd:cd08935 240 LGALLFLAsEKASSFVTGVVIPVDGGF 266
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 9-256 2.16e-44

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: 150.91  E-value: 2.16e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAclNDWKA-------NGLVVSGSVCDAS-VRDqrekLIQ 80
Cdd:cd05355  24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDA--EETKKlieeegrKCLLIPGDLGDESfCRD----LVK 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  81 EASSAFsGKLNILINNVGTNVRKPTVEY-SSEEYAKIMSTNLESAFHLSQIAHPLLKaSGvGSIVFISSV---AGLVHLS 156
Cdd:cd05355  98 EVVKEF-GKLDILVNNAAYQHPQESIEDiTTEQLEKTFRTNIFSMFYLTKAALPHLK-KG-SSIINTTSVtayKGSPHLL 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 157 SgsiYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLV-ETLLEKKefVEAVVSRTPLGRVGEPEEVSSLVAFLC 235
Cdd:cd05355 175 D---YAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIpSSFPEEK--VSEFGSQVPMGRAGQPAEVAPAYVFLA 249

                       250       260
                ....*....|....*....|.
gi 15239327 236 LPASSYITGQVISVDGGFTVN 256
Cdd:cd05355 250 SQDSSYVTGQVLHVNGGEIIN 270
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 7-255 3.45e-44

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: 149.46  E-value: 3.45e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   7 WSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSgsvCDASVRDQREKLIQEASSAF 86
Cdd:cd05345   1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQ---ADVTKRADVEAMVEAALSKF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  87 sGKLNILINNVGTNVR-KPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATK 165
Cdd:cd05345  78 -GRLDILVNNAGITHRnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 166 GALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLL--EKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:cd05345 157 GWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMgeDTPENRAKFRATIPLGRLSTPDDIANAALYLASDEASFIT 236

                       250
                ....*....|..
gi 15239327 244 GQVISVDGGFTV 255
Cdd:cd05345 237 GVALEVDGGRCI 248
PRK06138 PRK06138
SDR family oxidoreductase;
9-254 6.21e-44

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 149.15  E-value: 6.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGlVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGG-RAFARQGDVGSAEAVEALVDFVAARW-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  169 NQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK----KEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITG 244
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARhadpEALREALRARHPMNRFGTAEEVAQAALFLASDESSFATG 240

                        250
                 ....*....|
gi 15239327  245 QVISVDGGFT 254
Cdd:PRK06138 241 TTLVVDGGWL 250
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 7-254 1.87e-43

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 148.24  E-value: 1.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    7 W-SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQeelnaclNDWKANGLVVSgsVCDASVRDQREKLIQEASSA 85
Cdd:PRK06171   4 WlNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHG-------GDGQHENYQFV--PTDVSSAEEVNHTVAEIIEK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FsGKLNILINNVGTNVRKPTV---------EYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLS 156
Cdd:PRK06171  75 F-GRIDGLVNNAGINIPRLLVdekdpagkyELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  157 SGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKtslvETLLEKKEFVEAV-----------------VSRTPLG 219
Cdd:PRK06171 154 GQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILE----ATGLRTPEYEEALaytrgitveqlragytkTSTIPLG 229

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15239327  220 RVGEPEEVSSLVAFLCLPASSYITGQVISVDGGFT 254
Cdd:PRK06171 230 RSGKLSEVADLVCYLLSDRASYITGVTTNIAGGKT 264
PRK06500 PRK06500
SDR family oxidoreductase;
9-252 3.53e-43

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 147.02  E-value: 3.53e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSgsvCDA-SVRDQREkLIQEASSAFs 87
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIR---ADAgDVAAQKA-LAQALAEAF- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLkASGvGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK06500  79 GRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLL-ANP-ASIVLNGSINAHIGMPNSSVYAASKAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETL----LEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK06500 157 LLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLglpeATLDAVAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFIV 236


                 ....*....
gi 15239327  244 GQVISVDGG 252
Cdd:PRK06500 237 GSEIIVDGG 245
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 11-252 4.47e-43

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: 146.71  E-value: 4.47e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELN-ACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGK 89
Cdd:cd08930   2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEqLKEELTNLYKNRVIALELDITSKESIKELIESYLEKF-GR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  90 LNILINNVGTNVR---KPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLV----------HLS 156
Cdd:cd08930  81 IDILINNAYPSPKvwgSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIapdfriyentQMY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 157 SGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSlvetllEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCL 236
Cdd:cd08930 161 SPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNN------QPSEFLEKYTKKCPLKRMLNPEDLRGAIIFLLS 234

                       250
                ....*....|....*.
gi 15239327 237 PASSYITGQVISVDGG 252
Cdd:cd08930 235 DASSYVTGQNLVIDGG 250
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 8-254 8.26e-43

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 146.58  E-value: 8.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERF- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHP-LLKASGVGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK13394  83 GSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKhMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKH 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK--KEF---VEAVVSR-----TPLGRVGEPEEVSSLVAFLCL 236
Cdd:PRK13394 163 GLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEqaKELgisEEEVVKKvmlgkTVDGVFTTVEDVAQTVLFLSS 242

                        250
                 ....*....|....*...
gi 15239327  237 PASSYITGQVISVDGGFT 254
Cdd:PRK13394 243 FPSAALTGQSFVVSHGWF 260
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
9-254 8.88e-43

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 146.02  E-value: 8.88e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAK-VHTCSRNQEELNACLNDWKANGlvVSGSVCDASVRDqREK---LIQEASS 84
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDiAVNYARSRKAAEETAEEIEALG--RKALAVKANVGD-VEKikeMFAQIDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   85 AFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGAT 164
Cdd:PRK08063  79 EF-GRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  165 KGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITG 244
Cdd:PRK08063 158 KAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREELLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMIRG 237

                        250
                 ....*....|
gi 15239327  245 QVISVDGGFT 254
Cdd:PRK08063 238 QTIIVDGGRS 247
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 9-252 1.38e-42

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: 145.33  E-value: 1.38e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASvrdQREKLIQEASSAFSG 88
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQ---QVAALFERAVEEFGG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  89 kLNILINNVG-TNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:cd08944  78 -LDLLVNNAGaMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKE-----FVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYI 242
Cdd:cd08944 157 IRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEgalgpGGFHLLIHQLQGRLGRPEDVAAAVVFLLSDDASFI 236

                       250
                ....*....|
gi 15239327 243 TGQVISVDGG 252
Cdd:cd08944 237 TGQVLCVDGG 246
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 8-254 1.61e-42

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 145.64  E-value: 1.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSR-NQEELNACLNDWKANG---LVVSGsvcDASVRDQREKLIQEAS 83
Cdd:PRK08936   4 DLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIKKAGgeaIAVKG---DVTVESDVVNLIQTAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 SAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYG 162
Cdd:PRK08936  81 KEF-GTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIkGNIINMSSVHEQIPWPLFVHYA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  163 ATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYI 242
Cdd:PRK08936 160 ASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRADVESMIPMGYIGKPEEIAAVAAWLASSEASYV 239

                        250
                 ....*....|..
gi 15239327  243 TGQVISVDGGFT 254
Cdd:PRK08936 240 TGITLFADGGMT 251
PRK07063 PRK07063
SDR family oxidoreductase;
9-255 1.75e-42

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 145.58  E-value: 1.75e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKA--NGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARdvAGARVLAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK07063  85 -GPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKH 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRT----PLGRVGEPEEVSSLVAFLCLPASSYI 242
Cdd:PRK07063 164 GLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPAAARAETlalqPMKRIGRPEEVAMTAVFLASDEAPFI 243

                        250
                 ....*....|...
gi 15239327  243 TGQVISVDGGFTV 255
Cdd:PRK07063 244 NATCITIDGGRSV 256
PRK05867 PRK05867
SDR family oxidoreductase;
7-254 1.76e-42

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 145.56  E-value: 1.76e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    7 WSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK05867   5 FDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAEL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 SGkLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVG-SIVFISSVAG-LVHLSSG-SIYGA 163
Cdd:PRK05867  85 GG-IDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGgVIINTASMSGhIINVPQQvSHYCA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAvvsRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK05867 164 SKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQPLWEP---KIPLGRLGRPEELAGLYLYLASEASSYMT 240

                        250
                 ....*....|.
gi 15239327  244 GQVISVDGGFT 254
Cdd:PRK05867 241 GSDIVIDGGYT 251
PRK09135 PRK09135
pteridine reductase; Provisional
 8-256 2.07e-42

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 145.07  E-value: 2.07e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKV--HtCSRNQEELNAC---LNDWKANG-LVVSGSVCDAsvrDQREKLIQE 81
Cdd:PRK09135   3 TDSAKVALITGGARRIGAAIARTLHAAGYRVaiH-YHRSAAEADALaaeLNALRPGSaAALQADLLDP---DALPELVAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   82 ASSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIY 161
Cdd:PRK09135  79 CVAAF-GRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQR-GAIVNITDIHAERPLKGYPVY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  162 GATKGALNQLTRNLACEWASDnIRTNCVAPWYI-----KTSLVEtllekkEFVEAVVSRTPLGRVGEPEEVSSLVAFLcL 236
Cdd:PRK09135 157 CAAKAALEMLTRSLALELAPE-VRVNAVAPGAIlwpedGNSFDE------EARQAILARTPLKRIGTPEDIAEAVRFL-L 228

                        250       260
                 ....*....|....*....|
gi 15239327  237 PASSYITGQVISVDGGFTVN 256
Cdd:PRK09135 229 ADASFITGQILAVDGGRSLT 248
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 8-256 2.41e-42

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: 144.92  E-value: 2.41e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAC-------------LNDWKANglvvsgsvcdasvrdq 74
Cdd:cd05351   4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLvrecpgiepvcvdLSDWDAT---------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  75 REKLIQeassafSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLV 153
Cdd:cd05351  68 EEALGS------VGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQR 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 154 HLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAF 233
Cdd:cd05351 142 ALTNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILF 221

                       250       260
                ....*....|....*....|...
gi 15239327 234 LCLPASSYITGQVISVDGGFTVN 256
Cdd:cd05351 222 LLSDKSSMTTGSTLPVDGGFLAS 244
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
8-252 3.97e-42

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 152.31  E-value: 3.97e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVsGSVCDASVRDQREKLIQEASSAFS 87
Cdd:PRK08324 419 PLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRAL-GVACDVTDEAAVQAAFEEAALAFG 497

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GkLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK08324 498 G-VDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASKNAVNPGPNFGAYGAAKA 576

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAP-------------WyIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAF 233
Cdd:PRK08324 577 AELHLVRQLALELGPDGIRVNGVNPdavvrgsgiwtgeW-IEARAAAYGLSEEELEEFYRARNLLKREVTPEDVAEAVVF 655

                        250
                 ....*....|....*....
gi 15239327  234 LCLPASSYITGQVISVDGG 252
Cdd:PRK08324 656 LASGLLSKTTGAIITVDGG 674
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-257 4.02e-42

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 144.48  E-value: 4.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    7 WSLAGKTALVTGGTRGIGRAVVEELAKFGAK-VHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSA 85
Cdd:PRK06077   2 YSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLvVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLVHLSSGSIYGATK 165
Cdd:PRK06077  82 Y-GVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREGG--AIVNIASVAGIRPAYGLSIYGAMK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  166 GALNQLTRNLACEWASdNIRTNCVAPWYIKTSLVETL-----LEKKEFVEAVvsrTPLGRVGEPEEVSSLVAFLClpASS 240
Cdd:PRK06077 159 AAVINLTKYLALELAP-KIRVNAIAPGFVKTKLGESLfkvlgMSEKEFAEKF---TLMGKILDPEEVAEFVAAIL--KIE 232

                        250
                 ....*....|....*..
gi 15239327  241 YITGQVISVDGGFTVNG 257
Cdd:PRK06077 233 SITGQVFVLDSGESLKG 249
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 7-255 4.86e-42

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 144.13  E-value: 4.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    7 WSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAf 86
Cdd:PRK08085   5 FSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKD- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 SGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK08085  84 IGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQV 246
Cdd:PRK08085 164 AVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEAFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNGHL 243


                 ....*....
gi 15239327  247 ISVDGGFTV 255
Cdd:PRK08085 244 LFVDGGMLV 252
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 11-254 4.90e-42

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: 144.51  E-value: 4.90e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKAN--GLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:cd08940   2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAkhGVKVLYHGADLSKPAAIEDMVAYAQRQF-G 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:cd08940  81 GVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 169 NQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLE---KKEFV-------EAVVSRTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:cd08940 161 VGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQISalaQKNGVpqeqaarELLLEKQPSKQFVTPEQLGDTAVFLASDA 240

                       250
                ....*....|....*.
gi 15239327 239 SSYITGQVISVDGGFT 254
Cdd:cd08940 241 ASQITGTAVSVDGGWT 256
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 9-254 5.13e-42

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: 144.14  E-value: 5.13e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVhTCSRNQEELNACLndwkANGL---VVSGSVCDASVRDQREKLIQEASSA 85
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGARV-VIADIDDDAGQAV----AAELgdpDISFVHCDVTVEADVRAAVDTAVAR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  86 FsGKLNILINNVGTNVRKPT--VEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:cd05326  77 F-GRLDIMFNNAGVLGAPCYsiLETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLV-ETLLEKKEFVEAVVSR--TPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:cd05326 156 SKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLtAGFGVEDEAIEEAVRGaaNLKGTALRPEDIAAAVLYLASDDSR 235

                       250
                ....*....|....
gi 15239327 241 YITGQVISVDGGFT 254
Cdd:cd05326 236 YVSGQNLVVDGGLT 249
PRK06398 PRK06398
aldose dehydrogenase; Validated
 9-255 6.01e-42

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 144.20  E-value: 6.01e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAclndwkanglvVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYND-----------VDYFKVDVSNKEQVIKGIDYVISKY-G 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:PRK06398  72 RIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  169 NQLTRNLACEWASdNIRTNCVAPWYIKTSLVE--TLLEKKEFVEAVVSRT-------PLGRVGEPEEVSSLVAFLCLPAS 239
Cdd:PRK06398 152 LGLTRSIAVDYAP-TIRCVAVCPGSIRTPLLEwaAELEVGKDPEHVERKIrewgemhPMKRVGKPEEVAYVVAFLASDLA 230

                        250
                 ....*....|....*.
gi 15239327  240 SYITGQVISVDGGFTV 255
Cdd:PRK06398 231 SFITGECVTVDGGLRA 246
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
9-255 1.26e-41

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 143.40  E-value: 1.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNqEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDIS-PEIEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKE-G 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAG-LVHLSSGSIYGATKGA 167
Cdd:PRK08226  82 RIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYALTKAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLL------EKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:PRK08226 162 IVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIArqsnpeDPESVLTEMAKAIPLRRLADPLEVGELAAFLASDESSY 241

                        250
                 ....*....|....
gi 15239327  242 ITGQVISVDGGFTV 255
Cdd:PRK08226 242 LTGTQNVIDGGSTL 255
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 9-262 1.44e-41

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 143.17  E-value: 1.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDasVRDQR--EKLIQEASSAF 86
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSAD--VRDYAavEAAFAQIADEF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISS------VAGLVHLSsgsi 160
Cdd:PRK07576  85 -GPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG-ASIIQISApqafvpMPMQAHVC---- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  161 ygATKGALNQLTRNLACEWASDNIRTNCVAPWYIK-TSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPAS 239
Cdd:PRK07576 159 --AAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAgTEGMARLAPSPELQAAVAQSVPLKRNGTKQDIANAALFLASDMA 236

                        250       260
                 ....*....|....*....|...
gi 15239327  240 SYITGQVISVDGGFTVNGFSYAM 262
Cdd:PRK07576 237 SYITGVVLPVDGGWSLGGASIAM 259
PRK12743 PRK12743
SDR family oxidoreductase;
12-257 1.64e-41

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 142.87  E-value: 1.64e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVH-TCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKL 90
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGiTWHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRL-GRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIA-HPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:PRK12743  82 DVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAaRHMVKQGQGGRIINITSVHEHTPLPGASAYTAAKHALG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  170 QLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLE--KKEFVEAVvsrtPLGRVGEPEEVSSLVAFLCLPASSYITGQVI 247
Cdd:PRK12743 162 GLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSdvKPDSRPGI----PLGRPGDTHEIASLVAWLCSEGASYTTGQSL 237

                        250
                 ....*....|
gi 15239327  248 SVDGGFTVNG 257
Cdd:PRK12743 238 IVDGGFMLAN 247
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 8-253 1.76e-41

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 143.50  E-value: 1.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK08277   7 SLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDF- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEY---------------SSEEYAKIMSTNLESAFHLSQI-AHPLLKASGvGSIVFISSVAG 151
Cdd:PRK08277  86 GPCDILINGAGGNHPKATTDNefhelieptktffdlDEEGFEFVFDLNLLGTLLPTQVfAKDMVGRKG-GNIINISSMNA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  152 LVHLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKK-----EFVEAVVSRTPLGRVGEPEE 226
Cdd:PRK08277 165 FTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALLFNEdgsltERANKILAHTPMGRFGKPEE 244

                        250       260
                 ....*....|....*....|....*...
gi 15239327  227 VSSLVAFLCLP-ASSYITGQVISVDGGF 253
Cdd:PRK08277 245 LLGTLLWLADEkASSFVTGVVLPVDGGF 272
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 9-252 1.83e-41

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: 143.05  E-value: 1.83e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNqEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:cd08937   2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERF-G 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  89 KLNILINNVGTNV-RKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVA--GLVHLSsgsiYGATK 165
Cdd:cd08937  80 RVDVLINNVGGTIwAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIAtrGIYRIP----YSAAK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 166 GALNQLTRNLACEWASDNIRTNCVAP-------WYIKTSLVETLLEKKE----FVEAVVSRTPLGRVGEPEEVSSLVAFL 234
Cdd:cd08937 156 GGVNALTASLAFEHARDGIRVNAVAPggteappRKIPRNAAPMSEQEKVwyqrIVDQTLDSSLMGRYGTIDEQVRAILFL 235

                       250
                ....*....|....*...
gi 15239327 235 CLPASSYITGQVISVDGG 252
Cdd:cd08937 236 ASDEASYITGTVLPVGGG 253
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 8-256 2.96e-41

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 142.38  E-value: 2.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANG---LVVSGSVCDASVrdqREKLIQEASS 84
Cdd:PRK07478   3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGgeaVALAGDVRDEAY---AKALVALAVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   85 AFsGKLNILINNVGTNVR-KPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGL-VHLSSGSIYG 162
Cdd:PRK07478  80 RF-GGLDIAFNNAGTLGEmGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHtAGFPGMAAYA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  163 ATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYI 242
Cdd:PRK07478 159 ASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEALAFVAGLHALKRMAQPEEIAQAALFLASDAASFV 238

                        250
                 ....*....|....
gi 15239327  243 TGQVISVDGGFTVN 256
Cdd:PRK07478 239 TGTALLVDGGVSIT 252
PRK07069 PRK07069
short chain dehydrogenase; Validated
 14-252 6.38e-41

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 141.39  E-value: 6.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEE----LNACLNDWKANGlVVSGSVCDASVRDQREKLIQEASSAFSGk 89
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAgldaFAAEINAAHGEG-VAFAAVQDVTDEAQWQALLAQAADAMGG- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   90 LNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:PRK07069  80 LSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  170 QLTRNLA--CEWASDNIRTNCVAPWYIKTSLVETL---LEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITG 244
Cdd:PRK07069 160 SLTKSIAldCARRGLDVRCNSIHPTFIRTGIVDPIfqrLGEEEATRKLARGVPLGRLGEPDDVAHAVLYLASDESRFVTG 239


                 ....*...
gi 15239327  245 QVISVDGG 252
Cdd:PRK07069 240 AELVIDGG 247
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 12-252 2.76e-40

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: 139.96  E-value: 2.76e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWK--ANGLVVSGSVCDASVRDQREKLIQEASSAFsGK 89
Cdd:cd05330   4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLeiAPDAEVLLIKADVSDEAQVEAYVDATVEQF-GR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  90 LNILINNVGTNVRK-PTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:cd05330  83 IDGFFNNAGIEGKQnLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 169 NQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK------KEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYI 242
Cdd:cd05330 163 VGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSLKQlgpenpEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDDAGYV 242

                       250
                ....*....|
gi 15239327 243 TGQVISVDGG 252
Cdd:cd05330 243 NAAVVPIDGG 252
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 12-254 3.25e-40

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: 139.13  E-value: 3.25e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVH-TCSRNQEELNACLNDWKANGLVVSGSVCDasvRDQREKLIQEASSAFsGKL 90
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVvNYYRSTESAEAVAAEAGERAIAIQADVRD---RDQVQAMIEEAKNHF-GPV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  91 NILINNV------GTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSvaGLVHLssGSI---- 160
Cdd:cd05349  77 DTIVNNAlidfpfDPDQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGT--NLFQN--PVVpyhd 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 161 YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLlEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:cd05349 153 YTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAA-TPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWAR 231

                       250
                ....*....|....
gi 15239327 241 YITGQVISVDGGFT 254
Cdd:cd05349 232 AVTGQNLVVDGGLV 245
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 9-253 4.68e-40

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 138.72  E-value: 4.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVH-TCSRNQ---EELNACLNDWKANGLVVSGSVCD-ASVRdqreKLIQEAS 83
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAvNYAGSAaaaDELVAEIEAAGGRAIAVQADVADaAAVT----RLFDAAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 SAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLVHLSSGSIYGA 163
Cdd:PRK12937  79 TAF-GRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQGG--RIINLSTSVIALPLPGYGPYAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLvetLLEKK--EFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:PRK12937 156 SKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL---FFNGKsaEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAW 232

                        250
                 ....*....|..
gi 15239327  242 ITGQVISVDGGF 253
Cdd:PRK12937 233 VNGQVLRVNGGF 244
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 9-258 5.66e-40

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 139.32  E-value: 5.66e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGsvcDASVRDQREKLIQEASSAFsG 88
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEG---DVTSYADNQRAVDQTVDAF-G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVG-----TNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:PRK06200  80 KLDCFVGNAGiwdynTSLVDIPAETLDTAFDEIFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYPGGGGPLYTA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDnIRTNCVAPWYIKTSLV---------ETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFL 234
Cdd:PRK06200 159 SKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLRgpaslgqgeTSISDSPGLADMIAAITPLQFAPQPEDHTGPYVLL 237

                        250       260
                 ....*....|....*....|....*
gi 15239327  235 CLPA-SSYITGQVISVDGGFTVNGF 258
Cdd:PRK06200 238 ASRRnSRALTGVVINADGGLGIRGI 262
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 8-253 2.85e-39

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 137.06  E-value: 2.85e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVH-TCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVViNYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK12935  83 -GKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEkkEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPAsSYITGQV 246
Cdd:PRK12935 162 GMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPE--EVRQKIVAKIPKKRFGQADEIAKGVVYLCRDG-AYITGQQ 238


                 ....*..
gi 15239327  247 ISVDGGF 253
Cdd:PRK12935 239 LNINGGL 245
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 11-252 3.28e-39

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 136.73  E-value: 3.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKL 90
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKF-GRI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSV------AGLVHLSSgsiygA 163
Cdd:PRK07677  80 DALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIkGNIINMVATyawdagPGVIHSAA-----A 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNqLTRNLACEWASD-NIRTNCVAPWYI-KTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:PRK07677 155 KAGVLA-MTRTLAVEWGRKyGIRVNAIAPGPIeRTGGADKLWESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAY 233

                        250
                 ....*....|.
gi 15239327  242 ITGQVISVDGG 252
Cdd:PRK07677 234 INGTCITMDGG 244
PRK08628 PRK08628
SDR family oxidoreductase;
9-254 1.24e-38

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 135.47  E-value: 1.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEElNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPD-DEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKF-G 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKpTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:PRK08628  83 RIDGLVNNAGVNDGV-GLEAGREAFVASLERNLIHYYVMAHYCLPHLKASR-GAIVNISSKTALTGQGGTSGYAAAKGAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  169 NQLTRNLACEWASDNIRTNCVAPWYIKTSL----VETLLEKKEFVEAVVSRTPLG-RVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK08628 161 LALTREWAVALAKDGVRVNAVIPAEVMTPLyenwIATFDDPEAKLAAITAKIPLGhRMTTAEEIADTAVFLLSERSSHTT 240

                        250
                 ....*....|.
gi 15239327  244 GQVISVDGGFT 254
Cdd:PRK08628 241 GQWLFVDGGYV 251
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 12-252 1.80e-38

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: 134.97  E-value: 1.80e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLN 91
Cdd:cd08945   4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARY-GPID 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ--IAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:cd08945  83 VLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKevLKAGGMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 170 QLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLE---------KKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:cd08945 163 GFTKALGLELARTGITVNAVCPGFVETPMAASVREhyadiwevsTEEAFDRITARVPLGRYVTPEEVAGMVAYLIGDGAA 242

                       250
                ....*....|..
gi 15239327 241 YITGQVISVDGG 252
Cdd:cd08945 243 AVTAQALNVCGG 254
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 11-255 3.64e-38

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 133.55  E-value: 3.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELnaclndwkangLVVSGSVCDASVRDQREKLIQEAssafsGKL 90
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPD-----------LSGNFHFLQLDLSDDLEPLFDWV-----PSV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGT-NVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:PRK06550  69 DILCNTAGIlDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  170 QLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISV 249
Cdd:PRK06550 149 GFTKQLALDYAKDGIQVFGIAPGAVKTPMTAADFEPGGLADWVARETPIKRWAEPEEVAELTLFLASGKADYMQGTIVPI 228


                 ....*.
gi 15239327  250 DGGFTV 255
Cdd:PRK06550 229 DGGWTL 234
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 8-252 3.72e-37

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 132.23  E-value: 3.72e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKA--NGLVVSGSVCDASVRDQREKLIqEASSA 85
Cdd:PRK05875   4 SFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEAlkGAGAVRYEPADVTDEDQVARAV-DAATA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FSGKLNILINNVGTN-VRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGL-VHLSSGSiYGA 163
Cdd:PRK05875  83 WHGRLHGVVHCAGGSeTIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASnTHRWFGA-YGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK05875 162 TKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSADYRACTPLPRVGEVEDVANLAMFLLSDAASWIT 241


                 ....*....
gi 15239327  244 GQVISVDGG 252
Cdd:PRK05875 242 GQVINVDGG 250
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 8-252 3.92e-37

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 131.07  E-value: 3.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGsvCDASVRDQREKLIQEASSAFs 87
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGG--IDLVDPQAARRAVDEVNRQF- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK12828  81 GRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFveavvsrtplGRVGEPEEVSSLVAFLCLPASSYITGQVI 247
Cdd:PRK12828 161 VARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMPDADF----------SRWVTPEQIAAVIAFLLSDEAQAITGASI 230


                 ....*
gi 15239327  248 SVDGG 252
Cdd:PRK12828 231 PVDGG 235
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 12-211 4.15e-37

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: 131.20  E-value: 4.15e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCD-ASVrdqrEKLIQEASSAFsGKL 90
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDeESI----KAAVKEVIERF-GRI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQ 170
Cdd:cd05374  76 DVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEA 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15239327 171 LTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEA 211
Cdd:cd05374 156 LSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPE 196
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 11-252 4.48e-37

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: 131.36  E-value: 4.48e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAClNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFSGkL 90
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKV-AEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGG-L 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVG-SIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:cd08943  79 DIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGgNIVFNASKNAVAPGPNAAAYSAAKAAEA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 170 QLTRNLACEWASDNIRTNCVAP--------WYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:cd08943 159 HLARCLALEGGEDGIRVNTVNPdavfrgskIWEGVWRAARAKAYGLLEEEYRTRNLLKREVLPEDVAEAVVAMASEDFGK 238

                       250
                ....*....|.
gi 15239327 242 ITGQVISVDGG 252
Cdd:cd08943 239 TTGAIVTVDGG 249
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 9-250 5.13e-37

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 131.28  E-value: 5.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAK-VHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK06198   4 LDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAF- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK06198  83 GRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAAYCASKG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSlVETLLEKKE------FVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:PRK06198 163 ALATLTRNAAYALLRNRIRVNGLNIGWMATE-GEDRIQREFhgapddWLEKAAATQPFGRLLDPDEVARAVAFLLSDESG 241

                        250
                 ....*....|
gi 15239327  241 YITGQVISVD 250
Cdd:PRK06198 242 LMTGSVIDFD 251
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
11-256 5.45e-37

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 131.39  E-value: 5.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKL 90
Cdd:PRK08643   2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTF-GDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVG-SIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:PRK08643  81 NVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGgKIINATSQAGVVGNPELAVYSSTKFAVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  170 QLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK------KEF---VEAVVSRTPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:PRK08643 161 GLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQvgenagKPDewgMEQFAKDITLGRLSEPEDVANCVSFLAGPDSD 240

                        250
                 ....*....|....*.
gi 15239327  241 YITGQVISVDGGFTVN 256
Cdd:PRK08643 241 YITGQTIIVDGGMVFH 256
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 9-252 6.59e-37

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 131.18  E-value: 6.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQ-EELNACLNDWKANGLVVSGsvCDASVRDQREKLiqeassafs 87
Cdd:PRK06523   7 LAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSRpDDLPEGVEFVAADLTTAEG--CAAVARAVLERL--------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNvRKPT---VEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSI-YGA 163
Cdd:PRK06523  76 GGVDILVHVLGGS-SAPAggfAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPESTTaYAA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK------------KEFVEAVVSRTPLGRVGEPEEVSSLV 231
Cdd:PRK06523 155 AKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAERlaeaagtdyegaKQIIMDSLGGIPLGRPAEPEEVAELI 234

                        250       260
                 ....*....|....*....|.
gi 15239327  232 AFLCLPASSYITGQVISVDGG 252
Cdd:PRK06523 235 AFLASDRAASITGTEYVIDGG 255
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 13-258 7.33e-37

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: 131.05  E-value: 7.33e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  13 TALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQ-EELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLN 91
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDdDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDF-GRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  92 ILINNVGTNVRKPT--VEYSSEEYAKIMSTNLESAFHLSQ------IAHPLLKASGVGSIVFISSV-AGLVHLSSGSiYG 162
Cdd:cd05337  82 CLVNNAGIAVRPRGdlLDLTEDSFDRLIAINLRGPFFLTQavarrmVEQPDRFDGPHRSIIFVTSInAYLVSPNRGE-YC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 163 ATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK-KEFVEAvvSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:cd05337 161 ISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKyDELIAA--GLVPIRRWGQPEDIAKAVRTLASGLLPY 238

                       250
                ....*....|....*..
gi 15239327 242 ITGQVISVDGGFTVNGF 258
Cdd:cd05337 239 STGQPINIDGGLSMRRL 255
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 10-252 1.07e-36

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 130.45  E-value: 1.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   10 AGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQ--EELNACLndwKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSElvHEVAAEL---RAAGGEALALTADLETYAGAQAAMAAAVEAF- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVR-KPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAglvhlsSGSI----YG 162
Cdd:PRK12823  83 GRIDVLINNVGGTIWaKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIA------TRGInrvpYS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  163 ATKGALNQLTRNLACEWASDNIRTNCVAP-----------------------WYiktslvetllekKEFVEAVVSRTPLG 219
Cdd:PRK12823 157 AAKGGVNALTASLAFEYAEHGIRVNAVAPggteapprrvprnaapqseqekaWY------------QQIVDQTLDSSLMK 224

                        250       260       270
                 ....*....|....*....|....*....|...
gi 15239327  220 RVGEPEEVSSLVAFLCLPASSYITGQVISVDGG 252
Cdd:PRK12823 225 RYGTIDEQVAAILFLASDEASYITGTVLPVGGG 257
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 12-252 1.37e-36

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: 129.70  E-value: 1.37e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKV----HTCSRNQEELNACLNDWKANGLVVSGSVCDAsvrDQREKLIQEASSAFs 87
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVvvhyNRSEAEAQRLKDELNALRNSAVLVQADLSDF---AACADLVAAAFRAF- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFIsSVAGLVHLSSGSI-YGATKG 166
Cdd:cd05357  77 GRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINI-IDAMTDRPLTGYFaYCMSKA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 167 ALNQLTRNLACEWASdNIRTNCVAPWYIktslveTLLEK--KEFVEAVVSRTPLGRVGEPEEVSSLVAFLClpASSYITG 244
Cdd:cd05357 156 ALEGLTRSAALELAP-NIRVNGIAPGLI------LLPEDmdAEYRENALRKVPLKRRPSAEEIADAVIFLL--DSNYITG 226


                ....*...
gi 15239327 245 QVISVDGG 252
Cdd:cd05357 227 QIIKVDGG 234
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 1-257 1.68e-36

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: 129.96  E-value: 1.68e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   1 METDKRWslAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQE---ELNACLNDWKANGLVVSgsVCDASVRDQREK 77
Cdd:cd08933   1 MASGLRY--ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAagqALESELNRAGPGSCKFV--PCDVTKEEDIKT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  78 LIQEASSAFsGKLNILINNVGTNV-RKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLS 156
Cdd:cd08933  77 LISVTVERF-GRIDCLVNNAGWHPpHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLSSLVGSIGQK 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 157 SGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSR----TPLGRVGEPEEVSSLVA 232
Cdd:cd08933 155 QAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATIKEgelaQLLGRMGTEAESGLAAL 234

                       250       260
                ....*....|....*....|....*
gi 15239327 233 FLCLPAsSYITGQVISVDGGFTVNG 257
Cdd:cd08933 235 FLAAEA-TFCTGIDLLLSGGAELGY 258
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 9-252 1.81e-36

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 129.65  E-value: 1.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDasvRDQREKLIQEASSAFSG 88
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSD---RDEVKALGQKAEADLEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 kLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLS-QIAHPLLKASgVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK12936  81 -VDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTrELTHPMMRRR-YGRIINITSVVGVTGNPGQANYCASKAG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEfvEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVI 247
Cdd:PRK12936 159 MIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQK--EAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTI 236


                 ....*
gi 15239327  248 SVDGG 252
Cdd:PRK12936 237 HVNGG 241
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 10-255 2.48e-36

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: 129.13  E-value: 2.48e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  10 AGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNaclndwkangLVVSGSVCDASVRDQREKLIQEASSAFSGK 89
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLK----------ELERGPGITTRVLDVTDKEQVAALAKEEGR 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  90 LNILINNVGTnVRKPTV-EYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGS-IYGATKGA 167
Cdd:cd05368  71 IDVLFNCAGF-VHHGSIlDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRfVYSTTKAA 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAV----VSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:cd05368 150 VIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEAlkafAARQPLGRLATPEEVAALAVYLASDESAYVT 229

                       250
                ....*....|..
gi 15239327 244 GQVISVDGGFTV 255
Cdd:cd05368 230 GTAVVIDGGWSL 241
PRK06949 PRK06949
SDR family oxidoreductase;
9-253 7.26e-36

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 128.34  E-value: 7.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANG---LVVSGSVCD-ASVRDQREKLIQEAss 84
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGgaaHVVSLDVTDyQSIKAAVAHAETEA-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   85 afsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ-IAHPLL-KASGVGS------IVFISSVAGLVHLS 156
Cdd:PRK06949  85 ---GTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQeVAKRMIaRAKGAGNtkpggrIINIASVAGLRVLP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  157 SGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEkKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCL 236
Cdd:PRK06949 162 QIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWE-TEQGQKLVSMLPRKRVGKPEDLDGLLLLLAA 240

                        250
                 ....*....|....*..
gi 15239327  237 PASSYITGQVISVDGGF 253
Cdd:PRK06949 241 DESQFINGAIISADDGF 257
PRK07326 PRK07326
SDR family oxidoreductase;
8-191 1.51e-35

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 127.05  E-value: 1.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVsGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVL-GLAADVRDEADVQRAVDAIVAAF- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK07326  81 GGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTNFFAGGAAYNASKFG 159

                        170       180
                 ....*....|....*....|....
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAP 191
Cdd:PRK07326 160 LVGFSEAAMLDLRQYGIKVSTIMP 183
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 12-235 2.47e-35

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: 125.94  E-value: 2.47e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDwKANGLVVSgsvCDASVRDQREKLIQEASSAFsGKLN 91
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVP---YDARDPEDARALVDALRDRF-GRID 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQL 171
Cdd:cd08932  76 VLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRAL 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15239327 172 TRNLACEWASDNIRTNCVAPWYIKTSLVEtllekkefVEAVVSRTPLGRVGEPEEVSSLVAFLC 235
Cdd:cd08932 156 AHALRQEGWDHGVRVSAVCPGFVDTPMAQ--------GLTLVGAFPPEEMIQPKDIANLVRMVI 211
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 14-254 6.12e-35

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: 125.66  E-value: 6.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSvcdASVRDQREKLIQEassafSGKLNIL 93
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRLTPLDVADA---AAVREVCSRLLAE-----HGPIDAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  94 INNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQLTR 173
Cdd:cd05331  73 VNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSK 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 174 NLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVS------RT--PLGRVGEPEEVSSLVAFLCLPASSYITGQ 245
Cdd:cd05331 153 CLGLELAPYGVRCNVVSPGSTDTAMQRTLWHDEDGAAQVIAgvpeqfRLgiPLGKIAQPADIANAVLFLASDQAGHITMH 232


                ....*....
gi 15239327 246 VISVDGGFT 254
Cdd:cd05331 233 DLVVDGGAT 241
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-253 1.11e-34

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 125.19  E-value: 1.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTR--GIGRAVVEELAKFGAKV--HTCSRNQEELNACLNDWKA---------NGLVVSGSVCDASVRDQ 74
Cdd:PRK12748   2 PLMKKIALVTGASRlnGIGAAVCRRLAAKGIDIffTYWSPYDKTMPWGMHDKEPvllkeeiesYGVRCEHMEIDLSQPYA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   75 REKLIQEASSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ--IAHPLLKASGvgSIVFISSVAGL 152
Cdd:PRK12748  82 PNRVFYAVSERL-GDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSafAKQYDGKAGG--RIINLTSGQSL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  153 VHLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPwyiktSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVA 232
Cdd:PRK12748 159 GPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNP-----GPTDTGWITEELKHHLVPKFPQGRVGEPVDAARLIA 233

                        250       260
                 ....*....|....*....|.
gi 15239327  233 FLCLPASSYITGQVISVDGGF 253
Cdd:PRK12748 234 FLVSEEAKWITGQVIHSEGGF 254
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 9-227 1.21e-34

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: 125.01  E-value: 1.21e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEEL----NACLNDWKANGLVVSGsvcDASVRDQREKLIQEASS 84
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLeevkSECLELGAPSPHVVPL---DMSDLEDAEQVVEEALK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  85 AFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGAT 164
Cdd:cd05332  78 LF-GGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAAS 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239327 165 KGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVgEPEEV 227
Cdd:cd05332 157 KHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGSMSAKMDDTTANGM-SPEEC 218
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
9-252 1.40e-34

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 125.14  E-value: 1.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEelnACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPA---RARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERF-G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ-IAHPLLKASGVGSIVFISSVAG-----LVhlssgSIYG 162
Cdd:PRK07067  80 GIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQaVARHMVEQGRGGKIINMASQAGrrgeaLV-----SHYC 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  163 ATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSL---VETLL---------EKKEFVEAVVsrtPLGRVGEPEEVSSL 230
Cdd:PRK07067 155 ATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMwdqVDALFaryenrppgEKKRLVGEAV---PLGRMGVPDDLTGM 231

                        250       260
                 ....*....|....*....|..
gi 15239327  231 VAFLCLPASSYITGQVISVDGG 252
Cdd:PRK07067 232 ALFLASADADYIVAQTYNVDGG 253
PRK12746 PRK12746
SDR family oxidoreductase;
8-253 1.53e-34

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 124.76  E-value: 1.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHT-CSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK12746   3 NLDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 -----SGKLNILINNVGTNVRKpTVEYSSEE-YAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLVHLSSGSI 160
Cdd:PRK12746  83 qirvgTSEIDILVNNAGIGTQG-TIENTTEEiFDEIMAVNIKAPFFLIQQTLPLLRAEG--RVINISSAEVRLGFTGSIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  161 YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASS 240
Cdd:PRK12746 160 YGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRNFATNSSVFGRIGQVEDIADAVAFLASSDSR 239

                        250
                 ....*....|...
gi 15239327  241 YITGQVISVDGGF 253
Cdd:PRK12746 240 WVTGQIIDVSGGF 252
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-255 1.82e-34

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 124.69  E-value: 1.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVH-TCSRNQEELNACLNDWKANG---LVVSGSVCDASvrdQREKLIQEASSAFs 87
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAiNDRPDDEELAATQQELRALGvevIFFPADVADLS---AHEAMLDAAQAAW- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINN--VGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ------IAHPLLKASGVGSIVFISSV-AGLVHLSSG 158
Cdd:PRK12745  79 GRIDCLVNNagVGVKVRGDLLDLTPESFDRVLAINLRGPFFLTQavakrmLAQPEPEELPHRSIVFVSSVnAIMVSPNRG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  159 SiYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK-KEFVEAVVsrTPLGRVGEPEEVSSLVAFLCLP 237
Cdd:PRK12745 159 E-YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAKyDALIAKGL--VPMPRWGEPEDVARAVAALASG 235

                        250
                 ....*....|....*...
gi 15239327  238 ASSYITGQVISVDGGFTV 255
Cdd:PRK12745 236 DLPYSTGQAIHVDGGLSI 253
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 12-196 5.30e-34

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: 122.62  E-value: 5.30e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANglvVSGSVCDASVRDQREKLIQEASSAFsGKLN 91
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEG---VLGLAGDVRDEADVRRAVDAMEEAF-GGLD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQL 171
Cdd:cd08929  77 ALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGL 156

                       170       180
                ....*....|....*....|....*
gi 15239327 172 TRNLACEWASDNIRTNCVAPWYIKT 196
Cdd:cd08929 157 SEAAMLDLREANIRVVNVMPGSVDT 181
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-253 5.99e-34

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 123.09  E-value: 5.99e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    7 WSLAGKTALVTGGTRGIGRAVVEELAKFGAKVhtCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK12481   4 FDLNGKVAIITGCNTGLGQGMAIGLAKAGADI--VGVGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ-IAHPLLKASGVGSIVFISSV---AGLVHLSSgsiYG 162
Cdd:PRK12481  82 -GHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQaVAKQFVKQGNGGKIINIASMlsfQGGIRVPS---YT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  163 ATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYI 242
Cdd:PRK12481 158 ASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRADTARNEAILERIPASRWGTPDDLAGPAIFLSSSASDYV 237

                        250
                 ....*....|.
gi 15239327  243 TGQVISVDGGF 253
Cdd:PRK12481 238 TGYTLAVDGGW 248
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 11-191 6.17e-34

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: 122.75  E-value: 6.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEEL----NACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLeeavEEIEAEANASGQKVSYISADLSDYEEVEQAFAQAVEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:cd08939  81 -GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKF 159

                       170       180
                ....*....|....*....|....*
gi 15239327 167 ALNQLTRNLACEWASDNIRTNCVAP 191
Cdd:cd08939 160 ALRGLAESLRQELKPYNIRVSVVYP 184
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-252 8.25e-34

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 122.76  E-value: 8.25e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDF-G 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTnVR----------KPTVEYSSEEYAKIMSTNL--------ESAFHLSQiahplLKASGVgsIVFISSVA 150
Cdd:PRK08217  82 QLNGLINNAGI-LRdgllvkakdgKVTSKMSLEQFQSVIDVNLtgvflcgrEAAAKMIE-----SGSKGV--IINISSIA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  151 glvhlSSGSI----YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLleKKEFVEAVVSRTPLGRVGEPEE 226
Cdd:PRK08217 154 -----RAGNMgqtnYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAM--KPEALERLEKMIPVGRLGEPEE 226

                        250       260
                 ....*....|....*....|....*.
gi 15239327  227 VSSLVAFLClpASSYITGQVISVDGG 252
Cdd:PRK08217 227 IAHTVRFII--ENDYVTGRVLEIDGG 250
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-253 2.89e-33

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 121.52  E-value: 2.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    7 WSLAGKTALVTGGTRGIGRAVVEELAKFGAKVhtCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK08993   6 FSLEGKVAVVTGCDTGLGQGMALGLAEAGCDI--VGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ-IAHPLLKASGVGSIVFISSV---AGLVHLSSgsiYG 162
Cdd:PRK08993  84 -GHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQaAAKHFIAQGNGGKIINIASMlsfQGGIRVPS---YT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  163 ATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYI 242
Cdd:PRK08993 160 ASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEILDRIPAGRWGLPSDLMGPVVFLASSASDYI 239

                        250
                 ....*....|.
gi 15239327  243 TGQVISVDGGF 253
Cdd:PRK08993 240 NGYTIAVDGGW 250
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-220 3.59e-33

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 120.95  E-value: 3.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK07666   4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNEL- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK07666  83 GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFG 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLV----------ETLLEKKEFVEAVVSRTPLGR 220
Cdd:PRK07666 163 VLGLTESLMQEVRKHNIRVTALTPSTVATDMAvdlgltdgnpDKVMQPEDLAEFIVAQLKLNK 225
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 9-257 1.56e-32

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 119.76  E-value: 1.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKA-NGLVVSGSVCDASVRDQREKLIQEAssafs 87
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAaHGVDVAVHALDLSSPEAREQLAAEA----- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGlVHLSSGSIYGAT-KG 166
Cdd:PRK06125  80 GDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAG-ENPDADYICGSAgNA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEA--------VVSRTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:PRK06125 159 ALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLLKGRARAELgdesrwqeLLAGLPLGRPATPEEVADLVAFLASPR 238

                        250
                 ....*....|....*....
gi 15239327  239 SSYITGQVISVDGGFTVNG 257
Cdd:PRK06125 239 SGYTSGTVVTVDGGISARG 257
PRK06128 PRK06128
SDR family oxidoreductase;
9-252 2.66e-32

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 119.96  E-value: 2.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKV-----HTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQrekLIQEAS 83
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIalnylPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQ---LVERAV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 SAFSGkLNILINNVGTNV-RKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASG----VGSIVFISSVAGLVHlssg 158
Cdd:PRK06128 130 KELGG-LDILVNIAGKQTaVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGAsiinTGSIQSYQPSPTLLD---- 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  159 siYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:PRK06128 205 --YASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLASQE 282

                        250
                 ....*....|....
gi 15239327  239 SSYITGQVISVDGG 252
Cdd:PRK06128 283 SSYVTGEVFGVTGG 296
PRK06114 PRK06114
SDR family oxidoreductase;
5-254 2.92e-32

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 118.73  E-value: 2.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    5 KRWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEE-LNACLNDWKANG---LVVSGSVCDASvrdQREKLIQ 80
Cdd:PRK06114   2 QLFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAETAEHIEAAGrraIQIAADVTSKA---DLRAAVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   81 EASSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVhLSSG-- 158
Cdd:PRK06114  79 RTEAEL-GALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGII-VNRGll 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  159 -SIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLvETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLP 237
Cdd:PRK06114 157 qAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPM-NTRPEMVHQTKLFEEQTPMQRMAKVDEMVGPAVFLLSD 235

                        250
                 ....*....|....*..
gi 15239327  238 ASSYITGQVISVDGGFT 254
Cdd:PRK06114 236 AASFCTGVDLLVDGGFV 252
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 7-256 3.01e-32

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 118.83  E-value: 3.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    7 WSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEElnaclndwkANGLVVSGSVCD----ASVRDQREKLIQEa 82
Cdd:PRK08220   4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLT---------QEDYPFATFVLDvsdaAAVAQVCQRLLAE- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   83 ssafSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYG 162
Cdd:PRK08220  74 ----TGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  163 ATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVS------RT--PLGRVGEPEEVSSLVAFL 234
Cdd:PRK08220 150 ASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLWVDEDGEQQVIAgfpeqfKLgiPLGKIARPQEIANAVLFL 229

                        250       260
                 ....*....|....*....|..
gi 15239327  235 CLPASSYITGQVISVDGGFTVN 256
Cdd:PRK08220 230 ASDLASHITLQDIVVDGGATLG 251
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-256 6.93e-32

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 117.88  E-value: 6.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKV----HTCSRNQEELNACLNDwkaNGLVVSGSVCDasvRDQREKLIQEASSAFS 87
Cdd:PRK08642   6 QTVLVTGGSRGLGAAIARAFAREGARVvvnyHQSEDAAEALADELGD---RAIALQADVTD---REQVQAMFATATEHFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNV------GTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSvaglvHLSSGSI- 160
Cdd:PRK08642  80 KPITTVVNNAladfsfDGDARKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGT-----NLFQNPVv 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  161 ----YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKT---SLVETllekKEFVEAVVSRTPLGRVGEPEEVSSLVAF 233
Cdd:PRK08642 155 pyhdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTtdaSAATP----DEVFDLIAATTPLRKVTTPQEFADAVLF 230

                        250       260
                 ....*....|....*....|...
gi 15239327  234 LCLPASSYITGQVISVDGGFTVN 256
Cdd:PRK08642 231 FASPWARAVTGQNLVVDGGLVMN 253
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 9-254 1.99e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 116.75  E-value: 1.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDwkANGLVVSGSVCDAsvrDQREKLIQEASSAFsG 88
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADE--VGGLFVPTDVTDE---DAVNALFDTAAETY-G 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGtnVRKP----TVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISS-VAGLVHLSSGSIYGA 163
Cdd:PRK06057  79 SVDIAFNNAG--ISPPeddsILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASfVAVMGSATSQISYTA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKK-EFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYI 242
Cdd:PRK06057 157 SKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKDpERAARRLVHVPMGRFAEPEEIAAAVAFLASDDASFI 236

                        250
                 ....*....|..
gi 15239327  243 TGQVISVDGGFT 254
Cdd:PRK06057 237 TASTFLVDGGIS 248
PRK07062 PRK07062
SDR family oxidoreductase;
9-253 2.24e-31

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 116.68  E-value: 2.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLND--WKANGLVVSGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARlrEKFPGARLLAARCDVLDEADVAAFAAAVEARF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGL---VHLSSGSiygA 163
Cdd:PRK07062  86 -GGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALqpePHMVATS---A 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCvapwyIKTSLVETLLEKKEFVE------------AVVSRT---PLGRVGEPEEVS 228
Cdd:PRK07062 162 ARAGLLNLVKSLATELAPKGVRVNS-----ILLGLVESGQWRRRYEAradpgqsweawtAALARKkgiPLGRLGRPDEAA 236

                        250       260
                 ....*....|....*....|....*
gi 15239327  229 SLVAFLCLPASSYITGQVISVDGGF 253
Cdd:PRK07062 237 RALFFLASPLSSYTTGSHIDVSGGF 261
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 12-252 2.35e-31

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: 116.25  E-value: 2.35e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQE-----ELNACLNDWKAngLVVSgsvCDASVRDQREKLIQEASSAF 86
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENpgaaaELQAINPKVKA--TFVQ---CDVTSWEQLAAAFKKAIEKF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  87 sGKLNILINNVGTNVRKPTVEYSSEEYA--KIMSTNLESAFHLSQIAHPLLKAS---GVGSIVFISSVAGLVHLSSGSIY 161
Cdd:cd05323  76 -GRVDILINNAGILDEKSYLFAGKLPPPweKTIDVNLTGVINTTYLALHYMDKNkggKGGVIVNIGSVAGLYPAPQFPVY 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 162 GATKGALNQLTRNLACEWASD-NIRTNCVAPWYIKTSLVETLleKKEFVEAVVSRTplgrVGEPEEVssLVAFLCLPASS 240
Cdd:cd05323 155 SASKHGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPLLPDL--VAKEAEMLPSAP----TQSPEVV--AKAIVYLIEDD 226

                       250
                ....*....|..
gi 15239327 241 YITGQVISVDGG 252
Cdd:cd05323 227 EKNGAIWIVDGG 238
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 11-252 3.31e-31

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: 115.85  E-value: 3.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQE--ELNACLNDwkaNGLVVSGSVCDAsvrDQREKLIQEASSAFsG 88
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSpgETVAKLGD---NCRFVPVDVTSE---KDVKAALALAKAKF-G 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  89 KLNILINNVGTNV------RKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKAS--------GVgsIVFISSVAGLvh 154
Cdd:cd05371  75 RLDIVVNCAGIAVaaktynKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNepdqggerGV--IINTASVAAF-- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 155 lsSGSI----YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK-KEFVEAVVSrtPLGRVGEPEEVSS 229
Cdd:cd05371 151 --EGQIgqaaYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKvRDFLAKQVP--FPSRLGDPAEYAH 226

                       250       260
                ....*....|....*....|...
gi 15239327 230 LVAFLCLpaSSYITGQVISVDGG 252
Cdd:cd05371 227 LVQHIIE--NPYLNGEVIRLDGA 247
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 12-198 3.47e-31

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: 115.03  E-value: 3.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGA-KVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKL 90
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKY-GGL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  91 NILINNVGTnVRK--PTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGlvHLSSGsiYGATKGAL 168
Cdd:cd05324  80 DILVNNAGI-AFKgfDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLG--SLTSA--YGVSKAAL 154

                       170       180       190
                ....*....|....*....|....*....|
gi 15239327 169 NQLTRNLACEWASDNIRTNCVAPWYIKTSL 198
Cdd:cd05324 155 NALTRILAKELKETGIKVNACCPGWVKTDM 184
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 76-253 4.74e-31

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: 115.37  E-value: 4.74e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  76 EKLIQEASSAFsGKLNILINN-VGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVH 154
Cdd:cd05361  60 EELVDAVLQAG-GAIDVLVSNdYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKP 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 155 LSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIK------TSLVETlleKKEFVEAVVSRTPLGRVGEPEEVS 228
Cdd:cd05361 139 LAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNsptyfpTSDWEN---NPELRERVKRDVPLGRLGRPDEMG 215

                       170       180
                ....*....|....*....|....*
gi 15239327 229 SLVAFLCLPASSYITGQVISVDGGF 253
Cdd:cd05361 216 ALVAFLASRRADPITGQFFAFAGGY 240
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 9-255 6.97e-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: 6.97e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGsvcDASVRDQREKLIQEASSAFsG 88
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEG---DVRSLADNERAVARCVERF-G 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  89 KLNILINNVG-----TNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:cd05348  78 KLDCFIGNAGiwdysTSLVDIPEEKLDEAFDELFHINVKGYILGAKAALPALYATE-GSVIFTVSNAGFYPGGGGPLYTA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 164 TKGALNQLTRNLACEWASdNIRTNCVAPWYIKTSLV--------ETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLC 235
Cdd:cd05348 157 SKHAVVGLVKQLAYELAP-HIRVNGVAPGGMVTDLRgpaslgqgETSISTPPLDDMLKSILPLGFAPEPEDYTGAYVFLA 235

                       250       260
                ....*....|....*....|.
gi 15239327 236 LPASS-YITGQVISVDGGFTV 255
Cdd:cd05348 236 SRGDNrPATGTVINYDGGMGV 256
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 8-198 9.93e-31

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: 113.94  E-value: 9.93e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKAnglvVSGSVCDASVRDQREKLIQEASSAFS 87
Cdd:cd05370   2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN----IHTIVLDVGDAESVEALAEALLSEYP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 gKLNILINNVGT----NVRKPtvEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:cd05370  78 -NLDILINNAGIqrpiDLRDP--ASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCA 154

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15239327 164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSL 198
Cdd:cd05370 155 TKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTEL 189
PRK07577 PRK07577
SDR family oxidoreductase;
12-252 1.14e-30

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 114.05  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEElnaclnDWKANGLVvsgsvCDASVRDQREKLIQEASSAFSgkLN 91
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGIARSAID------DFPGELFA-----CDLADIEQTAATLAQINEIHP--VD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSiYGATKGALNQL 171
Cdd:PRK07577  71 AIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRAIFGALDRTS-YSAAKSALVGC 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  172 TRNLACEWASDNIRTNCVAPWYIKTSL------VETLLEKKefveaVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQ 245
Cdd:PRK07577 150 TRTWALELAEYGITVNAVAPGPIETELfrqtrpVGSEEEKR-----VLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQ 224


                 ....*..
gi 15239327  246 VISVDGG 252
Cdd:PRK07577 225 VLGVDGG 231
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 9-252 1.21e-30

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: 114.64  E-value: 1.21e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDasvRDQREKLIQEASSAFsG 88
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTD---QASIDRCVAALVDRW-G 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVG-SIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:cd05363  77 SIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRGgKIINMASQAGRRGEALVGVYCATKAA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSL---VETLL---------EKKEFVEAVVsrtPLGRVGEPEEVSSLVAFLC 235
Cdd:cd05363 157 VISLTQSAGLNLIRHGINVNAIAPGVVDGEHwdgVDAKFaryenrprgEKKRLVGEAV---PFGRMGRAEDLTGMAIFLA 233

                       250
                ....*....|....*..
gi 15239327 236 LPASSYITGQVISVDGG 252
Cdd:cd05363 234 STDADYIVAQTYNVDGG 250
PRK07074 PRK07074
SDR family oxidoreductase;
12-254 2.92e-30

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 113.71  E-value: 2.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVvsGSVCD-ASVRDQREKLIQEASSAfsGKL 90
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFV--PVACDlTDAASLAAALANAAAER--GPV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGlVHLSSGSIYGATKGALNQ 170
Cdd:PRK07074  79 DVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNG-MAALGHPAYSAAKAGLIH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  171 LTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFV-EAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISV 249
Cdd:PRK07074 158 YTKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAANPQVfEELKKWYPLQDFATPDDVANAVLFLASPAARAITGVCLPV 237


                 ....*
gi 15239327  250 DGGFT 254
Cdd:PRK07074 238 DGGLT 242
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
9-253 9.63e-30

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 112.03  E-value: 9.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHT-CSRNQEELNACLNDWKANG---LVVSGSVCD-ASVRDQREKLIQEAs 83
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAgCGPNSPRRVKWLEDQKALGfdfIASEGNVGDwDSTKAAFDKVKAEV- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 safsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:PRK12938  80 ----GEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYST 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLleKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK12938 156 AKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAI--RPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFST 233

                        250
                 ....*....|
gi 15239327  244 GQVISVDGGF 253
Cdd:PRK12938 234 GADFSLNGGL 243
PRK07985 PRK07985
SDR family oxidoreductase;
9-252 1.06e-29

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 113.17  E-value: 1.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTC-----SRNQEELNACLNDWKANGLVVSGSVCDASVRdqrEKLIQEAS 83
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISylpveEEDAQDVKKIIEECGRKAVLLPGDLSDEKFA---RSLVHEAH 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 SAFSGkLNILINNVGTNVRKPTV-EYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLV---HLSSgs 159
Cdd:PRK07985 124 KALGG-LDIMALVAGKQVAIPDIaDLTSEQFQKTFAINVFALFWLTQEAIPLLPKGA--SIITTSSIQAYQpspHLLD-- 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  160 iYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPAS 239
Cdd:PRK07985 199 -YAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQES 277

                        250
                 ....*....|...
gi 15239327  240 SYITGQVISVDGG 252
Cdd:PRK07985 278 SYVTAEVHGVCGG 290
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-253 1.16e-29

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 112.19  E-value: 1.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTR--GIGRAVVEELAKFGAKV-HTCSRN-----------------QEELnaclndwKANGLVVSGSVC 67
Cdd:PRK12859   3 QLKNKVAVVTGVSRldGIGAAICKELAEAGADIfFTYWTAydkempwgvdqdeqiqlQEEL-------LKNGVKVSSMEL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   68 DASVRDQREKLIQEASSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLS-QIAHPLLKASGvGSIVFI 146
Cdd:PRK12859  76 DLTQNDAPKELLNKVTEQL-GYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSsQFARGFDKKSG-GRIINM 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  147 SSVAGLVHLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVEtllekKEFVEAVVSRTPLGRVGEPEE 226
Cdd:PRK12859 154 TSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMT-----EEIKQGLLPMFPFGRIGEPKD 228

                        250       260
                 ....*....|....*....|....*..
gi 15239327  227 VSSLVAFLCLPASSYITGQVISVDGGF 253
Cdd:PRK12859 229 AARLIKFLASEEAEWITGQIIHSEGGF 255
PRK07831 PRK07831
SDR family oxidoreductase;
9-249 1.25e-29

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 112.05  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTG--GTrGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKAN-GL-VVSGSVCDASVRDQREKLIQEASS 84
Cdd:PRK07831  15 LAGKVVLVTAaaGT-GIGSATARRALEEGARVVISDIHERRLGETADELAAElGLgRVEAVVCDVTSEAQVDALIDAAVE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   85 AFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYGA 163
Cdd:PRK07831  94 RL-GRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHgGVIVNNASVLGWRAQHGQAHYAA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPwyiktSL-VETLLEK---KEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPAS 239
Cdd:PRK07831 173 AKAGVMALTRCSALEAAEYGVRINAVAP-----SIaMHPFLAKvtsAELLDELAAREAFGRAAEPWEVANVIAFLASDYS 247

                        250
                 ....*....|
gi 15239327  240 SYITGQVISV 249
Cdd:PRK07831 248 SYLTGEVVSV 257
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 9-233 1.49e-29

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: 111.48  E-value: 1.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEAL-G 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:cd08934  80 RLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGV 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239327 169 NQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLE--KKEFVEAVVSR-TPLgrvgEPEEVSSLVAF 233
Cdd:cd08934 160 NAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHtiTKEAYEERISTiRKL----QAEDIAAAVRY 223
PRK08416 PRK08416
enoyl-ACP reductase;
11-254 3.11e-29

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 111.02  E-value: 3.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKV-HTCSRNQEELNACLNDWKAN-GLVVSGSVCDASVRDQREKLIQEASSAFSg 88
Cdd:PRK08416   8 GKTLVISGGTRGIGKAIVYEFAQSGVNIaFTYNSNVEEANKIAEDLEQKyGIKAKAYPLNILEPETYKELFKKIDEDFD- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRkPTVEysseEYAKIMS----------TNLESAFHL-SQIAHPLLKASGVGSIVFISSVAGLVHLSS 157
Cdd:PRK08416  87 RVDFFISNAIISGR-AVVG----GYTKFMRlkpkglnniyTATVNAFVVgAQEAAKRMEKVGGGSIISLSSTGNLVYIEN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  158 GSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLP 237
Cdd:PRK08416 162 YAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNYEEVKAKTEELSPLNRMGQPEDLAGACLFLCSE 241

                        250
                 ....*....|....*..
gi 15239327  238 ASSYITGQVISVDGGFT 254
Cdd:PRK08416 242 KASWLTGQTIVVDGGTT 258
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 11-255 1.36e-28

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: 108.82  E-value: 1.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVhTCSRNQEELNACLNDWKA-NGLVVSGSVCDASVRdqreKLIQEASSAFSGK 89
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKV-VFADIDEERGADFAEAEGpNLFFVHGDVADETLV----KFVVYAMLEKLGR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  90 LNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:cd09761  76 IDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAASKGGLV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 170 QLTRNLACEWASDnIRTNCVAPWYIKTSlvetllEKKEFVEAVVS-----RTPLGRVGEPEEVSSLVAFLCLPASSYITG 244
Cdd:cd09761 155 ALTHALAMSLGPD-IRVNCISPGWINTT------EQQEFTAAPLTqedhaQHPAGRVGTPKDIANLVLFLCQQDAGFITG 227

                       250
                ....*....|.
gi 15239327 245 QVISVDGGFTV 255
Cdd:cd09761 228 ETFIVDGGMTK 238
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 13-242 2.10e-28

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: 108.48  E-value: 2.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  13 TALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLNI 92
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEV-GDVTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  93 LINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQLT 172
Cdd:cd05339  80 LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 173 RNLACEWAS---DNIRTNCVAPWYIKTSLVETLLEKKEFveavvsrtpLGRVGEPEEVSSLVA--------FLCLPASSY 241
Cdd:cd05339 160 ESLRLELKAygkPGIKTTLVCPYFINTGMFQGVKTPRPL---------LAPILEPEYVAEKIVrailtnqqMLYLPFYAY 230


                .
gi 15239327 242 I 242
Cdd:cd05339 231 F 231
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 9-252 2.45e-28

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 108.62  E-value: 2.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGA--KVHTCSRnQEELNACLNDWKANGlvvsGSVCDASVRDQREKLIQEASSAF 86
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGAlvAIHYGNR-KEEAEETVYEIQSNG----GSAFSIGANLESLHGVEALYSSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 ---------SGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLVHLSS 157
Cdd:PRK12747  77 dnelqnrtgSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNS--RIINISSAATRISLPD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  158 GSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLP 237
Cdd:PRK12747 155 FIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYATTISAFNRLGEVEDIADTAAFLASP 234

                        250
                 ....*....|....*
gi 15239327  238 ASSYITGQVISVDGG 252
Cdd:PRK12747 235 DSRWVTGQLIDVSGG 249
PRK06181 PRK06181
SDR family oxidoreductase;
11-198 2.82e-28

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 108.53  E-value: 2.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKL 90
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARF-GGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEE-YAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:PRK06181  80 DILVNNAGITMWSRFDELTDLSvFERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGYAASKHALH 158

                        170       180
                 ....*....|....*....|....*....
gi 15239327  170 QLTRNLACEWASDNIRTNCVAPWYIKTSL 198
Cdd:PRK06181 159 GFFDSLRIELADDGVAVTVVCPGFVATDI 187
PLN02253 PLN02253
xanthoxin dehydrogenase
 9-254 3.94e-28

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 108.76  E-value: 3.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVhtCSRN-QEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKV--CIVDlQDDLGQNVCDSLGGEPNVCFFHCDVTVEDDVSRAVDFTVDKF- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVG------TNVRKptVEYSseEYAKIMSTNLESAF----HLSQIAHPLLKasgvGSIVFISSVAGLVHLSS 157
Cdd:PLN02253  93 GTLDIMVNNAGltgppcPDIRN--VELS--EFEKVFDVNVKGVFlgmkHAARIMIPLKK----GSIVSLCSVASAIGGLG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  158 GSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVS--RTPLGRVGE-------PEEVS 228
Cdd:PLN02253 165 PHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTEDALAgfRAFAGKNANlkgveltVDDVA 244

                        250       260
                 ....*....|....*....|....*.
gi 15239327  229 SLVAFLCLPASSYITGQVISVDGGFT 254
Cdd:PLN02253 245 NAVLFLASDEARYISGLNLMIDGGFT 270
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 9-252 9.82e-28

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 106.97  E-value: 9.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELN---ACLNDWKANGLVVSGSVCDasvRDQREKLIQEASSA 85
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDevaAEIDDLGRRALAVPTDITD---EDQCANLVALALER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FsGKLNILINNVGTN-VRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAgLVHLSSG-SIYGA 163
Cdd:PRK07890  80 F-GRVDALVNNAFRVpSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMV-LRHSQPKyGAYKM 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK---------KEFVEAVVSRTPLGRVGEPEEVSSLVAFL 234
Cdd:PRK07890 157 AKGALLAASQSLATELGPQGIRVNSVAPGYIWGDPLKGYFRHqagkygvtvEQIYAETAANSDLKRLPTDDEVASAVLFL 236

                        250
                 ....*....|....*...
gi 15239327  235 CLPASSYITGQVISVDGG 252
Cdd:PRK07890 237 ASDLARAITGQTLDVNCG 254
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 8-253 1.31e-27

(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: 106.64  E-value: 1.31e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKV---------HTCSRNQEELNACLNDWKANG---LVVSGSVCDAsvrdqr 75
Cdd:cd05353   2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVvvndlggdrKGSGKSSSAADKVVDEIKAAGgkaVANYDSVEDG------ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  76 EKLIQEASSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVhl 155
Cdd:cd05353  76 EKIVKTAIDAF-GRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLY-- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 156 ssGSI----YGATKGALNQLTRNLACEWASDNIRTNCVAPwYIKTSLVETLLeKKEFVEAVvsrtplgrvgEPEEVSSLV 231
Cdd:cd05353 153 --GNFgqanYSAAKLGLLGLSNTLAIEGAKYNITCNTIAP-AAGSRMTETVM-PEDLFDAL----------KPEYVAPLV 218

                       250       260
                ....*....|....*....|..
gi 15239327 232 AFLClPASSYITGQVISVDGGF 253
Cdd:cd05353 219 LYLC-HESCEVTGGLFEVGAGW 239
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 11-220 1.72e-27

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: 105.76  E-value: 1.72e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAC----LNDWKANGLVVsgsVCDASVRDQR-EKLIQEASSA 85
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVakeiEEKYGVETKTI---AADFSAGDDIyERIEKELEGL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  86 FSGklnILINNVGTNVRKPTV--EYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:cd05356  78 DIG---ILVNNVGISHSIPEYflETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSA 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239327 164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVE----TLLEK--KEFVEAVVSRtpLGR 220
Cdd:cd05356 155 SKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKirksSLFVPspEQFVRSALNT--LGL 215
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 9-249 1.96e-27

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: 106.38  E-value: 1.96e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRN-QEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFS 87
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTiLPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 GKLNILINNV-------GTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLsSGSI 160
Cdd:cd09763  81 GRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYL-FNVA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 161 YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTpLGRVGEPEEVS--SLVAFLCLPA 238
Cdd:cd09763 160 YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEGSWHAKERD-AFLNGETTEYSgrCVVALAADPD 238

                       250
                ....*....|.
gi 15239327 239 SSYITGQVISV 249
Cdd:cd09763 239 LMELSGRVLIT 249
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 9-246 2.24e-27

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: 105.94  E-value: 2.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLND------------WKANGLVVSGSVCDASVRDQRE 76
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDNGSAKslpgtieetaeeIEAAGGQALPIVVDVRDEDQVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  77 KLIQEASSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLS 156
Cdd:cd05338  81 ALVEATVDQF-GRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPAR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 157 SGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPwyikTSLVETLLEKKEFVEAVVSRTPlgrvgEPEEVS-SLVAFLC 235
Cdd:cd05338 160 GDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWP----STAIETPAATELSGGSDPARAR-----SPEILSdAVLAILS 230

                       250
                ....*....|.
gi 15239327 236 LPASSYiTGQV 246
Cdd:cd05338 231 RPAAER-TGLV 240
PRK09730 PRK09730
SDR family oxidoreductase;
12-252 8.96e-27

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 104.16  E-value: 8.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVH-TCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIqEASSAFSGKL 90
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAvNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMF-TAIDQHDEPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVE-YSSEEYAKIMSTNLESAF-----HLSQIAHpllKASGVG-SIVFISSVAGLVHLSSGSI-YG 162
Cdd:PRK09730  81 AALVNNAGILFTQCTVEnLTAERINRVLSTNVTGYFlccreAVKRMAL---KHGGSGgAIVNVSSAASRLGAPGEYVdYA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  163 ATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEfVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYI 242
Cdd:PRK09730 158 ASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGR-VDRVKSNIPMQRGGQPEEVAQAIVWLLSDKASYV 236

                        250
                 ....*....|
gi 15239327  243 TGQVISVDGG 252
Cdd:PRK09730 237 TGSFIDLAGG 246
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 9-252 2.96e-26

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 103.40  E-value: 2.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLV-VSGSVCDASVRDQREKLIQEASSAfs 87
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVdVSYIVADLTKREDLERTVKELKNI-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK08339  84 GEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRIS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKK---------EFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:PRK08339 164 MAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDRakregksveEALQEYAKPIPLGRLGEPEEIGYLVAFLASDL 243

                        250
                 ....*....|....
gi 15239327  239 SSYITGQVISVDGG 252
Cdd:PRK08339 244 GSYINGAMIPVDGG 257
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 9-258 4.71e-25

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: 99.71  E-value: 4.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTG--GTRGIGRAVVEELAKFGAKV---HTCSRNQEELNACLNDWKANgLVVsgsVCDASVRDQREKLIQEAS 83
Cdd:COG0623   3 LKGKRGLITGvaNDRSIAWGIAKALHEEGAELaftYQGEALKKRVEPLAEELGSA-LVL---PCDVTDDEQIDALFDEIK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  84 SAFsGKLNILINNVG----TNVRKPTVEYSSEEYAKIMSTnleSA--FH-LSQIAHPLLKASGvgSIVFISSVAGLVHLS 156
Cdd:COG0623  79 EKW-GKLDFLVHSIAfapkEELGGRFLDTSREGFLLAMDI---SAysLVaLAKAAEPLMNEGG--SIVTLTYLGAERVVP 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 157 SGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCL 236
Cdd:COG0623 153 NYNVMGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKTLAASGIPGFDKLLDYAEERAPLGRNVTIEEVGNAAAFLLS 232

                       250       260
                ....*....|....*....|..
gi 15239327 237 PASSYITGQVISVDGGFTVNGF 258
Cdd:COG0623 233 DLASGITGEIIYVDGGYHIMGM 254
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 11-199 5.96e-25

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: 99.99  E-value: 5.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGL--VVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGnaKVEVIQLDLSSLASVRQFAEEFLARF-P 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  89 KLNILINNVGTNVrkPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLV--------HLSSGS- 159
Cdd:cd05327  80 RLDILINNAGIMA--PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAgpidfndlDLENNKe 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15239327 160 -----IYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLV 199
Cdd:cd05327 158 yspykAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELL 202
PRK09186 PRK09186
flagellin modification protein A; Provisional
 8-255 7.95e-25

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 99.29  E-value: 7.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSV--CDASVRDQREKLIQEASSA 85
Cdd:PRK09186   1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLveLDITDQESLEEFLSKSAEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FsGKLNILINNV---GTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLV-----HLSS 157
Cdd:PRK09186  81 Y-GKIDGAVNCAyprNKDYGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVapkfeIYEG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  158 GSI-----YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVEtllekkEFVEAVVSRTPLGRVGEPEEVSSLVA 232
Cdd:PRK09186 160 TSMtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQPE------AFLNAYKKCCNGKGMLDPDDICGTLV 233

                        250       260
                 ....*....|....*....|...
gi 15239327  233 FLCLPASSYITGQVISVDGGFTV 255
Cdd:PRK09186 234 FLLSDQSKYITGQNIIVDDGFSL 256
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 9-175 8.02e-25

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: 99.08  E-value: 8.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAClndwKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEA----AAANPGLHTIVLDVADPASIAALAEQVTAEF-P 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  89 KLNILINNVG----TNVRKPtvEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGAT 164
Cdd:COG3967  78 DLNVLINNAGimraEDLLDE--AEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSAT 155

                       170
                ....*....|.
gi 15239327 165 KGALNQLTRNL 175
Cdd:COG3967 156 KAALHSYTQSL 166
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 12-201 9.75e-25

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: 98.89  E-value: 9.75e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVC-DASVRDQREKLIQEASSAFSgKL 90
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQlDVSDRESIEAALENLPEEFR-DI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  91 NILINNVGTNVRKPTV-EYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:cd05346  80 DILVNNAGLALGLDPAqEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVR 159

                       170       180       190
                ....*....|....*....|....*....|..
gi 15239327 170 QLTRNLACEWASDNIRTNCVAPwyiktSLVET 201
Cdd:cd05346 160 QFSLNLRKDLIGTGIRVTNIEP-----GLVET 186
PRK12742 PRK12742
SDR family oxidoreductase;
9-253 1.88e-24

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 97.91  E-value: 1.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKV---HTCSRNQEELNACLNDWKANGLvvsgsvcDASVRDQREKLIQEassa 85
Cdd:PRK12742   4 FTGKKVLVLGGSRGIGAAIVRRFVTDGANVrftYAGSKDAAERLAQETGATAVQT-------DSADRDAVIDVVRK---- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 fSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAhpLLKASGVGSIVFISSVAG-LVHLSSGSIYGAT 164
Cdd:PRK12742  73 -SGALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEA--ARQMPEGGRIIIIGSVNGdRMPVAGMAAYAAS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  165 KGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSrtpLGRVGEPEEVSSLVAFLCLPASSYITG 244
Cdd:PRK12742 150 KSALQGMARGLARDFGPRGITINVVQPGPIDTDANPANGPMKDMMHSFMA---IKRHGRPEEVAGMVAWLAGPEASFVTG 226


                 ....*....
gi 15239327  245 QVISVDGGF 253
Cdd:PRK12742 227 AMHTIDGAF 235
PRK08264 PRK08264
SDR family oxidoreductase;
8-213 2.02e-24

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 97.65  E-value: 2.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGA-KVHTCSRNQEELnaclnDWKANGLV-VSGSVCD-ASVRdqrekliqeASS 84
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGAaKVYAAARDPESV-----TDLGPRVVpLQLDVTDpASVA---------AAA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   85 AFSGKLNILINNVGTNVRKPTVEYSSEEYAK-IMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:PRK08264  69 EAASDVTILVNNAGIFRTGSLLLEGDEDALRaEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSA 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVV 213
Cdd:PRK08264 149 SKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAGLDAPKASPADVA 198
PRK06123 PRK06123
SDR family oxidoreductase;
12-252 2.37e-24

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 97.93  E-value: 2.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFG-AKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKL 90
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGyAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDREL-GRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEY-SSEEYAKIMSTNLESAFHLSQIA----HPLLKASGvGSIVFISSVAGLVHLSSGSI-YGAT 164
Cdd:PRK06123  82 DALVNNAGILEAQMRLEQmDAARLTRIFATNVVGSFLCAREAvkrmSTRHGGRG-GAIVNVSSMAARLGSPGEYIdYAAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  165 KGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEfVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITG 244
Cdd:PRK06123 161 KGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGR-VDRVKAGIPMGRGGTAEEVARAILWLLSDEASYTTG 239


                 ....*...
gi 15239327  245 QVISVDGG 252
Cdd:PRK06123 240 TFIDVSGG 247
PRK07201 PRK07201
SDR family oxidoreductase;
4-223 4.12e-24

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 101.18  E-value: 4.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    4 DKRWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEAS 83
Cdd:PRK07201 364 DLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDIL 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 SAFsGKLNILINNVGTNVRKpTVEYSSE---EYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSI 160
Cdd:PRK07201 444 AEH-GHVDYLVNNAGRSIRR-SVENSTDrfhDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNAPRFSA 521

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  161 YGATKGALNQLTRNLACEWASDNI----------RTNCVAPWYIKTSlVETLLEKKE---FVEAVVSR-----TPLGRVG 222
Cdd:PRK07201 522 YVASKAALDAFSDVAASETLSDGItfttihmplvRTPMIAPTKRYNN-VPTISPEEAadmVVRAIVEKpkridTPLGTFA 600


                 .
gi 15239327  223 E 223
Cdd:PRK07201 601 E 601
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 6-231 7.91e-24

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: 96.43  E-value: 7.91e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   6 RWSlaGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWK-ANGLVVSGSVCDASVRDQREKLIQEASS 84
Cdd:cd05343   3 RWR--GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQsAGYPTLFPYQCDLSNEEQILSMFSAIRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  85 AFSGkLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV--GSIVFISSVAG--LVHLSSGSI 160
Cdd:cd05343  81 QHQG-VDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSMSGhrVPPVSVFHF 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15239327 161 YGATKGALNQLTRNLACE--WASDNIRTNCVAPWYIKTSLVETLLEKK-EFVEAVVSRTPlgrVGEPEEVSSLV 231
Cdd:cd05343 160 YAATKHAVTALTEGLRQElrEAKTHIRATSISPGLVETEFAFKLHDNDpEKAAATYESIP---CLKPEDVANAV 230
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 13-253 8.26e-24

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: 96.41  E-value: 8.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  13 TALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNaclndwkanglvvsgsvCDASVRDQREKLIQEASSAFSGKLNI 92
Cdd:cd05328   1 TIVITGAASGIGAATAELLEDAGHTVIGIDLREADVI-----------------ADLSTPEGRAAAIADVLARCSGVLDG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  93 LINNVGTNVRKPTVEysseeyakIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAG---------LVHLSSGS---- 159
Cdd:cd05328  64 LVNCAGVGGTTVAGL--------VLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGagwaqdkleLAKALAAGtear 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 160 --------------IYGATKGALNQLTRNLACEWASD-NIRTNCVAPWYIKTSLVETLLEKKEFVEAVVS-RTPLGRVGE 223
Cdd:cd05328 136 avalaehagqpgylAYAGSKEALTVWTRRRAATWLYGaGVRVNTVAPGPVETPILQAFLQDPRGGESVDAfVTPMGRRAE 215

                       250       260       270
                ....*....|....*....|....*....|
gi 15239327 224 PEEVSSLVAFLCLPASSYITGQVISVDGGF 253
Cdd:cd05328 216 PDEIAPVIAFLASDAASWINGANLFVDGGL 245
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 11-252 1.39e-23

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 95.87  E-value: 1.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAC---LNDWKANGLVVsGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVaqeINAEYGEGMAY-GFGADATSEQSVLALSRGVDEIF- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK12384  80 GRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAKF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPW-YIKTSLVETLLE--------KKEFVEAV-VSRTPLGRVGEPEEVSSLVAFLCL 236
Cdd:PRK12384 160 GGVGLTQSLALDLAEYGITVHSLMLGnLLKSPMFQSLLPqyakklgiKPDEVEQYyIDKVPLKRGCDYQDVLNMLLFYAS 239

                        250
                 ....*....|....*.
gi 15239327  237 PASSYITGQVISVDGG 252
Cdd:PRK12384 240 PKASYCTGQSINVTGG 255
PRK07041 PRK07041
SDR family oxidoreductase;
15-252 1.71e-23

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 95.10  E-value: 1.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   15 LVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVcDASVRDQREKLIQEAssafsGKLNILI 94
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPVRTAAL-DITDEAAVDAFFAEA-----GPFDHVV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   95 NNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHpllKASGvGSIVFISSVAGLVHLSSGSIYGATKGALNQLTRN 174
Cdd:PRK07041  75 ITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAAR---IAPG-GSLTFVSGFAAVRPSASGVLQGAINAALEALARG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  175 LACEWASdnIRTNCVAPWYIKTSLVETLLE--KKEFVEAVVSRTPLGRVGEPEEVSSLVAFLClpASSYITGQVISVDGG 252
Cdd:PRK07041 151 LALELAP--VRVNTVSPGLVDTPLWSKLAGdaREAMFAAAAERLPARRVGQPEDVANAILFLA--ANGFTTGSTVLVDGG 226
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 14-200 3.02e-23

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: 94.70  E-value: 3.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFSGkLNIL 93
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGG-LDLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  94 INNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQLTR 173
Cdd:cd05350  80 IINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAE 159

                       170       180
                ....*....|....*....|....*..
gi 15239327 174 NLACEWASDNIRTNCVAPWYIKTSLVE 200
Cdd:cd05350 160 SLRYDVKKRGIRVTVINPGFIDTPLTA 186
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 14-198 3.43e-23

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: 94.28  E-value: 3.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  14 ALVTGGTRGIGRAVVEELAKFG-AKVHTCSRNQEELNAcLNDWKANGLVVSgsVCDASVRDQREKLIQEASSAF-SGKLN 91
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATE-LAALGASHSRLH--ILELDVTDEIAESAEAVAERLgDAGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  92 ILINNVGT-NVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAG---LVHLSSGSIYGATKGA 167
Cdd:cd05325  78 VLINNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsigDNTSGGWYSYRASKAA 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 15239327 168 LNQLTRNLACEWASDNIRtnCVA--PWYIKTSL 198
Cdd:cd05325 158 LNMLTKSLAVELKRDGIT--VVSlhPGWVRTDM 188
PRK06947 PRK06947
SDR family oxidoreductase;
12-252 1.83e-22

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 92.56  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVH-TCSRNQ---EELNACLNDWKANGLVVSGSVCDASvrdQREKLIQEASSAFs 87
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGiNYARDAaaaEETADAVRAAGGRACVVAGDVANEA---DVIAMFDAVQSAF- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVG-TNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKAS---GVGSIVFISSVAGLVhlssGSI--- 160
Cdd:PRK06947  79 GRLDALVNNAGiVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrggRGGAIVNVSSIASRL----GSPney 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  161 --YGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSlVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:PRK06947 155 vdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETE-IHASGGQPGRAARLGAQTPLGRAGEADEVAETIVWLLSDA 233

                        250
                 ....*....|....
gi 15239327  239 SSYITGQVISVDGG 252
Cdd:PRK06947 234 ASYVTGALLDVGGG 247
PRK09134 PRK09134
SDR family oxidoreductase;
12-252 2.64e-22

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 92.30  E-value: 2.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAK--FGAKVHtCSRNQEELNACLNDWKANG---LVVSgsvCDASVRDQREKLIQEASSAF 86
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAhgFDVAVH-YNRSRDEAEALAAEIRALGrraVALQ---ADLADEAEVRALVARASAAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 sGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIV-------------FISsvaglv 153
Cdd:PRK09134  86 -GPITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVnmidqrvwnlnpdFLS------ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  154 hlssgsiYGATKGALNQLTRNLACEWASDnIRTNCVAPwyiKTSLVETLLEKKEFvEAVVSRTPLGRVGEPEEVSSLVAF 233
Cdd:PRK09134 159 -------YTLSKAALWTATRTLAQALAPR-IRVNAIGP---GPTLPSGRQSPEDF-ARQHAATPLGRGSTPEEIAAAVRY 226

                        250       260
                 ....*....|....*....|
gi 15239327  234 L-CLPAssyITGQVISVDGG 252
Cdd:PRK09134 227 LlDAPS---VTGQMIAVDGG 243
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 11-257 2.87e-22

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: 92.26  E-value: 2.87e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTG--GTRGIGRAVVEELAKFGAKV---HTCSRNQEELNACLNDWKANGLVVsgsVCDASVRDQREKLIQEASSA 85
Cdd:cd05372   1 GKRILITGiaNDRSIAWGIAKALHEAGAELaftYQPEALRKRVEKLAERLGESALVL---PCDVSNDEEIKELFAEVKKD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  86 FsGKLNILINNVG----TNVRKPTVEYSSEEYAKIMSTnleSAFHLSQIAHPLLK--ASGvGSIVFISSVAGLVHLSSGS 159
Cdd:cd05372  78 W-GKLDGLVHSIAfapkVQLKGPFLDTSRKGFLKALDI---SAYSLVSLAKAALPimNPG-GSIVTLSYLGSERVVPGYN 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 160 IYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKT------SLVETLLEkkeFVEAvvsRTPLGRVGEPEEVSSLVAF 233
Cdd:cd05372 153 VMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTlaasgiTGFDKMLE---YSEQ---RAPLGRNVTAEEVGNTAAF 226

                       250       260
                ....*....|....*....|....
gi 15239327 234 LCLPASSYITGQVISVDGGFTVNG 257
Cdd:cd05372 227 LLSDLSSGITGEIIYVDGGYHIMG 250
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-252 3.21e-22

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 93.31  E-value: 3.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKV----HTCSRNQEELNACLNDWKANGLVVSGSVCDasvRDQREKLIQEAS 83
Cdd:PRK07792   9 DLSGKVAVVTGAAAGLGRAEALGLARLGATVvvndVASALDASDVLDEIRAAGAKAVAVAGDISQ---RATADELVATAV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 SAfsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIA----HPLLKASG---VGSIVFISSVAGLVHLS 156
Cdd:PRK07792  86 GL--GGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAaaywRAKAKAAGgpvYGRIVNTSSEAGLVGPV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  157 SGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPwYIKTSLVETLLEKKEFVEAvVSRTPLGrvgePEEVSSLVAFLCL 236
Cdd:PRK07792 164 GQANYGAAKAGITALTLSAARALGRYGVRANAICP-RARTAMTADVFGDAPDVEA-GGIDPLS----PEHVVPLVQFLAS 237

                        250
                 ....*....|....*.
gi 15239327  237 PASSYITGQVISVDGG 252
Cdd:PRK07792 238 PAAAEVNGQVFIVYGP 253
PRK08267 PRK08267
SDR family oxidoreductase;
12-200 4.60e-22

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 91.92  E-value: 4.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSgsVCDASVRDQREKLIQEASSAFSGKLN 91
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAWTG--ALDVTDRAAWDAALADFAAATGGRLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASgVGSIVF-ISSVAGLVHLSSGSIYGATKGALNQ 170
Cdd:PRK08267  80 VLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKAT-PGARVInTSSASAIYGQPGLAVYSATKFAVRG 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 15239327  171 LTRNLACEWASDNIRTNCVAPWYIKTSLVE 200
Cdd:PRK08267 159 LTEALDLEWRRHGIRVADVMPLFVDTAMLD 188
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 11-200 4.82e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 92.02  E-value: 4.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDasvRDQREKLIQEASSAFsGKL 90
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTD---RAAVFAAVETAVEHF-GRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQ 170
Cdd:PRK08263  79 DIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEG 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 15239327  171 LTRNLACEwasdnirtncVAPWYIKTSLVE 200
Cdd:PRK08263 159 MSEALAQE----------VAEFGIKVTLVE 178
PRK09072 PRK09072
SDR family oxidoreductase;
9-198 5.14e-22

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 91.93  E-value: 5.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSgSVCDASVRDQREKLIQEASSAfsG 88
Cdd:PRK09072   3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHRW-VVADLTSEAGREAVLARAREM--G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:PRK09072  80 GINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFAL 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 15239327  169 NQLTRNLACEWASDNIRTNCVAPWYIKTSL 198
Cdd:PRK09072 160 RGFSEALRRELADTGVRVLYLAPRATRTAM 189
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 13-191 1.26e-21

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: 90.42  E-value: 1.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  13 TALVTGGTRGIGRAVVEELAK--FGAKVHTCSRNQEELNACLNDwKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKL 90
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKrgSPSVVVLLARSEEPLQELKEE-LRPGLRVTTVKADLSDAAGVEQLLEAIRKLD-GER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  91 NILINNVGT-NVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:cd05367  79 DLLINNAGSlGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAAR 158

                       170       180
                ....*....|....*....|...
gi 15239327 169 NQLTRNLACEwaSDNIRTNCVAP 191
Cdd:cd05367 159 DMFFRVLAAE--EPDVRVLSYAP 179
PRK12744 PRK12744
SDR family oxidoreductase;
8-254 1.33e-21

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 90.57  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAK---VHTCS-RNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEAS 83
Cdd:PRK12744   5 SLKGKVVLIAGGAKNLGGLIARDLAAQGAKavaIHYNSaASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 SAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASgvGSIVFIssVAGLVHLSSG--SIY 161
Cdd:PRK12744  85 AAF-GRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDN--GKIVTL--VTSLLGAFTPfySAY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  162 GATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLV---ETlLEKKEFVEAVVSRTPLGRVG--EPEEVSSLVAFLcL 236
Cdd:PRK12744 160 AGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFFypqEG-AEAVAYHKTAAALSPFSKTGltDIEDIVPFIRFL-V 237

                        250
                 ....*....|....*...
gi 15239327  237 PASSYITGQVISVDGGFT 254
Cdd:PRK12744 238 TDGWWITGQTILINGGYT 255
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 12-198 1.34e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 90.73  E-value: 1.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAclndwkANGlvVSGSVCD----ASVRDQREKLIQEAssafs 87
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAP------IPG--VELLELDvtddASVQAAVDEVIARA----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK06179  72 GRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHA 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSL 198
Cdd:PRK06179 152 VEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 11-200 1.44e-21

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: 90.16  E-value: 1.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGA-KVHTCSRNQEELnACLNDWKANGLVVsgsvCDASVRDQREklIQEASSAFSgK 89
Cdd:cd05354   3 DKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSA-AHLVAKYGDKVVP----LRLDVTDPES--IKAAAAQAK-D 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  90 LNILINNVGTNVRKPTVEYSSEEYAKI-MSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:cd05354  75 VDVVINNAGVLKPATLLEEGALEALKQeMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAA 154

                       170       180       190
                ....*....|....*....|....*....|..
gi 15239327 169 NQLTRNLACEWASDNIRTNCVAPWYIKTSLVE 200
Cdd:cd05354 155 YSLTQGLRAELAAQGTLVLSVHPGPIDTRMAA 186
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 9-245 1.97e-21

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: 89.56  E-value: 1.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANG------LVVSGSVCDAsvrDQREKLIQEA 82
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGgrqpqwFILDLLTCTS---ENCQQLAQRI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  83 SSAFsGKLNILINNVG-TNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIY 161
Cdd:cd05340  79 AVNY-PRLDGVLHNAGlLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAY 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 162 GATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVetllekkefVEAVVSRTPLgRVGEPEEVSSLVAFLCLPASSY 241
Cdd:cd05340 158 AVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMR---------ASAFPTEDPQ-KLKTPADIMPLYLWLMGDDSRR 227


                ....
gi 15239327 242 ITGQ 245
Cdd:cd05340 228 KTGM 231
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-251 1.08e-20

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 90.67  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVhTC---SRNQEELNACLNDwkanglvVSGS--VCDASVRDQREKLIqEAS 83
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHV-VCldvPAAGEALAAVANR-------VGGTalALDITAPDAPARIA-EHL 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 SAFSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFhlsQIAHPLLKASGV---GSIVFISSVAGLvhlsSG-- 158
Cdd:PRK08261 279 AERHGGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPL---RITEALLAAGALgdgGRIVGVSSISGI----AGnr 351

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  159 --SIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVetllEKKEFVEAVVSR--TPLGRVGEPEEVSSLVAFL 234
Cdd:PRK08261 352 gqTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMT----AAIPFATREAGRrmNSLQQGGLPVDVAETIAWL 427

                        250
                 ....*....|....*..
gi 15239327  235 CLPASSYITGQVISVDG 251
Cdd:PRK08261 428 ASPASGGVTGNVVRVCG 444
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 12-231 1.14e-20

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: 87.51  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSgsVCDASVRDQREKLIQEASSAFSGKLN 91
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVVAG--ALDVTDRAAWAAALADFAAATGGRLD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQL 171
Cdd:cd08931  79 ALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGL 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 172 TRNLACEWASDNIRTNCVAPWYIKTSLVETllekkeFVEAVVSRTPLGRVGEPEEVSSLV 231
Cdd:cd08931 159 TEALDVEWARHGIRVADVWPWFVDTPILTK------GETGAAPKKGLGRVLPVSDVAKVV 212
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 9-199 1.16e-20

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 88.47  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK05876   4 FPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLL-G 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHP-LLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK05876  83 HVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYG 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLV 199
Cdd:PRK05876 163 VVGLAETLAREVTADGIGVSVLCPMVVETNLV 194
PRK05717 PRK05717
SDR family oxidoreductase;
11-254 1.27e-19

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 85.33  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDasvRDQREKLIQEASSAFsGKL 90
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVAD---EAQVAAGVAEVLGQF-GRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVG-TNVRKPTVE-YSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:PRK05717  86 DALVCNAAiADPHNTTLEsLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSEPDTEAYAASKGGL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  169 NQLTRNLACEWASDnIRTNCVAPWYIKTSlVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVIS 248
Cdd:PRK05717 165 LALTHALAISLGPE-IRVNAVSPGWIDAR-DPSQRRAEPLSEADHAQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFV 242


                 ....*.
gi 15239327  249 VDGGFT 254
Cdd:PRK05717 243 VDGGMT 248
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
9-258 1.75e-19

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 84.77  E-value: 1.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTG--GTRGIGRAVVEELAKFGAKVHTC------SRNQ---EELNACLNDwkanGLVVSgsvCDASVRDQREK 77
Cdd:PRK07370   4 LTGKKALVTGiaNNRSIAWGIAQQLHAAGAELGITylpdekGRFEkkvRELTEPLNP----SLFLP---CDVQDDAQIEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   78 LIQEASSAFsGKLNILINNVG-TNVRKPTVEYS---SEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLV 153
Cdd:PRK07370  77 TFETIKQKW-GKLDILVHCLAfAGKEELIGDFSatsREGFARALEISAYSLAPLCKAAKPLMSEGG--SIVTLTYLGGVR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  154 HLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKT---SLVETLLEKKEFVEAVvsrTPLGRVGEPEEVSSL 230
Cdd:PRK07370 154 AIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTlasSAVGGILDMIHHVEEK---APLRRTVTQTEVGNT 230

                        250       260
                 ....*....|....*....|....*...
gi 15239327  231 VAFLCLPASSYITGQVISVDGGFTVNGF 258
Cdd:PRK07370 231 AAFLLSDLASGITGQTIYVDAGYCIMGM 258
PRK07454 PRK07454
SDR family oxidoreductase;
12-242 2.13e-19

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 84.24  E-value: 2.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLN 91
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQF-GCPD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQL 171
Cdd:PRK07454  86 VLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAF 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239327  172 TRNLACEWASDNIRTNCVAPWYIKTSLVETllekkEFVEAVVSRTPLGRvgePEEVSSLVAFLC-LPASSYI 242
Cdd:PRK07454 166 TKCLAEEERSHGIRVCTITLGAVNTPLWDT-----ETVQADFDRSAMLS---PEQVAQTILHLAqLPPSAVI 229
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 14-255 8.23e-19

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: 83.44  E-value: 8.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEE----LNACLNDWKAN-GLVVSGSVCDASVRDQR-EKLIQEASSAFs 87
Cdd:TIGR02685   4 AVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAaastLAAELNARRPNsAVTCQADLSNSATLFSRcEAIIDACFRAF- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    88 GKLNILINNVGTNVRKPTVEYSSEEY---AKIMSTNLESAFHLSQIAHPLL------KASGVG--------SIVFISSVA 150
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPLLRGDAGEGvgdKKSLEVQVAELFGSNAIAPYFLikafaqRQAGTRaeqrstnlSIVNLCDAM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   151 GLVHLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPwyiKTSLVETLLEKKEfVEAVVSRTPLG-RVGEPEEVSS 229
Cdd:TIGR02685 163 TDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAP---GLSLLPDAMPFEV-QEDYRRKVPLGqREASAEQIAD 238

                         250       260
                  ....*....|....*....|....*.
gi 15239327   230 LVAFLCLPASSYITGQVISVDGGFTV 255
Cdd:TIGR02685 239 VVIFLVSPKAKYITGTCIKVDGGLSL 264
PRK08340 PRK08340
SDR family oxidoreductase;
15-254 1.46e-18

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 82.55  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   15 LVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVcDASVRDQREKLIQEASSAFsGKLNILI 94
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGEVYAVKA-DLSDKDDLKNLVKEAWELL-GGIDALV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   95 NNVGtNVRkptVEYSSEEYAKIMSTNLESAFHL-------SQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK08340  82 WNAG-NVR---CEPCMLHEAGYSDWLEAALLHLvapgyltTLLIQAWLEKKMKGVLVYLSSVSVKEPMPPLVLADVTRAG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEK------KEFVEA----VVSRTPLGRVGEPEEVSSLVAFLCLP 237
Cdd:PRK08340 158 LVQLAKGVSRTYGGKGIRAYTVLLGSFDTPGARENLARiaeergVSFEETwereVLERTPLKRTGRWEELGSLIAFLLSE 237

                        250
                 ....*....|....*..
gi 15239327  238 ASSYITGQVISVDGGFT 254
Cdd:PRK08340 238 NAEYMLGSTIVFDGAMT 254
PRK05650 PRK05650
SDR family oxidoreductase;
15-202 2.11e-18

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 82.01  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   15 LVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKA---NGLVVSgsvCDASVRDQREKLIQEASSAFSGkLN 91
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREaggDGFYQR---CDVRDYSQLTALAQACEEKWGG-ID 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQL 171
Cdd:PRK05650  80 VIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVAL 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15239327  172 TRNLACEWASDNIRTNCVAPWYIKTSLVETL 202
Cdd:PRK05650 160 SETLLVELADDEIGVHVVCPSFFQTNLLDSF 190
PRK05866 PRK05866
SDR family oxidoreductase;
9-191 7.40e-18

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 80.94  E-value: 7.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRI-G 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEySSE---EYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSG-SIYGAT 164
Cdd:PRK05866 117 GVDILINNAGRSIRRPLAE-SLDrwhDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATWGVLSEASPLfSVYNAS 195

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15239327  165 KGALNQLTRNLACEWASDNI----------RTNCVAP 191
Cdd:PRK05866 196 KAALSAVSRVIETEWGDRGVhsttlyyplvATPMIAP 232
PRK06182 PRK06182
short chain dehydrogenase; Validated
 12-200 1.12e-17

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 80.00  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNaclnDWKANGL-VVSGSVCDASVRDQREKLIQEASsafsGKL 90
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKME----DLASLGVhPLSLDVTDEASIKAAVDTIIAEE----GRI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALnq 170
Cdd:PRK06182  76 DVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFAL-- 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 15239327  171 ltrnlacEWASDNIRTNcVAPWYIKTSLVE 200
Cdd:PRK06182 154 -------EGFSDALRLE-VAPFGIDVVVIE 175
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 9-252 1.23e-17

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 80.10  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKV---------HTCSRNQEELNACLNDWKANG--LVVSGSvcDASVRDQREK 77
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVvvndigvglDGSASGGSAAQAVVDEIVAAGgeAVANGD--DIADWDGAAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   78 LIQEASSAFsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKA-SGVG-----SIVFISSVAG 151
Cdd:PRK07791  82 LVDAAVETF-GGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRAeSKAGravdaRIINTSSGAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  152 LvhlsSGSI----YGATKGALNQLTRNLACEWASDNIRTNCVAPwYIKTSLVETllekkefVEAVVSRTPLGrvGE---- 223
Cdd:PRK07791 161 L----QGSVgqgnYSAAKAGIAALTLVAAAELGRYGVTVNAIAP-AARTRMTET-------VFAEMMAKPEE--GEfdam 226

                        250       260       270
                 ....*....|....*....|....*....|
gi 15239327  224 -PEEVSSLVAFLCLPASSYITGQVISVDGG 252
Cdd:PRK07791 227 aPENVSPLVVWLGSAESRDVTGKVFEVEGG 256
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 9-252 1.28e-17

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 79.42  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELnACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFSG 88
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKL-KRMKKTLSKYGNIHYVVGDVSSTESARNVIEKAAKVLNA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 kLNILINNVGTNVRKPTVEYSSEEyaKIMSTNLESAFHLSQIAHPLLKASgvGSIVFISSVAGL-----VHLSsgsiYGA 163
Cdd:PRK05786  82 -IDGLVVTVGGYVEDTVEEFSGLE--EMLTNHIKIPLYAVNASLRFLKEG--SSIVLVSSMSGIykaspDQLS----YAV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKefveavvsRTPLGRVGE-PEEVSSLVAFLCLPASSYI 242
Cdd:PRK05786 153 AKAGLAKAVEILASELLGRGIRVNGIAPTTISGDFEPERNWKK--------LRKLGDDMApPEDFAKVIIWLLTDEADWV 224

                        250
                 ....*....|
gi 15239327  243 TGQVISVDGG 252
Cdd:PRK05786 225 DGVVIPVDGG 234
PRK06194 PRK06194
hypothetical protein; Provisional
 9-200 1.54e-17

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 80.06  E-value: 1.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsG 88
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERF-G 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASG------VGSIVFISSVAGLVHLSSGSIYG 162
Cdd:PRK06194  83 AVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAekdpayEGHIVNTASMAGLLAPPAMGIYN 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15239327  163 ATKGALNQLTRNL--ACEWASDNIRTNCVAPWYIKTSLVE 200
Cdd:PRK06194 163 VSKHAVVSLTETLyqDLSLVTDQVGASVLCPYFVPTGIWQ 202
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 11-252 1.88e-17

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: 79.43  E-value: 1.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKAN-GLVVSGSVCDASVRDQREKLIQEASSAFsGK 89
Cdd:cd05322   2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEyGEKAYGFGADATNEQSVIALSKGVDEIF-KR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  90 LNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:cd05322  81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAKFGG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 169 NQLTRNLACEWASDNIRTNCVAPW-YIKTSLVETLLE--------KKEFVEAV-VSRTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:cd05322 161 VGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQSLLPqyakklgiKESEVEQYyIDKVPLKRGCDYQDVLNMLLFYASPK 240

                       250
                ....*....|....
gi 15239327 239 SSYITGQVISVDGG 252
Cdd:cd05322 241 ASYCTGQSINITGG 254
PRK07832 PRK07832
SDR family oxidoreductase;
12-201 8.22e-17

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 77.78  E-value: 8.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVC-DASVRDQREKLIQEASSAFsGKL 90
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRAlDISDYDAVAAFAADIHAAH-GSM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQ-IAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:PRK07832  80 DVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIEtFVPPMVAAGRGGHLVNVSSAAGLVALPWHAAYSASKFGLR 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15239327  170 QLTRNLACEWASDNIRTNCVAPWYIKTSLVET 201
Cdd:PRK07832 160 GLSEVLRFDLARHGIGVSVVVPGAVKTPLVNT 191
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 9-191 9.97e-17

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 77.22  E-value: 9.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSV-CD---ASVRDQREkLIQEASS 84
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIpLDlltATPQNYQQ-LADTIEE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   85 AFsGKLNILINNVGT-NVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:PRK08945  89 QF-GRLDGVLHNAGLlGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYAV 167

                        170       180
                 ....*....|....*....|....*...
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAP 191
Cdd:PRK08945 168 SKFATEGMMQVLADEYQGTNLRVNCINP 195
PRK08703 PRK08703
SDR family oxidoreductase;
8-191 1.96e-16

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 76.12  E-value: 1.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDwkangLVVSGSVCDASVR--------DQREKLI 79
Cdd:PRK08703   3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDA-----IVEAGHPEPFAIRfdlmsaeeKEFEQFA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   80 QEASSAFSGKLNILINNVGT-NVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSG 158
Cdd:PRK08703  78 ATIAEATQGKLDGIVHCAGYfYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYW 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 15239327  159 SIYGATKGALNQLTRNLACEWAS-DNIRTNCVAP 191
Cdd:PRK08703 158 GGFGASKAALNYLCKVAADEWERfGNLRANVLVP 191
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 16-183 2.11e-16

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: 75.88  E-value: 2.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  16 VTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLNILIN 95
Cdd:cd05360   5 ITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERF-GRIDTWVN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  96 NVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQLTRNL 175
Cdd:cd05360  84 NAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESL 163


                ....*...
gi 15239327 176 ACEWASDN 183
Cdd:cd05360 164 RAELAHDG 171
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 13-184 3.15e-16

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: 75.50  E-value: 3.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  13 TALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLND-WKANGLVVSGSVCDASVRDQREKLIQEASSAFsGKLN 91
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDiIRDAGGSAKAVPTDARDEDEVIALFDLIEEEI-GPLE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQL 171
Cdd:cd05373  80 VLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRAL 159

                       170
                ....*....|...
gi 15239327 172 TRNLACEWASDNI 184
Cdd:cd05373 160 AQSMARELGPKGI 172
PRK06914 PRK06914
SDR family oxidoreductase;
10-201 4.86e-16

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 75.83  E-value: 4.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   10 AGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQRE-KLIQEASSAFsG 88
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQQNIKVQQLDVTDQNSiHNFQLVLKEI-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYAL 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15239327  169 NQLTRNLACEWASDNIRTNCVAPWYIKTSLVET 201
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEPGSYNTNIWEV 193
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
67-255 5.14e-16

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 75.36  E-value: 5.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   67 CDASVRDQREKLIQEASSAFsGKLNILINNVGTNVRK----PTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgS 142
Cdd:PRK07533  67 LDVREPGQLEAVFARIAEEW-GRLDFLLHSIAFAPKEdlhgRVVDCSREGFALAMDVSCHSFIRMARLAEPLMTNGG--S 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  143 IVFISSVAGLVHLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVG 222
Cdd:PRK07533 144 LLTMSYYGAEKVVENYNLMGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKTRAASGIDDFDALLEDAAERAPLRRLV 223

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15239327  223 EPEEVSSLVAFLCLPASSYITGQVISVDGGFTV 255
Cdd:PRK07533 224 DIDDVGAVAAFLASDAARRLTGNTLYIDGGYHI 256
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 12-254 1.34e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 74.29  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAkFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAfsGKLN 91
Cdd:PRK06940   2 KEVVVVIGAGGIGQAIARRVG-AGKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQTL--GPVT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   92 ILINNVGTNVRKPTVE-------YSS----EEYAKIMstnlesafhlsqiahpllkASGvGSIVFISSVAG--------- 151
Cdd:PRK06940  79 GLVHTAGVSPSQASPEailkvdlYGTalvlEEFGKVI-------------------APG-GAGVVIASQSGhrlpaltae 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  152 ------------LVHL---------SSGSIYGATKGAlNQL-TRNLACEWASDNIRTNCVAPWYIKTSLVETLL--EKKE 207
Cdd:PRK06940 139 qeralattpteeLLSLpflqpdaieDSLHAYQIAKRA-NALrVMAEAVKWGERGARINSISPGIISTPLAQDELngPRGD 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 15239327  208 FVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVDGGFT 254
Cdd:PRK06940 218 GYRNMFAKSPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVDGGAT 264
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 8-227 1.65e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 74.21  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWkanGLVVSGSVcDASVRDQREKLIQEASSAFs 87
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL---GLVVGGPL-DVTDPASFAAFLDAVEADL- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK07825  77 GPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLvetllekkefveavVSRTPLG---RVGEPEEV 227
Cdd:PRK07825 157 VVGFTDAARLELRGTGVHVSVVLPSFVNTEL--------------IAGTGGAkgfKNVEPEDV 205
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 11-251 3.83e-15

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: 72.36  E-value: 3.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVhtCSRNQ---EELNACLNdwkanglvvsgsVCDASVRDQREKLIQEASSAFS 87
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFKSRGWWV--ASIDLaenEEADASII------------VLDSDSFTEQAKQVVASVARLS 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 GKLNILINNVGTNVRKPTVEYSSEEYAKIM-STNLESAFHLSQIAHPLLKASGVgsIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:cd05334  67 GKVDALICVAGGWAGGSAKSKSFVKNWDLMwKQNLWTSFIASHLATKHLLSGGL--LVLTGAKAALEPTPGMIGYGAAKA 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327 167 ALNQLTRNLACEW--ASDNIRTNCVAPwyiktSLVETLLEKKEFVEAVVSR-TPlgrvgePEEVSSLVAFLCLPASSYIT 243
Cdd:cd05334 145 AVHQLTQSLAAENsgLPAGSTANAILP-----VTLDTPANRKAMPDADFSSwTP------LEFIAELILFWASGAARPKS 213


                ....*...
gi 15239327 244 GQVISVDG 251
Cdd:cd05334 214 GSLIPVVT 221
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 8-178 9.69e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 72.65  E-value: 9.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:PRK07109   5 PIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEEL- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK07109  84 GPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHA 163

                        170
                 ....*....|.
gi 15239327  168 LNQLTRNLACE 178
Cdd:PRK07109 164 IRGFTDSLRCE 174
PRK08219 PRK08219
SDR family oxidoreductase;
12-243 4.11e-14

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 69.58  E-value: 4.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKfGAKVHTCSRNQEELNACLNDWK-ANGLVVSGSVCDAsvrdqrekliQEASSAFSGKL 90
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELAAELPgATPFPVDLTDPEA----------IAAAVEQLGRL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGATKGALNQ 170
Cdd:PRK08219  73 DVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAASKFALRA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239327  171 LTRNLACEWAsDNIRTNCVAPWYIKTSLVETL--LEKKEFVEAVVSRtplgrvgePEEVSSLVAF-LCLPASSYIT 243
Cdd:PRK08219 152 LADALREEEP-GNVRVTSVHPGRTDTDMQRGLvaQEGGEYDPERYLR--------PETVAKAVRFaVDAPPDAHIT 218
PRK06139 PRK06139
SDR family oxidoreductase;
8-180 6.78e-14

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 70.13  E-value: 6.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANG---LVVSGSVCDAsvrDQREKLIQEASS 84
Cdd:PRK06139   4 PLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGaevLVVPTDVTDA---DQVKALATQAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   85 aFSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGAT 164
Cdd:PRK06139  81 -FGGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSAS 159

                        170
                 ....*....|....*.
gi 15239327  165 KGALNQLTRNLACEWA 180
Cdd:PRK06139 160 KFGLRGFSEALRGELA 175
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
126-252 7.48e-14

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 68.87  E-value: 7.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  126 HLSQIAHPLLKASGvgSIVFISSVAG------------LVHLSS---------------GSIYGATKGALNQLTRNLACE 178
Cdd:PRK12428  77 HLTEALLPRMAPGG--AIVNVASLAGaewpqrlelhkaLAATASfdegaawlaahpvalATGYQLSKEALILWTMRQAQP 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  179 W-ASDNIRTNCVAPwyiktSLVET-LLekKEFV----EAVVSR--TPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVD 250
Cdd:PRK12428 155 WfGARGIRVNCVAP-----GPVFTpIL--GDFRsmlgQERVDSdaKRMGRPATADEQAAVLVFLCSDAARWINGVNLPVD 227


                 ..
gi 15239327  251 GG 252
Cdd:PRK12428 228 GG 229
PRK08017 PRK08017
SDR family oxidoreductase;
12-200 1.09e-13

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 68.96  E-value: 1.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNaclndwKANGLVVSGSVCDASVRDQREKLIQEASSAFSGKLN 91
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVA------RMNSLGFTGILLDLDDPESVERAADEVIALTDNRLY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQL 171
Cdd:PRK08017  77 GLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAW 156

                        170       180
                 ....*....|....*....|....*....
gi 15239327  172 TRNLACEWASDNIRTNCVAPWYIKTSLVE 200
Cdd:PRK08017 157 SDALRMELRHSGIKVSLIEPGPIRTRFTD 185
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 8-227 1.15e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 69.23  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLND--WKANGLVVSGSVCDasvRDQREKLIQEASSA 85
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAElgGDDRVLTVVADVTD---LAAMQAAAEEAVER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGATK 165
Cdd:PRK05872  83 F-GGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPGMAAYCASK 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15239327  166 GALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTP--LGRVGEPEEV 227
Cdd:PRK05872 161 AGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDADADLPAFRELRARLPwpLRRTTSVEKC 224
PRK05693 PRK05693
SDR family oxidoreductase;
12-201 3.38e-13

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 67.51  E-value: 3.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLN-DWKANGLVVSgsvCDASVRDQREKLIQEassafSGKL 90
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAaGFTAVQLDVN---DGAALARLAEELEAE-----HGGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSGSIYGATKGALNQ 170
Cdd:PRK05693  74 DVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSR-GLVVNIGSVSGVLVTPFAGAYCASKAAVHA 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15239327  171 LTRNLACEWASDNIRTNCVAPWYIKTSLVET 201
Cdd:PRK05693 153 LSDALRLELAPFGVQVMEVQPGAIASQFASN 183
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 14-239 4.83e-13

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: 65.61  E-value: 4.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  14 ALVTGGTRGIGRAVVEELAKFGA-KVhtcsrnqeelnaclndwkangLVVSgsvcdasvrdqrekliqeassafsgKLNI 92
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGSpKV---------------------LVVS-------------------------RRDV 34

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  93 LINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQLT 172
Cdd:cd02266  35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239327 173 RNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVvsRTPLGRVGEPEEVSSLVAFLCLPAS 239
Cdd:cd02266 115 QQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGN--RRHGVRTMPPEEVARALLNALDRPK 179
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 14-199 5.21e-13

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: 66.07  E-value: 5.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDwkanglvvsgsvcDASVRdqreKLIQEAssafsGKLNIL 93
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQVDITD-------------EASIK----ALFEKV-----GHFDAI 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  94 INNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLkASGvGSIVFISSVAGLVHLSSGSIYGATKGALNQLTR 173
Cdd:cd11731  59 VSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL-NDG-GSITLTSGILAQRPIPGGAAAATVNGALEGFVR 136

                       170       180
                ....*....|....*....|....*.
gi 15239327 174 NLACEwASDNIRTNCVAPWYIKTSLV 199
Cdd:cd11731 137 AAAIE-LPRGIRINAVSPGVVEESLE 161
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 14-179 1.32e-12

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: 64.85  E-value: 1.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAClndwkANGLVVSGSVCDASVRDQREKLIQEAssafsGKLNIL 93
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGL-----AAEVGALARPADVAAELEVWALAQEL-----GPLDLL 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  94 INNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASgvGSIVFISSVAGLVHLSSGSIYGATKGALNQLTR 173
Cdd:cd11730  71 VYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAG--ARLVFLGAYPELVMLPGLSAYAAAKAALEAYVE 148


                ....*.
gi 15239327 174 NLACEW 179
Cdd:cd11730 149 VARKEV 154
PRK05855 PRK05855
SDR family oxidoreductase;
6-201 1.44e-12

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 66.93  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    6 RWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSA 85
Cdd:PRK05855 310 RGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAE 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   86 FsGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGV-GSIVFISSVAGLVHLSSGSIYGAT 164
Cdd:PRK05855 390 H-GVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTgGHIVNVASAAAYAPSRSLPAYATS 468

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15239327  165 KGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVET 201
Cdd:PRK05855 469 KAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVAT 505
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 15-252 3.98e-12

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 64.18  E-value: 3.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   15 LVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVvsgsvCDASVRDQREKLIQEASSAFSGkLNILI 94
Cdd:PRK06483   6 LITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGLRQAGAQCIQ-----ADFSTNAGIMAFIDELKQHTDG-LRAII 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   95 NNVGTNV-RKPTVEYSsEEYAKIMSTNLESAFHLSQIAHPLLKASGVGsivfissVAGLVHLS-----SGS----IYGAT 164
Cdd:PRK06483  80 HNASDWLaEKPGAPLA-DVLARMMQIHVNAPYLLNLALEDLLRGHGHA-------ASDIIHITdyvveKGSdkhiAYAAS 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  165 KGALNQLTRNLACEWASdNIRTNCVAPwyiktSLVetLLEKK---EFVEAVVSRTPLGRVGEPEEVSSLVAFLClpASSY 241
Cdd:PRK06483 152 KAALDNMTLSFAAKLAP-EVKVNSIAP-----ALI--LFNEGddaAYRQKALAKSLLKIEPGEEEIIDLVDYLL--TSCY 221

                        250
                 ....*....|.
gi 15239327  242 ITGQVISVDGG 252
Cdd:PRK06483 222 VTGRSLPVDGG 232
PRK08278 PRK08278
SDR family oxidoreductase;
8-217 4.89e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 64.15  E-value: 4.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKV-----------------HTCSrnqEELNAclndwkANG--LVVsgsVCD 68
Cdd:PRK08278   3 SLSGKTLFITGASRGIGLAIALRAARDGANIviaaktaephpklpgtiHTAA---EEIEA------AGGqaLPL---VGD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   69 asVRD--QREKLIQEASSAFSGkLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFI 146
Cdd:PRK08278  71 --VRDedQVAAAVAKAVERFGG-IDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  147 S------------SVAglvhlssgsiYGATKGALNQLTRNLACEWASDNIRTNCVAP-WYIKTSLVETLLEKKEFVEAvv 213
Cdd:PRK08278 148 SpplnldpkwfapHTA----------YTMAKYGMSLCTLGLAEEFRDDGIAVNALWPrTTIATAAVRNLLGGDEAMRR-- 215


                 ....
gi 15239327  214 SRTP 217
Cdd:PRK08278 216 SRTP 219
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 9-238 6.59e-12

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 64.94  E-value: 6.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELnacLNDWKANGLVVSGSVCDASVRDQ-REKLIQEA---SS 84
Cdd:COG3347 423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAA---EAAAAELGGGYGADAVDATDVDVtAEAAVAAAfgfAG 499

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  85 AFSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVG-SIVFISSVAGLVHLSSGSIYGA 163
Cdd:COG3347 500 LDIGGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGgSSVFAVSKNAAAAAYGAAAAAT 579

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239327 164 TKGALNQLTRNLACEWASDNIRTNCVAPWyiktSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:COG3347 580 AKAAAQHLLRALAAEGGANGINANRVNPD----AVLDGSAIWASAARAERAAAYGIGNLLLEEVYRKRVALAVLV 650
PRK07102 PRK07102
SDR family oxidoreductase;
11-168 1.49e-11

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 62.63  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLV-VSGSVCDASVRDQREKLIQEASsafsGK 89
Cdd:PRK07102   1 MKKILIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVaVSTHELDILDTASHAAFLDSLP----AL 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15239327   90 LNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGAL 168
Cdd:PRK07102  77 PDIVLIAVGTLGDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAAL 155
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 11-191 1.81e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 62.63  E-value: 1.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVsgsVCDASVRDQREKLIQEASSAFsGKL 90
Cdd:PRK06180   4 MKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALAR---LLDVTDFDAIDAVVADAEATF-GPI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVrKPTVEYSS-EEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:PRK06180  80 DVLVNNAGYGH-EGAIEESPlAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALE 158

                        170       180
                 ....*....|....*....|..
gi 15239327  170 QLTRNLACEWASDNIRTNCVAP 191
Cdd:PRK06180 159 GISESLAKEVAPFGIHVTAVEP 180
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 15-191 2.74e-11

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 62.08  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   15 LVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDasvRDQREKLIQEASSAFSgKLNILI 94
Cdd:PRK10538   4 LVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRN---RAAIEEMLASLPAEWR-NIDVLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   95 NNVGTNV-RKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQLTR 173
Cdd:PRK10538  80 NNAGLALgLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSL 159

                        170
                 ....*....|....*...
gi 15239327  174 NLACEWASDNIRTNCVAP 191
Cdd:PRK10538 160 NLRTDLHGTAVRVTDIEP 177
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 12-210 3.47e-11

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: 61.71  E-value: 3.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGA---KVHTCSRN---QEELnaclndWKANGLVVSGS--VCDASVRDQrEKLIQEAS 83
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLASDPSkrfKVYATMRDlkkKGRL------WEAAGALAGGTleTLQLDVCDS-KSVAAAVE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  84 SAFSGKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGA 163
Cdd:cd09806  74 RVTERHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCA 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15239327 164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVE 210
Cdd:cd09806 154 SKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPEEVL 200
PRK07775 PRK07775
SDR family oxidoreductase;
12-198 6.18e-11

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 61.31  E-value: 6.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANG---LVVSGSVCDA-SVRDqrekLIQEASSAFs 87
Cdd:PRK07775  11 RPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGgeaVAFPLDVTDPdSVKS----FVAQAEEAL- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK07775  86 GEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAG 165

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSL 198
Cdd:PRK07775 166 LEAMVTNLQMELEGTGVRASIVHPGPTLTGM 196
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
9-259 1.33e-10

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 59.98  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTG--GTRGIGRAVVEELAKFGAKV---HTCSRNQEELNACLNDWKANgLVVSgsvCDASVRDQREKLIQEAS 83
Cdd:PRK08690   4 LQGKKILITGmiSERSIAYGIAKACREQGAELaftYVVDKLEERVRKMAAELDSE-LVFR---CDVASDDEINQVFADLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   84 SAFSGkLNILINNVGTNVRKPTV-----EYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVHLSSG 158
Cdd:PRK08690  80 KHWDG-LDGLVHSIGFAPKEALSgdfldSISREAFNTAHEISAYSLPALAKAARPMMRGRN-SAIVALSYLGAVRAIPNY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  159 SIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:PRK08690 158 NVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGIADFGKLLGHVAAHNPLRRNVTIEEVGNTAAFLLSDL 237

                        250       260
                 ....*....|....*....|.
gi 15239327  239 SSYITGQVISVDGGFTVNGFS 259
Cdd:PRK08690 238 SSGITGEITYVDGGYSINALS 258
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 11-198 1.51e-10

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 60.26  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDW--KANGLVVSGSVCDASVR-DQREKLIQEASSAFS 87
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIqsKYSKTQIKTVVVDFSGDiDEGVKRIKETIEGLD 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 gkLNILINNVGtnVRKPTVEY---SSEEYAK-IMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSG--SIY 161
Cdd:PLN02780 133 --VGVLINNVG--VSYPYARFfheVDEELLKnLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSDPlyAVY 208

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15239327  162 GATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSL 198
Cdd:PLN02780 209 AATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKM 245
PRK06482 PRK06482
SDR family oxidoreductase;
11-218 1.71e-10

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 59.74  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCD-ASVRdqreKLIQEASSAFsGK 89
Cdd:PRK06482   2 SKTWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDsAAVR----AVVDRAFAAL-GR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   90 LNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALN 169
Cdd:PRK06482  77 IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15239327  170 QLTRNLACEwasdnirtncVAPWYIKTSLVETLLEKKEFVEAVVSRTPL 218
Cdd:PRK06482 157 GFVEAVAQE----------VAPFGIEFTIVEPGPARTNFGAGLDRGAPL 195
PRK08177 PRK08177
SDR family oxidoreductase;
12-178 2.12e-10

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 58.89  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEelnaclndwKANGL----VVSGSVCDASVRDQREKLIQeassAFS 87
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQ---------QDTALqalpGVHIEKLDMNDPASLDQLLQ----RLQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GK-LNILINNVGTN--VRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKAsGVGSIVFISSVAGLVHLSSGS---IY 161
Cdd:PRK08177  69 GQrFDLLFVNAGISgpAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRP-GQGVLAFMSSQLGSVELPDGGempLY 147

                        170
                 ....*....|....*..
gi 15239327  162 GATKGALNQLTRNLACE 178
Cdd:PRK08177 148 KASKAALNSMTRSFVAE 164
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
123-253 2.63e-10

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 59.36  E-value: 2.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  123 SAFHLSQIAH---PLLKASGvgSIVFISSVAGLVHLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLV 199
Cdd:PRK08594 122 SAYSLTAVAReakKLMTEGG--SIVTLTYLGGERVVQNYNVMGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTLSA 199

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15239327  200 ETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVDGGF 253
Cdd:PRK08594 200 KGVGGFNSILKEIEERAPLRRTTTQEEVGDTAAFLFSDLSRGVTGENIHVDSGY 253
PRK07024 PRK07024
SDR family oxidoreductase;
16-200 3.38e-10

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 58.79  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   16 VTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAclndWKA-NGLVVSGSVCDASVRDQREklIQEASSAF---SGKLN 91
Cdd:PRK07024   7 ITGASSGIGQALAREYARQGATLGLVARRTDALQA----FAArLPKAARVSVYAADVRDADA--LAAAAADFiaaHGLPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   92 ILINNVGTNVRKPTVEYS-SEEYAKIMSTNLesaFHLSQIAHPLL---KASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK07024  81 VVIANAGISVGTLTEEREdLAVFREVMDTNY---FGMVATFQPFIapmRAARRGTLVGIASVAGVRGLPGAGAYSASKAA 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKTSLVE 200
Cdd:PRK07024 158 AIKYLESLRVELRPAGVRVVTIAPGYIRTPMTA 190
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
 88-264 6.00e-10

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 58.68  E-value: 6.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNV--GTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgsivfisSVAGLVHLSSGSI---YG 162
Cdd:PRK06300 118 GHIDILVHSLanSPEISKPLLETSRKGYLAALSTSSYSFVSLLSHFGPIMNPGG--------STISLTYLASMRAvpgYG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  163 ----ATKGALNQLTRNLACE----WasdNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFL 234
Cdd:PRK06300 190 ggmsSAKAALESDTKVLAWEagrrW---GIRVNTISAGPLASRAGKAIGFIERMVDYYQDWAPLPEPMEAEQVGAAAAFL 266

                        170       180       190
                 ....*....|....*....|....*....|
gi 15239327  235 CLPASSYITGQVISVDGGFTVNGFSYAMKP 264
Cdd:PRK06300 267 VSPLASAITGETLYVDHGANVMGIGPEMFP 296
PRK09291 PRK09291
SDR family oxidoreductase;
11-227 7.20e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 58.09  E-value: 7.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDQREKliqeassAFSGKL 90
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDRAQ-------AAEWDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGALNQ 170
Cdd:PRK09291  75 DVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239327  171 LTRNLACEWASDNIRTNCVAPWYIKTSLVETLLE--------KKEFVEAVVSRTPLGRVgEPEEV 227
Cdd:PRK09291 155 IAEAMHAELKPFGIQVATVNPGPYLTGFNDTMAEtpkrwydpARNFTDPEDLAFPLEQF-DPQEM 218
PRK06101 PRK06101
SDR family oxidoreductase;
13-200 9.11e-10

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 57.57  E-value: 9.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   13 TALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELnACLNDWKANGLVVSGSVCDasvrdqrEKLIQEASSAFSGKLNI 92
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVL-DELHTQSANIFTLAFDVTD-------HPGTKAALSQLPFIPEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   93 LINNVGtnvrkpTVEY------SSEEYAKIMSTNLESAFHLSQIAHPLLKASgvGSIVFISSVAGLVHLSSGSIYGATKG 166
Cdd:PRK06101  75 WIFNAG------DCEYmddgkvDATLMARVFNVNVLGVANCIEGIQPHLSCG--HRVVIVGSIASELALPRAEAYGASKA 146

                        170       180       190
                 ....*....|....*....|....*....|....
gi 15239327  167 ALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVE 200
Cdd:PRK06101 147 AVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTD 180
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 12-196 1.04e-09

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: 57.67  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVhtcsrnqeeLNACLNDWK--ANGL---------VVSGSVCDasvrdqrEKLIQ 80
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTV---------LAGCLTKNGpgAKELrrvcsdrlrTLQLDVTK-------PEQIK 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  81 EASSAFSGKLNI-----LINNVGTNVRKPTVEYSS-EEYAKIMSTNLESAFHLSQIAHPLLKASGvGSIVFISSVAGLVH 154
Cdd:cd09805  65 RAAQWVKEHVGEkglwgLVNNAGILGFGGDEELLPmDDYRKCMEVNLFGTVEVTKAFLPLLRRAK-GRVVNVSSMGGRVP 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15239327 155 LSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKT 196
Cdd:cd09805 144 FPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKT 185
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 12-153 1.19e-09

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: 55.95  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327     12 KTALVTGGTRGIGRAVVEELAKFGA-KVHTCSRN---QEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLSRSgpdAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVE- 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239327     88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLsqiaHPLLKASGVGSIVFISSVAGLV 153
Cdd:smart00822  80 GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNL----HELTADLPLDFFVLFSSIAGVL 141
PRK07023 PRK07023
SDR family oxidoreductase;
14-202 1.39e-09

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 56.95  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQ------------EELNACLNDWKANGLVVSGSVCDASVRDQREKLiqe 81
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARSRhpslaaaagerlAEVELDLSDAAAAAAWLAGDLLAAFVDGASRVL--- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   82 assafsgklniLINNVGTnVRK--PTVEYSSEEYAKIMSTNLesafhlsqiAHPLLKASGVGSIVFISSVAGLVHLSSG- 158
Cdd:PRK07023  81 -----------LINNAGT-VEPigPLATLDAAAIARAVGLNV---------AAPLMLTAALAQAASDAAERRILHISSGa 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15239327  159 --------SIYGATKGALNQLTRNLACEwASDNIRTNCVAPWYIKTSLVETL 202
Cdd:PRK07023 140 arnayagwSVYCATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGMQATI 190
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
 81-257 6.37e-09

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 55.55  E-value: 6.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   81 EASSAFSGKLNILINNV--GTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgsivfisSVAGLVHLSSG 158
Cdd:PLN02730 112 ESVKADFGSIDILVHSLanGPEVTKPLLETSRKGYLAAISASSYSFVSLLQHFGPIMNPGG--------ASISLTYIASE 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  159 SI---YG----ATKGALNQLTRNLACEWASD-NIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSL 230
Cdd:PLN02730 184 RIipgYGggmsSAKAALESDTRVLAFEAGRKyKIRVNTISAGPLGSRAAKAIGFIDDMIEYSYANAPLQKELTADEVGNA 263

                        170       180
                 ....*....|....*....|....*..
gi 15239327  231 VAFLCLPASSYITGQVISVDGGFTVNG 257
Cdd:PLN02730 264 AAFLASPLASAITGATIYVDNGLNAMG 290
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
123-252 1.20e-08

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 54.34  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  123 SAFHL---SQIAHPLLKASGvgSIVFISSVAGLVHLSSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLV 199
Cdd:PRK06079 118 SAYSLiavAKYARPLLNPGA--SIVTLTYFGSERAIPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAV 195

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15239327  200 ETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVDGG 252
Cdd:PRK06079 196 TGIKGHKDLLKESDSRTVDGVGVTIEEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 11-199 1.70e-08

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: 54.01  E-value: 1.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKA---NGLVVSGSVCDASVRDQRE---KLIQEASs 84
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRdtlNHEVIVRHLDLASLKSIRAfaaEFLAEED- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  85 afsgKLNILINNVGTnVRKPtveYSSEE--YAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVA---GLVHL---- 155
Cdd:cd09807  80 ----RLDVLINNAGV-MRCP---YSKTEdgFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAhkaGKINFddln 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15239327 156 -----SSGSIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLV 199
Cdd:cd09807 152 seksyNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELG 200
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 9-147 2.46e-08

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: 53.22  E-value: 2.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   9 LAGKTALVTGGTRGIGRAVVEELAKFGAKV---------H-----TCSRNQEELNAclndwkANGLVVSgSVCDASVRDQ 74
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVviaaktaepHpklpgTIYTAAEEIEA------AGGKALP-CIVDIRDEDQ 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239327  75 REKLIQEASSAFSGkLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFIS 147
Cdd:cd09762  74 VRAAVEKAVEKFGG-IDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLS 145
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 14-198 3.10e-08

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: 52.99  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    14 ALVTGGTRGIGRAVVEELAKF----GAKVHTCSRNQEELNACLNDWKA--NGLVV---SGSVCDASVRDQREKLIQEASS 84
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAerSGLRVvrvSLDLGAEAGLEQLLKALRELPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    85 AFSGKLNILINNVGT--NVRKPTVEYS-SEEYAKIMSTNLESAFHLSQI---AHPLLKASGVgSIVFISSVAGLVHLSSG 158
Cdd:TIGR01500  83 PKGLQRLLLINNAGTlgDVSKGFVDLSdSTQVQNYWALNLTSMLCLTSSvlkAFKDSPGLNR-TVVNISSLCAIQPFKGW 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 15239327   159 SIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSL 198
Cdd:TIGR01500 162 ALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDM 201
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 11-153 4.03e-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: 52.98  E-value: 4.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANglvvSGS------VCDASVRDQREKLIQEASS 84
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETE----SGNqniflhIVDMSDPKQVWEFVEEFKE 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15239327  85 AFSgKLNILINNVGTNVRKPtvEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLV 153
Cdd:cd09808  77 EGK-KLHVLINNAGCMVNKR--ELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGGMLV 142
PRK07984 PRK07984
enoyl-ACP reductase FabI;
159-255 5.05e-08

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 52.60  E-value: 5.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  159 SIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:PRK07984 157 NVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDL 236

                         90
                 ....*....|....*..
gi 15239327  239 SSYITGQVISVDGGFTV 255
Cdd:PRK07984 237 SAGISGEVVHVDGGFSI 253
PRK07806 PRK07806
SDR family oxidoreductase;
8-148 5.12e-08

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 52.41  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEElnaclndwKANGLV-------VSGSVCDASVRDQRE--KL 78
Cdd:PRK07806   3 DLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAP--------RANKVVaeieaagGRASAVGADLTDEESvaAL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   79 IQEASSAFsGKLNILINNVGTNVRKPTveysSEEYAkiMSTNLESAFHLSQIAHPLLKASgvGSIVFISS 148
Cdd:PRK07806  75 MDTAREEF-GGLDALVLNASGGMESGM----DEDYA--MRLNRDAQRNLARAALPLMPAG--SRVVFVTS 135
PRK09009 PRK09009
SDR family oxidoreductase;
15-179 5.19e-08

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 52.37  E-value: 5.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   15 LVTGGTRGIGRAVVEEL-AKF-GAKVHTCSRNQEElnaclnDWKANGLV-VSGSVCDasvrdqrEKLIQEASSAFSgKLN 91
Cdd:PRK09009   4 LIVGGSGGIGKAMVKQLlERYpDATVHATYRHHKP------DFQHDNVQwHALDVTD-------EAEIKQLSEQFT-QLD 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   92 ILINNVG---TNVRKPTVEYSS---EEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLV---HLSSGSIYG 162
Cdd:PRK09009  70 WLINCVGmlhTQDKGPEKSLQAldaDFFLQNITLNTLPSLLLAKHFTPKLKQSESAKFAVISAKVGSIsdnRLGGWYSYR 149

                        170
                 ....*....|....*..
gi 15239327  163 ATKGALNQLTRNLACEW 179
Cdd:PRK09009 150 ASKAALNMFLKTLSIEW 166
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
12-250 6.85e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 51.99  E-value: 6.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANGLVVSGsvCDASVRDQREKLIQEASS-----AF 86
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYNSNLTFHS--LDLQDVHELETNFNEILSsiqedNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   87 SGKLniLINNVGT-NVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKA-SGVGSIVFISSVAGLVHLSSGSIYGAT 164
Cdd:PRK06924  80 SSIH--LINNAGMvAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDwKVDKRVINISSGAAKNPYFGWSAYCSS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  165 KGALNQLTRNLACEWA--SDNIRTNCVAPWYIKTSLVETLLE--KKEF--VEAVVSRTPLGRVGEPEEVSSLVAFLcLPA 238
Cdd:PRK06924 158 KAGLDMFTQTVATEQEeeEYPVKIVAFSPGVMDTNMQAQIRSssKEDFtnLDRFITLKEEGKLLSPEYVAKALRNL-LET 236

                        250
                 ....*....|..
gi 15239327  239 SSYITGQVISVD 250
Cdd:PRK06924 237 EDFPNGEVIDID 248
PRK05884 PRK05884
SDR family oxidoreductase;
15-252 7.60e-08

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 51.73  E-value: 7.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   15 LVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAClndwkANGLVVSGSVCD----ASVRDQREKliqeassaFSGKL 90
Cdd:PRK05884   4 LVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVA-----AKELDVDAIVCDntdpASLEEARGL--------FPHHL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   91 NILINN-----VGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKaSGvGSIvfISSVAGLVhlSSGSIYGATK 165
Cdd:PRK05884  71 DTIVNVpapswDAGDPRTYSLADTANAWRNALDATVLSAVLTVQSVGDHLR-SG-GSI--ISVVPENP--PAGSAEAAIK 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  166 GALNQLTRNLACEWASDNIRTNCVAPwyikTSLVETLLEKkefveavVSRTPLGRVGEpeeVSSLVAFLCLPASSYITGQ 245
Cdd:PRK05884 145 AALSNWTAGQAAVFGTRGITINAVAC----GRSVQPGYDG-------LSRTPPPVAAE---IARLALFLTTPAARHITGQ 210


                 ....*..
gi 15239327  246 VISVDGG 252
Cdd:PRK05884 211 TLHVSHG 217
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 10-153 1.14e-07

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: 51.98  E-value: 1.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  10 AGKTALVTGGTRGIGRAVVEELAK-FGAKVHTCSR-----NQEELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEAS 83
Cdd:cd08953 204 PGGVYLVTGGAGGIGRALARALARrYGARLVLLGRsplppEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVR 283

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15239327  84 SAFsGKLNILINNVGTnVRKPTVEYSS-EEYAKIMSTNLESAFHLSQiahpLLKASGVGSIVFISSVAGLV 153
Cdd:cd08953 284 ERY-GAIDGVIHAAGV-LRDALLAQKTaEDFEAVLAPKVDGLLNLAQ----ALADEPLDFFVLFSSVSAFF 348
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
118-257 1.19e-07

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 51.48  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  118 STNLE-SAFHLSQIAH---PLLKASGvgSIV---FISSVAGlvhlssgSIY---GATKGALNQLTRNLACEWASDNIRTN 187
Cdd:PRK07889 114 ATALHvSAYSLKSLAKallPLMNEGG--SIVgldFDATVAW-------PAYdwmGVAKAALESTNRYLARDLGPRGIRVN 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15239327  188 CVAPWYIKTSLVETLLEKKEFVEAVVSRTPLG-RVGEPEEVSSLVAFLC---LPASsyiTGQVISVDGGFTVNG 257
Cdd:PRK07889 185 LVAAGPIRTLAAKAIPGFELLEEGWDERAPLGwDVKDPTPVARAVVALLsdwFPAT---TGEIVHVDGGAHAMG 255
PRK08251 PRK08251
SDR family oxidoreductase;
12-196 1.24e-07

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 51.09  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKAN--GLVVSGSVCDASVRDQREKLIQEASSAFsGK 89
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEFRDEL-GG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   90 LNILINN--------VGT---NVRKPTVEysseeyakimsTNLESAfhLSQI--AHPLLKASGVGSIVFISSVAGLVHLS 156
Cdd:PRK08251  82 LDRVIVNagigkgarLGTgkfWANKATAE-----------TNFVAA--LAQCeaAMEIFREQGSGHLVLISSVSAVRGLP 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15239327  157 SG-SIYGATKGALNQLTRNLACEWASDNIRTNCVAPWYIKT 196
Cdd:PRK08251 149 GVkAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRS 189
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
106-257 1.68e-07

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 50.90  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  106 VEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLVHLSSGSIYGATKGALNQLTRNLACEWASDNIR 185
Cdd:PRK08415 104 LETSKEAFNIAMEISVYSLIELTRALLPLLNDGA--SVLTLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVDLGKKGIR 181

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239327  186 TNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVDGGFTVNG 257
Cdd:PRK08415 182 VNAISAGPIKTLAASGIGDFRMILKWNEINAPLKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVDAGYNIMG 253
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
106-257 3.69e-07

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 50.01  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  106 VEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLVHLSSGSIYGATKGALNQLTRNLACEWASDNIR 185
Cdd:PRK06603 107 VDTSLENFHNSLHISCYSLLELSRSAEALMHDGG--SIVTLTYYGAEKVIPNYNVMGVAKAALEASVKYLANDMGENNIR 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239327  186 TNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYITGQVISVDGGFTVNG 257
Cdd:PRK06603 185 VNAISAGPIKTLASSAIGDFSTMLKSHAATAPLKRNTTQEDVGGAAVYLFSELSKGVTGEIHYVDCGYNIMG 256
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
13-176 4.14e-07

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 49.98  E-value: 4.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  13 TALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKANglVVSGSVCDasvRDQREKLIQEASSAFsgklnI 92
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVE--FVRGDLRD---PEALAAALAGVDAVV-----H 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  93 LINNVGTNVRKPtveysseeyAKIMSTNLESAFHLSQIAhpllKASGVGSIVFISSVA--GLVH--------LSSGSIYG 162
Cdd:COG0451  71 LAAPAGVGEEDP---------DETLEVNVEGTLNLLEAA----RAAGVKRFVYASSSSvyGDGEgpidedtpLRPVSPYG 137

                       170
                ....*....|....
gi 15239327 163 ATKGALNQLTRNLA 176
Cdd:COG0451 138 ASKLAAELLARAYA 151
PRK06196 PRK06196
oxidoreductase; Provisional
 9-148 3.14e-06

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 47.37  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDwkANGLVVSG-SVCD-ASVRDQREKLIQEASsaf 86
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAG--IDGVEVVMlDLADlESVRAFAERFLDSGR--- 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239327   87 sgKLNILINNVGtnVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISS 148
Cdd:PRK06196  99 --RIDILINNAG--VMACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSS 156
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 15-179 5.09e-06

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: 45.99  E-value: 5.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  15 LVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEElnacLNDWKANGL-VVSGSVCD-ASVRDqrekliqeassAFSGkLNI 92
Cdd:COG0702   3 LVTGATGFIGRRVVRALLARGHPVRALVRDPEK----AAALAAAGVeVVQGDLDDpESLAA-----------ALAG-VDA 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  93 LINNVGTNVR-KPTVEYsseeyakimstnlESAFHLSQIAhpllKASGVGSIVFISSVAglVHLSSGSIYGATKGALNQL 171
Cdd:COG0702  67 VFLLVPSGPGgDFAVDV-------------EGARNLADAA----KAAGVKRIVYLSALG--ADRDSPSPYLRAKAAVEEA 127


                ....*...
gi 15239327 172 TRNLACEW 179
Cdd:COG0702 128 LRASGLPY 135
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
162-255 7.63e-06

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 45.97  E-value: 7.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  162 GATKGALNQLTRNLACEWASDNIRTNCVAPWYIKT---SLVETLLEKKEFVEAVvsrTPLGRVGEPEEVSSLVAFLCLPA 238
Cdd:PRK06997 160 GLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTlaaSGIKDFGKILDFVESN---APLRRNVTIEEVGNVAAFLLSDL 236

                         90
                 ....*....|....*..
gi 15239327  239 SSYITGQVISVDGGFTV 255
Cdd:PRK06997 237 ASGVTGEITHVDSGFNA 253
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 15-152 8.33e-06

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: 46.22  E-value: 8.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  15 LVTGGTRGIGRAVVEELAKFGAKVHT-CSRNQEELNACLND--WKANGLVVSGSVCDASVRDQREKLIqeASSAFSGKLN 91
Cdd:cd05274 154 LITGGLGGLGLLVARWLAARGARHLVlLSRRGPAPRAAARAalLRAGGARVSVVRCDVTDPAALAALL--AELAAGGPLA 231

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239327  92 ILINNVGTnVRKPTV-EYSSEEYAKIMSTNLESAFHLsqiaHPLLKASGVGSIVFISSVAGL 152
Cdd:cd05274 232 GVIHAAGV-LRDALLaELTPAAFAAVLAAKVAGALNL----HELTPDLPLDFFVLFSSVAAL 288
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 10-165 9.17e-06

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: 46.07  E-value: 9.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  10 AGKTALVTGGTRGIGRAVVEELAKFGAK-VHTCSRNQEELNACLNDWKANGLVVSGSVCDASVRDqrEKLIQEASSAfsG 88
Cdd:cd05237   1 KGKTILVTGGAGSIGSELVRQILKFGPKkLIVFDRDENKLHELVRELRSRFPHDKLRFIIGDVRD--KERLRRAFKE--R 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  89 KLNILIN-----NVgtnvrkPTVEYSSEEYAKimsTNLESAFHLSQIAHpllkASGVGSIVFISS--VAGLVhlssgSIY 161
Cdd:cd05237  77 GPDIVFHaaalkHV------PSMEDNPEEAIK---TNVLGTKNVIDAAI----ENGVEKFVCISTdkAVNPV-----NVM 138


                ....
gi 15239327 162 GATK 165
Cdd:cd05237 139 GATK 142
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 8-147 1.47e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 45.38  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRN----QEELN--------ACLNDwKANGLVVSGSVcDASVRDQR 75
Cdd:PRK08303   5 PLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRStrarRSEYDrpetieetAELVT-AAGGRGIAVQV-DHLVPEQV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15239327   76 EKLIQEASSAfSGKLNILINNV--GTNV---RKPTVEYSSEEYAKIMSTNLESafHL--SQIAHPLLKASGVGSIVFIS 147
Cdd:PRK08303  83 RALVERIDRE-QGRLDILVNDIwgGEKLfewGKPVWEHSLDKGLRMLRLAIDT--HLitSHFALPLLIRRPGGLVVEIT 158
PRK05993 PRK05993
SDR family oxidoreductase;
12-196 2.72e-05

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 44.63  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDwkanglvvsGSVC---DASVRDQREKLIQEASSAFSG 88
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAE---------GLEAfqlDYAEPESIAALVAQVLELSGG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   89 KLNILINNvGTNVRKPTVE-YSSEEYAKIMSTNLESAFHLSQIAHPLLKASGVGSIVFISSVAGLVHLSSGSIYGATKGA 167
Cdd:PRK05993  76 RLDALFNN-GAYGQPGAVEdLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFA 154

                        170       180
                 ....*....|....*....|....*....
gi 15239327  168 LNQLTRNLACEWASDNIRTNCVAPWYIKT 196
Cdd:PRK05993 155 IEGLSLTLRMELQGSGIHVSLIEPGPIET 183
PRK05854 PRK05854
SDR family oxidoreductase;
9-169 5.05e-05

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 43.90  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    9 LAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWK--ANGLVVSGSVCD----ASVRDQREKLIQEA 82
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRtaVPDAKLSLRALDlsslASVAALGEQLRAEG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   83 SSafsgkLNILINNVGTnVRKPTVEYSSEEYAKIMSTNLESAFHLsqIAH--PLLKAsGVGSIVFISSVAglvhlssgsi 160
Cdd:PRK05854  92 RP-----IHLLINNAGV-MTPPERQTTADGFELQFGTNHLGHFAL--TAHllPLLRA-GRARVTSQSSIA---------- 152


                 ....*....
gi 15239327  161 ygATKGALN 169
Cdd:PRK05854 153 --ARRGAIN 159
PRK06720 PRK06720
hypothetical protein; Provisional
 6-98 5.14e-05

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 42.65  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    6 RWSLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAC---LNDWKANGLVVSgsvCDASVRDQREKLIQEA 82
Cdd:PRK06720  11 KMKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATveeITNLGGEALFVS---YDMEKQGDWQRVISIT 87

                         90
                 ....*....|....*.
gi 15239327   83 SSAFSgKLNILINNVG 98
Cdd:PRK06720  88 LNAFS-RIDMLFQNAG 102
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 14-176 9.07e-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: 9.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAclndwkANGLVVSGSVCDASVRDQREKLIQEAssafsgKLNIL 93
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNT------ARLADLRFVEGDLTDRDALEKLLADV------RPDAV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    94 INNVGTnvrkPTVEYSSEEYAKIMSTNLESAFHLSQiahpLLKASGVGSIVFISSVA--------------GLVHLSSGS 159
Cdd:pfam01370  69 IHLAAV----GGVGASIEDPEDFIEANVLGTLNLLE----AARKAGVKRFLFASSSEvygdgaeipqeettLTGPLAPNS 140

                         170
                  ....*....|....*..
gi 15239327   160 IYGATKGALNQLTRNLA 176
Cdd:pfam01370 141 PYAAAKLAGEWLVLAYA 157
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 13-153 9.63e-05

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: 42.16  E-value: 9.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    13 TALVTGGTRGIGRAVVEELAKFGAKvH--TCSRNQ---EELNACLNDWKANGLVVSGSVCDASVRDQREKLIQEASSAFs 87
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGAR-HlvLLSRSAaprPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEG- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239327    88 GKLNILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLsqiaHPLLKASGVGSIVFISSVAGLV 153
Cdd:pfam08659  80 PPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNL----HEATPDEPLDFFVLFSSIAGLL 141
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
 8-114 1.14e-04

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 42.76  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327    8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWkanglvvsgsvcDASVRDQREKLIQEASSAFS 87
Cdd:PRK07424 175 SLKGKTVAVTGASGTLGQALLKELHQQGAKVVALTSNSDKITLEINGE------------DLPVKTLHWQVGQEAALAEL 242

                         90       100
                 ....*....|....*....|....*....
gi 15239327   88 -GKLNILINNVGTNV-RKPTVEYSSEEYA 114
Cdd:PRK07424 243 lEKVDILIINHGINVhGERTPEAINKSYE 271
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
88-257 2.16e-04

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 41.66  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVG----TNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASGvgSIVFISSVAGLVHLSSGSIYGA 163
Cdd:PRK08159  87 GKLDFVVHAIGfsdkDELTGRYVDTSRDNFTMTMDISVYSFTAVAQRAEKLMTDGG--SILTLTYYGAEKVMPHYNVMGV 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  164 TKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSYIT 243
Cdd:PRK08159 165 AKAALEASVKYLAVDLGPKNIRVNAISAGPIKTLAASGIGDFRYILKWNEYNAPLRRTVTIEEVGDSALYLLSDLSRGVT 244

                        170
                 ....*....|....
gi 15239327  244 GQVISVDGGFTVNG 257
Cdd:PRK08159 245 GEVHHVDSGYHVVG 258
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 14-173 7.32e-04

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) 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. 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. 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: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 39.31  E-value: 7.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  14 ALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELnaclndWKANGLVVSGSVCDASVRDQREKLIQEASsafsgklnIL 93
Cdd:cd05226   1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKRL------SKEDQEPVAVVEGDLRDLDSLSDAVQGVD--------VV 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  94 INNVGTNVRKPTVEYSSEEYAKimstNLESAfhlsqiahplLKASGVGSIVFISSVAGLVHL------SSGSIYGATKGA 167
Cdd:cd05226  67 IHLAGAPRDTRDFCEVDVEGTR----NVLEA----------AKEAGVKHFIFISSLGAYGDLheetepSPSSPYLAVKAK 132


                ....*.
gi 15239327 168 LNQLTR 173
Cdd:cd05226 133 TEAVLR 138
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 8-51 7.76e-04

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 39.68  E-value: 7.76e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15239327   8 SLAGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEEL-NAC 51
Cdd:cd01078  25 DLKGKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAqKAA 69
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 15-71 8.04e-04

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. 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: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 39.53  E-value: 8.04e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15239327  15 LVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNAcLNDWKANglVVSGSVCDASV 71
Cdd:cd05243   3 LVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEK-LEAAGAE--VVVGDLTDAES 56
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
 16-85 8.88e-04

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. 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: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 40.02  E-value: 8.88e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  16 VTGGTRGIGRAVVEELAKFGAKVHTCSRNqEELNACLNDWKAnglvvsgSVCDASVRDQrEKLIQEASSA 85
Cdd:cd05262   5 VTGATGFIGSAVVRELVAAGHEVVGLARS-DAGAAKLEAAGA-------QVHRGDLEDL-DILRKAAAEA 65
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 10-52 1.13e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 39.75  E-value: 1.13e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15239327  10 AGKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACL 52
Cdd:COG0604 139 PGETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLR 181
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 12-179 1.28e-03

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. 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: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 39.54  E-value: 1.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEelnaclNDWKANGLVVSGSV----CDASVRDQREKLIQEAssafs 87
Cdd:cd05271   1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEA------YARRLLVMGDLGQVlfveFDLRDDESIRKALEGS----- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  88 gklNILINNVGtnVRKPTVEYSSEEyakimsTNLESAFHLSQIAhpllKASGVGSIVFISSVAGLVHlsSGSIYGATKGA 167
Cdd:cd05271  70 ---DVVINLVG--RLYETKNFSFED------VHVEGPERLAKAA----KEAGVERLIHISALGADAN--SPSKYLRSKAE 132

                       170
                ....*....|..
gi 15239327 168 LNQLTRNLACEW 179
Cdd:cd05271 133 GEEAVREAFPEA 144
PLN02657 PLN02657
3,8-divinyl protochlorophyllide a 8-vinyl reductase
 12-69 1.48e-03

3,8-divinyl protochlorophyllide a 8-vinyl reductase


Pssm-ID: 178263 [Multi-domain]  Cd Length: 390  Bit Score: 39.36  E-value: 1.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNA-----CLNDWKANGLVVSGSVCDA 69
Cdd:PLN02657  61 VTVLVVGATGYIGKFVVRELVRRGYNVVAVAREKSGIRGkngkeDTKKELPGAEVVFGDVTDA 123
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 10-53 2.30e-03

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 38.58  E-value: 2.30e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15239327  10 AGKTALVTGGTRGIGRAVVeELAK-FGAKVHTCSRNQEELNACLN 53
Cdd:cd05276 139 AGETVLIHGGASGVGTAAI-QLAKaLGARVIATAGSEEKLEACRA 182
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 11-98 2.61e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 38.47  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   11 GKTALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDwkanglvVSGSVCDASVRDQREKL-----IQEASSA 85
Cdd:PRK06197  16 GRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAAR-------ITAATPGADVTLQELDLtslasVRAAADA 88

                         90
                 ....*....|....*.
gi 15239327   86 FSG---KLNILINNVG 98
Cdd:PRK06197  89 LRAaypRIDLLINNAG 104
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 12-43 3.53e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. 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: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 38.04  E-value: 3.53e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 15239327  12 KTALVTGGTRGIGRAVVEELAKFGAKVHTCSR 43
Cdd:cd05265   1 MKILIIGGTRFIGKALVEELLAAGHDVTVFNR 32
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 12-202 3.64e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 37.49  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   12 KTALVTGGTRGIGRAVVEELAKfGAKVHTCSRNQEELNACLNDwkanglvvsgsvcDASVRDQREKLiqeassafsGKLN 91
Cdd:PRK07578   1 MKILVIGASGTIGRAVVAELSK-RHEVITAGRSSGDVQVDITD-------------PASIRALFEKV---------GKVD 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   92 ILINNVGTNVRKPTVEYSSEEYAKIMSTNLESAFHLSQIAHPLLKASgvGSIVFISSVAGLVHLSSGSIYGATKGALNQL 171
Cdd:PRK07578  58 AVVSAAGKVHFAPLAEMTDEDFNVGLQSKLMGQVNLVLIGQHYLNDG--GSFTLTSGILSDEPIPGGASAATVNGALEGF 135

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15239327  172 TRNLACEwASDNIRTNCVAPwyikTSLVETL 202
Cdd:PRK07578 136 VKAAALE-LPRGIRINVVSP----TVLTESL 161
PRK08862 PRK08862
SDR family oxidoreductase;
13-191 3.80e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 37.78  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   13 TALVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELNACLNDWKA-NGLVVSGSVCDASvRDQREKLIQEASSAFSGKLN 91
Cdd:PRK08862   7 IILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSAlTDNVYSFQLKDFS-QESIRHLFDAIEQQFNRAPD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   92 ILINNVgTNVRKPTV--EYSSEEYAKIMSTNLESAFHLSQI-AHPLLKASGVGSIVFISSVAGLVHLSSGSiygATKGAL 168
Cdd:PRK08862  86 VLVNNW-TSSPLPSLfdEQPSESFIQQLSSLASTLFTYGQVaAERMRKRNKKGVIVNVISHDDHQDLTGVE---SSNALV 161

                        170       180
                 ....*....|....*....|...
gi 15239327  169 NQLTRNLACEWASDNIRTNCVAP 191
Cdd:PRK08862 162 SGFTHSWAKELTPFNIRVGGVVP 184
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 15-205 3.93e-03

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: 37.99  E-value: 3.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  15 LVTGGTRGIGRAVVEELAKFGAKVHTCSRNQEELnaclndwkanglvvsgSVCDASVRDQREKLIQEAssafsgKLNILI 94
Cdd:cd05254   3 LITGATGMLGRALVRLLKERGYEVIGTGRSRASL----------------FKLDLTDPDAVEEAIRDY------KPDVII 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  95 NNVG-TNVRKptVEyssEEYAKIMSTNLESAFHLSQIAHpllkasGVGSIvfissvagLVHLSSG--------------- 158
Cdd:cd05254  61 NCAAyTRVDK--CE---SDPELAYRVNVLAPENLARAAK------EVGAR--------LIHISTDyvfdgkkgpykeeda 121

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15239327 159 ----SIYGATKGALNQLTRNLACEWAsdNIRTNCV-APWYIKTSLVETLLEK 205
Cdd:cd05254 122 pnplNVYGKSKLLGEVAVLNANPRYL--ILRTSWLyGELKNGENFVEWMLRL 171
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
 15-46 5.47e-03

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical 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: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 37.25  E-value: 5.47e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 15239327  15 LVTGGTRGIGRAVVEELAKFGAKVHTCSRNQE 46
Cdd:cd05269   2 LVTGATGKLGTAVVELLLAKVASVVALVRNPE 33
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
88-255 6.78e-03

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 37.03  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327   88 GKLNILINNVG----TNVRKPTVEYSSEEYAKIMstnLESAFHLSQIAH--PLLKASGvGSIVFISSVAGLVHLSSGSIY 161
Cdd:PRK06505  84 GKLDFVVHAIGfsdkNELKGRYADTTRENFSRTM---VISCFSFTEIAKraAKLMPDG-GSMLTLTYGGSTRVMPNYNVM 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239327  162 GATKGALNQLTRNLACEWASDNIRTNCVAPWYIKTSLVETLLEKKEFVEAVVSRTPLGRVGEPEEVSSLVAFLCLPASSY 241
Cdd:PRK06505 160 GVAKAALEASVRYLAADYGPQGIRVNAISAGPVRTLAGAGIGDARAIFSYQQRNSPLRRTVTIDEVGGSALYLLSDLSSG 239

                        170
                 ....*....|....
gi 15239327  242 ITGQVISVDGGFTV 255
Cdd:PRK06505 240 VTGEIHFVDSGYNI 253
 
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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