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Conserved domains on  [gi|226371731|ref|NP_113651|]
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inactive hydroxysteroid dehydrogenase-like protein 1 isoform a [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143247)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to very-long-chain 3-oxoacyl-CoA reductase that catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation; 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
67-309 1.93e-139

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: 394.28  E-value: 1.93e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKDKDVG 146
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERIEKELEGLDIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ILVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:cd05356   81 ILVNNVGISHSIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 227 HFSRALQYEYASKGIFVQSLIPFYVATSMTAPSnflhRCSWLVPSPKVYAHHAVSTLGISKRTTGYWSHSIQFLFAQYMP 306
Cdd:cd05356  161 FFSRALYEEYKSQGIDVQSLLPYLVATKMSKIR----KSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVP 236

                 ...
gi 226371731 307 EWL 309
Cdd:cd05356  237 EWI 239
 
Name Accession Description Interval E-value
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
67-309 1.93e-139

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: 394.28  E-value: 1.93e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKDKDVG 146
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERIEKELEGLDIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ILVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:cd05356   81 ILVNNVGISHSIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 227 HFSRALQYEYASKGIFVQSLIPFYVATSMTAPSnflhRCSWLVPSPKVYAHHAVSTLGISKRTTGYWSHSIQFLFAQYMP 306
Cdd:cd05356  161 FFSRALYEEYKSQGIDVQSLLPYLVATKMSKIR----KSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVP 236

                 ...
gi 226371731 307 EWL 309
Cdd:cd05356  237 EWI 239
PLN02780 PLN02780
ketoreductase/ oxidoreductase
20-307 3.22e-70

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 221.28  E-value: 3.22e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  20 CYMEALALVGAWYT---ARKSITVICDFYSLIRLHFIPRLGSRADLiKQYGRWAVVSGATDGIGKAYAEELASRGLNIIL 96
Cdd:PLN02780   4 CFVDKLKSQPLWLLvlfVLGSLSILKFFFTILNWVYVYFLRPAKNL-KKYGSWALVTGPTDGIGKGFAFQLARKGLNLVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  97 ISRNEEKLQVVAKDIADTY-KVETDIIVADFSSG-REIYLPIREALKDKDVGILVNNVGVFYPYPQYFTQLSEDKLWDII 174
Cdd:PLN02780  83 VARNPDKLKDVSDSIQSKYsKTQIKTVVVDFSGDiDEGVKRIKETIEGLDVGVLINNVGVSYPYARFFHEVDEELLKNLI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 175 NVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCC--KPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVA 252
Cdd:PLN02780 163 KVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIviPSDPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVA 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226371731 253 TSMTApsnfLHRCSWLVPSPKVYAHHAVSTLGISKRTTGYWSHSIQFLFAQYMPE 307
Cdd:PLN02780 243 TKMAS----IRRSSFLVPSSDGYARAALRWVGYEPRCTPYWPHSLIWGLISALPE 293
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
67-309 2.88e-49

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 165.04  E-value: 2.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPIREAL-KDKDV 145
Cdd:COG0300    5 GKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA-GARVEVVALDVTDPDAVAALAEAVLaRFGPI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPypQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYL 225
Cdd:COG0300   84 DVLVNNAGVGGG--GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 226 DHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSNFLHRCSWLvpSPKVYAHHAVStlGISKRTTGY---WSHSIQFLFA 302
Cdd:COG0300  162 EGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLL--SPEEVARAILR--ALERGRAEVyvgWDARLLARLL 237

                 ....*..
gi 226371731 303 QYMPEWL 309
Cdd:COG0300  238 RLLPRLF 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
68-260 4.52e-44

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 149.69  E-value: 4.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731   68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPIREALKD-KDVG 146
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL-GGKALFIQGDVTDRAQVKALVEQAVERlGRLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  147 ILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:pfam00106  80 ILVNNAGITGLGP--FSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVI 157
                         170       180       190
                  ....*....|....*....|....*....|....
gi 226371731  227 HFSRALQYEYASKGIFVQSLIPFYVATSMTAPSN 260
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
70-256 3.04e-11

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: 62.62  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731   70 AVVSGATDGIGKAYAEELASRGLN----IILISRNEEKLQVVAKDI-ADTYKVETDIIVADFSS--GREIYLPIREAL-- 140
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKCLKSpgsvLVLSARNDEALRQLKAEIgAERSGLRVVRVSLDLGAeaGLEQLLKALRELpr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  141 -KDKDVGILVNNVGVFYPYPQYFTQLSE----DKLWDIiNVN--IAAASLMVHVV--LPGmVERkkgAIVTISSGSCCKP 211
Cdd:TIGR01500  83 pKGLQRLLLINNAGTLGDVSKGFVDLSDstqvQNYWAL-NLTsmLCLTSSVLKAFkdSPG-LNR---TVVNISSLCAIQP 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 226371731  212 TPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:TIGR01500 158 FKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQ 202
 
Name Accession Description Interval E-value
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
67-309 1.93e-139

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: 394.28  E-value: 1.93e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKDKDVG 146
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYERIEKELEGLDIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ILVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:cd05356   81 ILVNNVGISHSIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 227 HFSRALQYEYASKGIFVQSLIPFYVATSMTAPSnflhRCSWLVPSPKVYAHHAVSTLGISKRTTGYWSHSIQFLFAQYMP 306
Cdd:cd05356  161 FFSRALYEEYKSQGIDVQSLLPYLVATKMSKIR----KSSLFVPSPEQFVRSALNTLGLSKRTTGYWSHALQGWVARLVP 236

                 ...
gi 226371731 307 EWL 309
Cdd:cd05356  237 EWI 239
PLN02780 PLN02780
ketoreductase/ oxidoreductase
20-307 3.22e-70

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 221.28  E-value: 3.22e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  20 CYMEALALVGAWYT---ARKSITVICDFYSLIRLHFIPRLGSRADLiKQYGRWAVVSGATDGIGKAYAEELASRGLNIIL 96
Cdd:PLN02780   4 CFVDKLKSQPLWLLvlfVLGSLSILKFFFTILNWVYVYFLRPAKNL-KKYGSWALVTGPTDGIGKGFAFQLARKGLNLVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  97 ISRNEEKLQVVAKDIADTY-KVETDIIVADFSSG-REIYLPIREALKDKDVGILVNNVGVFYPYPQYFTQLSEDKLWDII 174
Cdd:PLN02780  83 VARNPDKLKDVSDSIQSKYsKTQIKTVVVDFSGDiDEGVKRIKETIEGLDVGVLINNVGVSYPYARFFHEVDEELLKNLI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 175 NVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCC--KPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVA 252
Cdd:PLN02780 163 KVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIviPSDPLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVA 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226371731 253 TSMTApsnfLHRCSWLVPSPKVYAHHAVSTLGISKRTTGYWSHSIQFLFAQYMPE 307
Cdd:PLN02780 243 TKMAS----IRRSSFLVPSSDGYARAALRWVGYEPRCTPYWPHSLIWGLISALPE 293
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
67-309 2.88e-49

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 165.04  E-value: 2.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPIREAL-KDKDV 145
Cdd:COG0300    5 GKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAA-GARVEVVALDVTDPDAVAALAEAVLaRFGPI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPypQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYL 225
Cdd:COG0300   84 DVLVNNAGVGGG--GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 226 DHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSNFLHRCSWLvpSPKVYAHHAVStlGISKRTTGY---WSHSIQFLFA 302
Cdd:COG0300  162 EGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLL--SPEEVARAILR--ALERGRAEVyvgWDARLLARLL 237

                 ....*..
gi 226371731 303 QYMPEWL 309
Cdd:COG0300  238 RLLPRLF 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
68-260 4.52e-44

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 149.69  E-value: 4.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731   68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPIREALKD-KDVG 146
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGAL-GGKALFIQGDVTDRAQVKALVEQAVERlGRLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  147 ILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:pfam00106  80 ILVNNAGITGLGP--FSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVI 157
                         170       180       190
                  ....*....|....*....|....*....|....
gi 226371731  227 HFSRALQYEYASKGIFVQSLIPFYVATSMTAPSN 260
Cdd:pfam00106 158 GFTRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
67-257 2.79e-41

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: 144.16  E-value: 2.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIylpirEALKDK--- 143
Cdd:COG1028    6 GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA-GGRALAVAADVTDEAAV-----EALVAAava 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 ---DVGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:COG1028   80 afgRLDILVNNAGITPPGP--LEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAA 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:COG1028  158 SKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTR 194
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
70-259 1.12e-39

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: 139.73  E-value: 1.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETdiIVADFSSGREIYLPIREALKD-KDVGIL 148
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALGGNAVA--VQADVSDEEDVEALVEEALEEfGRLDIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDHF 228
Cdd:cd05233   79 VNNAGIARPGP--LEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGL 156
                        170       180       190
                 ....*....|....*....|....*....|.
gi 226371731 229 SRALQYEYASKGIFVQSLIPFYVATSMTAPS 259
Cdd:cd05233  157 TRSLALELAPYGIRVNAVAPGLVDTPMLAKL 187
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
67-257 7.45e-37

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: 132.23  E-value: 7.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYK-VETDiiVADFSSgreiylpIREALKD--K 143
Cdd:COG4221    5 GKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALaVPLD--VTDEAA-------VEAAVAAavA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DVG---ILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:COG4221   76 EFGrldVLVNNAGVALLGP--LEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAA 153
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:COG4221  154 TKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLD 190
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
67-255 3.75e-35

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 127.88  E-value: 3.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADtYKVETDIIVADFSSGREIYLPIrEALKDK--D 144
Cdd:PRK07666   7 GKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEA-YGVKVVIATADVSDYEEVTAAI-EQLKNElgS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVfypyPQY--FTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASK 222
Cdd:PRK07666  85 IDILINNAGI----SKFgkFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASK 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK07666 161 FGVLGLTESLMQEVRKHNIRVTALTPSTVATDM 193
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
67-260 1.76e-32

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 121.04  E-value: 1.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI----ADTYKVETDiiVADFSSGREIYLPIREALKD 142
Cdd:PRK05653   5 GKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraagGEARVLVFD--VSDEAAVRALIEAAVEAFGA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDvgILVNNVGVFYPYPqyFTQLSEDKlWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSAS 221
Cdd:PRK05653  83 LD--ILVNNAGITRDAL--LPRMSEED-WDrVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAA 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSN 260
Cdd:PRK05653 158 KAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLP 196
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
70-257 1.22e-31

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: 118.42  E-value: 1.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADtYKVETDIIVADFSSGREIYLPIREALKDKD-VGIL 148
Cdd:cd05333    3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKA-LGGNAAALEADVSDREAVEALVEKVEAEFGpVDIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGVfyPYPQYFTQLSEDKlWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDH 227
Cdd:cd05333   82 VNNAGI--TRDNLLMRMSEED-WDaVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIG 158
                        170       180       190
                 ....*....|....*....|....*....|
gi 226371731 228 FSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:cd05333  159 FTKSLAKELASRGITVNAVAPGFIDTDMTD 188
PRK12826 PRK12826
SDR family oxidoreductase;
67-258 2.45e-31

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 118.10  E-value: 2.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTY-KVETdiIVADFSSGREIYLPIREALKD-KD 144
Cdd:PRK12826   6 GRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGgKARA--RQVDVRDRAALKAAVAAGVEDfGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS--GScCKPTPQLAAFSASK 222
Cdd:PRK12826  84 LDILVANAGIFPLTP--FAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSvaGP-RVGYPGLAHYAASK 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:PRK12826 161 AGLVGFTRALALELAARNITVNSVHPGGVDTPMAGN 196
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
67-253 7.82e-30

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: 114.29  E-value: 7.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADtYKVETDIIVADFSSGREIylpirEALKDK--- 143
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRA-GGAGVLAVVADLTDPEDI-----DRLVEKagd 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 ---DVGILVNNVGvfYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:cd05344   75 afgRVDILVNNAG--GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNV 152
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:cd05344  153 ARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDT 185
PRK07454 PRK07454
SDR family oxidoreductase;
70-270 8.21e-30

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 113.90  E-value: 8.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPIREALKD-KDVGIL 148
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRST-GVKAAAYSIDLSNPEAIAPGIAELLEQfGCPDVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGVFYPYPQYFTQLSEdklWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDH 227
Cdd:PRK07454  88 INNAGMAYTGPLLEMPLSD---WQwVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAA 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226371731 228 FSRALQYEYASKGIFVQSLIPFYVATSM----TAPSNFlHRCSWLVP 270
Cdd:PRK07454 165 FTKCLAEEERSHGIRVCTITLGAVNTPLwdteTVQADF-DRSAMLSP 210
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
71-310 1.15e-29

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: 113.84  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKD-KDVGILV 149
Cdd:cd05332    7 IITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLEDAEQVVEEALKLfGGLDILI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 150 NNVGVfyPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDHFS 229
Cdd:cd05332   87 NNAGI--SMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGFF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 230 RALQYEYASKGIFVQSLIPFYVATSM---------TAPSNFLHRCSWLVPSPKVyAHHAVSTLGISKRTTgYWSHSIQFL 300
Cdd:cd05332  165 DSLRAELSEPNISVTVVCPGLIDTNIamnalsgdgSMSAKMDDTTANGMSPEEC-ALEILKAIALRKREV-FYARQVPLL 242
                        250
                 ....*....|...
gi 226371731 301 FA---QYMPEWLW 310
Cdd:cd05332  243 AVylrQLFPGLFD 255
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
67-259 1.39e-29

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: 113.22  E-value: 1.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIaDTYKVETDIIVADFSSGREIYLPIREALKD-KDV 145
Cdd:cd05347    5 GKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLI-EKEGVEATAFTCDVSDEEAIKAAVEAIEEDfGKI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYL 225
Cdd:cd05347   84 DILVNNAGIIRRHP--AEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGV 161
                        170       180       190
                 ....*....|....*....|....*....|....
gi 226371731 226 DHFSRALQYEYASKGIFVQSLIPFYVATSMTAPS 259
Cdd:cd05347  162 AGLTKALATEWARHGIQVNAIAPGYFATEMTEAV 195
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
67-257 3.18e-29

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 112.24  E-value: 3.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILI-SRNEEKLQVVAKDIADtYKVETDIIVADFSSGREIYLPIREALKDKD- 144
Cdd:PRK05565   5 GKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLEEIKE-EGGDAIAVKADVSSEEDVENLVEQIVEKFGk 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPqyFTQLSEDkLWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISS-----GSCCKptpqlAAF 218
Cdd:PRK05565  84 IDILVNNAGISNFGL--VTDMTDE-EWDrVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSiwgliGASCE-----VLY 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226371731 219 SASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK05565 156 SASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWS 194
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
67-256 4.37e-29

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 111.82  E-value: 4.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKL-QVVAKDIADtYKVETDIIVADFSSGREIYLPIREALKD-KD 144
Cdd:PRK05557   5 GKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaEALVAEIGA-LGGKALAVQGDVSDAESVERAVDEAKAEfGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK05557  84 VDILVNNAGITRDNL--LMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAG 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:PRK05557 162 VIGFTKSLARELASRGITVNAVAPGFIETDMT 193
FabG-like PRK07231
SDR family oxidoreductase;
67-257 1.04e-28

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 111.08  E-value: 1.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTykvETDIIV-ADFSSGREIYLPIREALKD-KD 144
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAG---GRAIAVaADVSDEADVEAAVAAALERfGS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYpQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK07231  82 VDILVNNAGTTHRN-GPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGA 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETGLLE 193
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
67-257 2.24e-28

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: 109.70  E-value: 2.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDiiVADFSSGREIYlpiREALKD-KDV 145
Cdd:cd05370    5 GNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNIHTIVLD--VGDAESVEALA---EALLSEyPNL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPqyFTQLSE--DKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKA 223
Cdd:cd05370   80 DILINNAGIQRPID--LRDPASdlDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKA 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:cd05370  158 ALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHE 191
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
67-256 1.83e-27

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 107.65  E-value: 1.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISR-NEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPIREALKDK-D 144
Cdd:PRK12825   6 GRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAVEAL-GRRAQAVQADVTDKAALEAAVAAAVERFgR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK12825  85 IDILVNNAGIFEDKP--LADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAG 162
                        170       180       190
                 ....*....|....*....|....*....|..
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:PRK12825 163 LVGLTKALARELAEYGITVNMVAPGDIDTDMK 194
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
67-259 7.24e-27

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: 105.80  E-value: 7.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVET---DIIVADFSSGREIYLPIREALKD- 142
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASGqkvSYISADLSDYEEVEQAFAQAVEKg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDVGILVNNVGVFypYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASK 222
Cdd:cd08939   81 GPPDLVVNCAGIS--IPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSK 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIP------FYVATSMTAPS 259
Cdd:cd08939  159 FALRGLAESLRQELKPYNIRVSVVYPpdtdtpGFEEENKTKPE 201
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
67-253 1.62e-26

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: 105.19  E-value: 1.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI--ADTYKVETDIIVADFSSGREIYLPIREAL-KDK 143
Cdd:cd05364    3 GKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSClqAGVSEKKILLVVADLTEEEGQDRIISTTLaKFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DVGILVNNVGVfyPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVErKKGAIVTISSGSCCKPTPQLAAFSASKA 223
Cdd:cd05364   83 RLDILVNNAGI--LAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIK-TKGEIVNVSSVAGGRSFPGVLYYCISKA 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:cd05364  160 ALDQFTRCTALELAPKGVRVNSVSPGVIVT 189
PRK07201 PRK07201
SDR family oxidoreductase;
51-259 2.05e-26

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 109.66  E-value: 2.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  51 HFIPRLGSRADLIKQ-YGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI-ADTYKVETdiIVADFSS 128
Cdd:PRK07201 354 HLDPDRARRRDLRGPlVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIrAKGGTAHA--YTCDLTD 431
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 129 GREIYLPIREALKDKD-VGILVNNVG------VfypypqyftQLSEDKLWD---IINVNIAAASLMVHVVLPGMVERKKG 198
Cdd:PRK07201 432 SAAVDHTVKDILAEHGhVDYLVNNAGrsirrsV---------ENSTDRFHDyerTMAVNYFGAVRLILGLLPHMRERRFG 502
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226371731 199 AIVTISSGSCCKPTPQLAAFSASKAYLDHFSRALQYEYASKGI-FVQSLIPFyVATSMTAPS 259
Cdd:PRK07201 503 HVVNVSSIGVQTNAPRFSAYVASKAALDAFSDVAASETLSDGItFTTIHMPL-VRTPMIAPT 563
PRK09072 PRK09072
SDR family oxidoreductase;
71-258 2.69e-26

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 105.02  E-value: 2.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIadTYKVETDIIVAD--FSSGREIYLpiREALKDKDVGIL 148
Cdd:PRK09072   9 LLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARL--PYPGRHRWVVADltSEAGREAVL--ARAREMGGINVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGV--FypypQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS--GSCckPTPQLAAFSASKAY 224
Cdd:PRK09072  85 INNAGVnhF----ALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGStfGSI--GYPGYASYCASKFA 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:PRK09072 159 LRGFSEALRRELADTGVRVLYLAPRATRTAMNSE 192
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
68-255 8.43e-26

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 103.31  E-value: 8.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKlqvVAKDIADTYKVETDII------VADFSSGREIYLPIREalK 141
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGND---CAKDWFEEYGFTEDQVrlkeldVTDTEECAEALAEIEE--E 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDVGILVNNVGVfyPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSAS 221
Cdd:PRK12824  78 EGPVDILVNNAGI--TRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAA 155
                        170       180       190
                 ....*....|....*....|....*....|....
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK12824 156 KAGMIGFTKALASEGARYGITVNCIAPGYIATPM 189
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
70-312 5.71e-25

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: 100.87  E-value: 5.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQ-VVAKDIADTYKVETDII-VADFSSGREIYLPIREALKDKDVGI 147
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDeLKAELLNPNPSVEVEILdVTDEERNQLVIAELEAELGGLDLVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 148 LvnNVGVFYPYPQYFTQLSEDKlwDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDH 227
Cdd:cd05350   81 I--NAGVGKGTSLGDLSFKAFR--ETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 228 FSRALQYEYASKGIFVQSLIPFYVATSMTAPSnflHRCSWLVpSPKVYAHHAVStlGISKRTTGY---WSHSIQFLFAQY 304
Cdd:cd05350  157 LAESLRYDVKKRGIRVTVINPGFIDTPLTANM---FTMPFLM-SVEQAAKRIYK--AIKKGAAEPtfpWRLAVPLRLLKL 230

                 ....*...
gi 226371731 305 MPEWLWVW 312
Cdd:cd05350  231 LPERLRRR 238
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
70-259 2.36e-24

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: 99.23  E-value: 2.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQvvakDIADTYKVETDIIVADFSSGREIYLPIREALK-DKDVGIL 148
Cdd:cd05374    3 VLITGCSSGIGLALALALAAQGYRVIATARNPDKLE----SLGELLNDNLEVLELDVTDEESIKAAVKEVIErFGRIDVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGvfypYPQYFT--QLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:cd05374   79 VNNAG----YGLFGPleETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALE 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 227 HFSRALQYEYASKGIFVQSLIPFYVATSMTAPS 259
Cdd:cd05374  155 ALSESLRLELAPFGIKVTIIEPGPVRTGFADNA 187
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
70-257 3.44e-24

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: 98.85  E-value: 3.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVaDFSSGREIYLPIREALKDK-DVGIL 148
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKC-DVSKREEVYEAAKKIKKEVgDVTIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDHF 228
Cdd:cd05339   81 INNAGVVSGKK--LLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGF 158
                        170       180       190
                 ....*....|....*....|....*....|..
gi 226371731 229 SRALQYE---YASKGIFVQSLIPFYVATSMTA 257
Cdd:cd05339  159 HESLRLElkaYGKPGIKTTLVCPYFINTGMFQ 190
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
67-255 7.93e-24

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: 97.93  E-value: 7.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDiiVADFSSGREIYLPIrealkdKDVG 146
Cdd:cd05351    7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPGIEPVCVD--LSDWDATEEALGSV------GPVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERK-KGAIVTISSGSCCKPTPQLAAFSASKAYL 225
Cdd:cd05351   79 LLVNNAAVAILQP--FLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCSTKAAL 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 226371731 226 DHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:cd05351  157 DMLTKVMALELGPHKIRVNSVNPTVVMTDM 186
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
68-257 1.18e-23

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: 97.61  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPIREAL-KDKDVG 146
Cdd:cd08945    4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREA-GVEADGRTCDVRSVPEIEALVAAAVaRYGPID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ILVNNVGvfYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLP--GMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:cd08945   83 VLVNNAG--RSGGGATAELADELWLDVVETNLTGVFRVTKEVLKagGMLERGTGRIINIASTGGKQGVVHAAPYSASKHG 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:cd08945  161 VVGFTKALGLELARTGITVNAVCPGFVETPMAA 193
PRK12828 PRK12828
short chain dehydrogenase; Provisional
67-258 6.67e-23

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 95.25  E-value: 6.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKDKDvg 146
Cdd:PRK12828   7 GKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFGRLD-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ILVNNVGVFyPYpQYFTQLSEDKlWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYL 225
Cdd:PRK12828  85 ALVNIAGAF-VW-GTIADGDADT-WDrMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGV 161
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 226 DHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:PRK12828 162 ARLTEALAAELLDRGITVNAVLPSIIDTPPNRA 194
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
70-253 8.77e-23

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: 95.04  E-value: 8.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREiylpIREALKD-----KD 144
Cdd:cd05346    3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRES----IEAALENlpeefRD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVfypypqyftQLSEDKLWDI--------INVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLA 216
Cdd:cd05346   79 IDILVNNAGL---------ALGLDPAQEAdledwetmIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGN 149
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 217 AFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:cd05346  150 VYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVET 186
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
67-294 1.68e-22

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: 94.60  E-value: 1.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIA---DTYKVETdiIVADFSSGREIYLPIREALKDK 143
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKketGNAKVEV--IQLDLSSLASVRQFAEEFLARF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 D-VGILVNNVGVFYPYpqyfTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGS-----------CCKP 211
Cdd:cd05327   79 PrLDILINNAGIMAPP----RRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAhragpidfndlDLEN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 212 TP---QLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMT--APSNFLHRC---SWLVPSPKVYAH---HAV 280
Cdd:cd05327  155 NKeysPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLrrNGSFFLLYKllrPFLKKSPEQGAQtalYAA 234
                        250
                 ....*....|....
gi 226371731 281 STLGISKRTTGYWS 294
Cdd:cd05327  235 TSPELEGVSGKYFS 248
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
67-256 1.95e-22

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: 94.14  E-value: 1.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI-ADTYKVEtdIIVADFSSGREIYLPIREALKD-KD 144
Cdd:cd08934    3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELeAEGGKAL--VLELDVTDEQQVDAAVERTVEAlGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPQYFTQLSEdklWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKA 223
Cdd:cd08934   81 LDILVNNAGIMLLGPVEDADTTD---WTrMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKF 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:cd08934  158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTELR 190
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
70-260 2.78e-22

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: 93.20  E-value: 2.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDiiVADFSSGREIylpiREALKDKDVGI-- 147
Cdd:cd08932    3 ALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGGDVEAVPYD--ARDPEDARAL----VDALRDRFGRIdv 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 148 LVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDH 227
Cdd:cd08932   77 LVHNAGIGRPTT--LREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRA 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 228 FSRALQYEYASKGIFVQSLIPFYVATSMTAPSN 260
Cdd:cd08932  155 LAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLT 187
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
67-258 4.12e-22

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: 93.28  E-value: 4.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADT-YKVETdiIVADFSS--GREIYLPIREALKDK 143
Cdd:cd05329    6 GKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgFKVEG--SVCDVSSrsERQELMDTVASHFGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DVGILVNNVGVFYPYPQyfTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKA 223
Cdd:cd05329   84 KLNILVNNAGTNIRKEA--KDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKG 161
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:cd05329  162 ALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEP 196
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
64-255 4.47e-22

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 93.33  E-value: 4.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  64 KQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVvAKDI------ADTYKVEtdiiVADFSSGREIYLPIR 137
Cdd:PRK08226   3 KLTGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKL-ADELcgrghrCTAVVAD----VRDPASVAAAIKRAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 138 EALKDKDvgILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS--GSCCKpTPQL 215
Cdd:PRK08226  78 EKEGRID--ILVNNAGVCRLGS--FLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSvtGDMVA-DPGE 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226371731 216 AAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK08226 153 TAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPM 192
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
61-257 6.10e-22

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: 92.78  E-value: 6.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  61 DLIKQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREAL 140
Cdd:cd05352    2 DLFSLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 141 KD-KDVGILVNNVGVfyPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGS---CCKPTPQlA 216
Cdd:cd05352   82 KDfGKIDILIANAGI--TVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSgtiVNRPQPQ-A 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226371731 217 AFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:cd05352  159 AYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTD 199
PRK06484 PRK06484
short chain dehydrogenase; Validated
64-257 7.74e-22

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 95.69  E-value: 7.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  64 KQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVetdiIVADFSSGREIYLPIREALKD- 142
Cdd:PRK06484   2 KAQSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHA----LAMDVSDEAQIREGFEQLHREf 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDVGILVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKG-AIVTISSGSCCKPTPQLAAFSAS 221
Cdd:PRK06484  78 GRIDVLVNNAGVTDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGaAIVNVASGAGLVALPKRTAYSAS 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK06484 158 KAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVA 193
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
72-257 9.21e-22

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: 92.15  E-value: 9.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  72 VSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDiiVADFSSGREIYLPIREALKDKDVgiLVNN 151
Cdd:COG3967   10 ITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLHTIVLD--VADPASIAALAEQVTAEFPDLNV--LINN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 152 VGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDHFSRA 231
Cdd:COG3967   86 AGIMRAEDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYTQS 165
                        170       180
                 ....*....|....*....|....*.
gi 226371731 232 LQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:COG3967  166 LRHQLKDTSVKVIELAPPAVDTDLTG 191
PRK12939 PRK12939
short chain dehydrogenase; Provisional
67-264 1.40e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 91.96  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI----ADTYKVETDiiVADFSSGREIYLPIREALKD 142
Cdd:PRK12939   7 GKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALeaagGRAHAIAAD--LADPASVQRFFDAAAAALGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDvgILVNNVGVfypypqyfTQLS-----EDKLWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLA 216
Cdd:PRK12939  85 LD--GLVNNAGI--------TNSKsatelDIDTWDaVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 226371731 217 AFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA--PSNFLHR 264
Cdd:PRK12939 155 AYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEATAyvPADERHA 204
PRK05866 PRK05866
SDR family oxidoreductase;
67-259 1.69e-21

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 92.50  E-value: 1.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPIREALKD-KDV 145
Cdd:PRK05866  40 GKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRA-GGDAMAVPCDLSDLDAVDALVADVEKRiGGV 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPqyfTQLSEDKLWDI---INVNIAAASLMVHVVLPGMVERKKGAIVTISS-GSCCKPTPQLAAFSAS 221
Cdd:PRK05866 119 DILINNAGRSIRRP---LAESLDRWHDVertMVLNYYAPLRLIRGLAPGMLERGDGHIINVATwGVLSEASPLFSVYNAS 195
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPS 259
Cdd:PRK05866 196 KAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIAPT 233
PRK07775 PRK07775
SDR family oxidoreductase;
68-255 1.99e-21

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 91.74  E-value: 1.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI--------ADTYKVETDIIVADFSSGREiylpirEA 139
Cdd:PRK07775  11 RPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIradggeavAFPLDVTDPDSVKSFVAQAE------EA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 140 LKDKDVgiLVNNVGVFYPYPQYftQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFS 219
Cdd:PRK07775  85 LGEIEV--LVSGAGDTYFGKLH--EISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYG 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 220 ASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK07775 161 AAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGM 196
PRK12829 PRK12829
short chain dehydrogenase; Provisional
67-256 2.47e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 91.27  E-value: 2.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKDKDVg 146
Cdd:PRK12829  11 GLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGAKVTATVADVADPAQVERVFDTAVERFGGLDV- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 iLVNNVGVFYPypqYFTQLS-EDKLWD-IINVNIAAASLMVHVVLPGMVERKKG-AIVTISSGSCCKPTPQLAAFSASKA 223
Cdd:PRK12829  90 -LVNNAGIAGP---TGGIDEiTPEQWEqTLAVNLNGQFYFARAAVPLLKASGHGgVIIALSSVAGRLGYPGRTPYAASKW 165
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:PRK12829 166 AVVGLVKSLAIELGPLGIRVNAILPGIVRGPRM 198
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
67-255 3.27e-21

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: 90.61  E-value: 3.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVetdIIVADFSSgreiylpIREALKDKD-V 145
Cdd:cd05368    2 GKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITTRV---LDVTDKEQ-------VAALAKEEGrI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYpypqYFTQLS-EDKLWDI-INVNIAAASLMVHVVLPGMVERKKGAIVTISS-GSCCKPTPQLAAFSASK 222
Cdd:cd05368   72 DVLFNCAGFVH----HGSILDcEDDDWDFaMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSvASSIKGVPNRFVYSTTK 147
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:cd05368  148 AAVIGLTKSVAADFAQQGIRCNAICPGTVDTPS 180
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
61-257 3.54e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 90.78  E-value: 3.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  61 DLIKQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIAdTYKVETDIIVADFSSGREIYLPIREAL 140
Cdd:PRK08213   6 ELFDLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLE-ALGIDALWIAADVADEADIERLAEETL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 141 KD-KDVGILVNNVGVFYPYPqyftqlSED---KLWD-IINVNIAAASLMVHVVLP-GMVERKKGAIVTISSGSCCKPTP- 213
Cdd:PRK08213  85 ERfGHVDILVNNAGATWGAP------AEDhpvEAWDkVMNLNVRGLFLLSQAVAKrSMIPRGYGRIINVASVAGLGGNPp 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226371731 214 ---QLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK08213 159 evmDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTR 205
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
70-295 3.90e-21

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: 89.99  E-value: 3.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLN-IILISRNEEKLQVVAKDI----ADTYKVETDiiVADFSSGREIYLPIREalKDKD 144
Cdd:cd05324    3 ALVTGANRGIGFEIVRQLAKSGPGtVILTARDVERGQAAVEKLraegLSVRFHQLD--VTDDASIEAAADFVEE--KYGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPQyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCckptPQLAAFSASKAY 224
Cdd:cd05324   79 LDILVNNAGIAFKGFD-DSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLG----SLTSAYGVSKAA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSNFLhrcswlvpSPKVYAHHAV--STLGISKRTTGYWSH 295
Cdd:cd05324  154 LNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAPK--------TPEEGAETPVylALLPPDGEPTGKFFS 218
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
67-255 1.32e-20

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: 88.99  E-value: 1.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADT-YKVETDIivadfSSGREIYLPIREAL-KDKD 144
Cdd:cd05345    5 GKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAaIAIQADV-----TKRADVEAMVEAALsKFGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYpYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:cd05345   80 LDILVNNAGITH-RNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGW 158
                        170       180       190
                 ....*....|....*....|....*....|.
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:cd05345  159 VVTATKAMAVELAPRNIRVNCLCPVAGETPL 189
PRK06949 PRK06949
SDR family oxidoreductase;
67-255 1.66e-20

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 89.05  E-value: 1.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI----ADTYKVETDiiVADFSSgreiylpIREALK- 141
Cdd:PRK06949   9 GKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIeaegGAAHVVSLD--VTDYQS-------IKAAVAh 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 -DKDVG---ILVNNVGVfyPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGA--------IVTISSGSCC 209
Cdd:PRK06949  80 aETEAGtidILVNNSGV--STTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASVAGL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226371731 210 KPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK06949 158 RVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEI 203
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
67-255 1.69e-20

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: 88.49  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIIL-ISRNEEKLQVVAKDI-----------ADTYKVETdiIVADFSSGREIYL 134
Cdd:cd05362    3 GKVALVTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAEIeaaggkaiavqADVSDPSQ--VARLFDAAEKAFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 135 PirealkdkdVGILVNNVGVFYPYPqyFTQLSEdKLWD-IINVNIAAASLMVHVVLPGMveRKKGAIVTISSGSCCKPTP 213
Cdd:cd05362   81 G---------VDILVNNAGVMLKKP--IAETSE-EEFDrMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTP 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226371731 214 QLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:cd05362  147 NYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
67-253 2.34e-20

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: 88.66  E-value: 2.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILIS-RNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKD-KD 144
Cdd:cd08940    2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGfGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQfGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:cd08940   82 VDILVNNAGIQHVAP--IEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHG 159
                        170       180
                 ....*....|....*....|....*....
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:cd08940  160 VVGLTKVVALETAGTGVTCNAICPGWVLT 188
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
70-261 2.75e-20

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: 87.85  E-value: 2.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGlniilisrnEEKLQVVAKDIADTY--------KVETdiIVADFSSGREIylpirEALK 141
Cdd:cd05354    6 VLVTGANRGIGKAFVESLLAHG---------AKKVYAAVRDPGSAAhlvakygdKVVP--LRLDVTDPESI-----KAAA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 D--KDVGILVNNVGVFYPYpQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFS 219
Cdd:cd05354   70 AqaKDVDVVINNAGVLKPA-TLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYS 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226371731 220 ASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSNF 261
Cdd:cd05354  149 ASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAGG 190
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
71-257 3.59e-20

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: 87.73  E-value: 3.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNI--ILISRNEEKLQVVAKDIADTYKVetDIIVADFSS---GREIYLPIREALKDKDv 145
Cdd:cd05367    3 ILTGASRGIGRALAEELLKRGSPSvvVLLARSEEPLQELKEELRPGLRV--TTVKADLSDaagVEQLLEAIRKLDGERD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 gILVNNVGVFYPYPQYFtQLSEDKLWDIINVNIAAASLMVHVVLPGMVERK-KGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:cd05367   80 -LLINNAGSLGPVSKIE-FIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSSGAAVNPFKGWGLYCSSKAA 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 225 LDHFSRALQYEYasKGIFVQSLIPFYVATSMTA 257
Cdd:cd05367  158 RDMFFRVLAAEE--PDVRVLSYAPGVVDTDMQR 188
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
67-252 3.65e-20

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: 88.28  E-value: 3.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI----ADTYKVETDiiVADFSSGREIYLPIREALKD 142
Cdd:cd08935    5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEItalgGRAIALAAD--VLDRASLERAREEIVAQFGT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDvgILVNNVGVFYPYP------------QYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCK 210
Cdd:cd08935   83 VD--ILINGAGGNHPDAttdpehyepeteQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFS 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226371731 211 PTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP-FYVA 252
Cdd:cd08935  161 PLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPgFFVT 203
PRK07063 PRK07063
SDR family oxidoreductase;
67-256 7.92e-20

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 87.03  E-value: 7.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI------ADTYKVETDI-----IVADFSSGREIYLP 135
Cdd:PRK07063   7 GKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIardvagARVLAVPADVtdaasVAAAVAAAEEAFGP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 136 IrealkdkDVgiLVNNVG--VFY-PYpqyftQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPT 212
Cdd:PRK07063  87 L-------DV--LVNNAGinVFAdPL-----AMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKII 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226371731 213 PQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:PRK07063 153 PGCFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLT 196
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
67-260 1.19e-19

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 86.51  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKvetdIIVADFSSGREIYLPIREALKD-KDV 145
Cdd:PRK12936   6 GRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVK----IFPANLSDRDEVKALGQKAEADlEGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVfyPYPQYFTQLSeDKLWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK12936  82 DILVNNAGI--TKDGLFVRMS-DEDWDsVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAG 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSN 260
Cdd:PRK12936 159 MIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLN 194
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
78-257 1.61e-19

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: 85.95  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731   78 GIGKAYAEELASRGLNIILISRNEEKLQVVAKdIADtyKVETDIIVADFSSGREIylpirEALKD---KDVG---ILVNN 151
Cdd:pfam13561   7 GIGWAIARALAEEGAEVVLTDLNEALAKRVEE-LAE--ELGAAVLPCDVTDEEQV-----EALVAaavEKFGrldILVNN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  152 VGVFYPYPQYFTQLSEDkLWD-IINVNIAAASLMVHVVLPGMveRKKGAIVTISSGSCCKPTPQLAAFSASKAYLDHFSR 230
Cdd:pfam13561  79 AGFAPKLKGPFLDTSRE-DFDrALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTR 155
                         170       180
                  ....*....|....*....|....*..
gi 226371731  231 ALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:pfam13561 156 YLAVELGPRGIRVNAISPGPIKTLAAS 182
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
70-253 2.15e-19

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: 85.70  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI----ADTYKVETDIivadfSSGREIYLPIREALKD-KD 144
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIqqagGQAIGLECNV-----TSEQDLEAVVKATVSQfGG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPQYFTQLSEDKLWdIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:cd05365   77 ITILVNNAGGGGPKPFDMPMTEEDFEW-AFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAA 155
                        170       180
                 ....*....|....*....|....*....
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:cd05365  156 VNHMTRNLAFDLGPKGIRVNAVAPGAVKT 184
PRK09242 PRK09242
SDR family oxidoreductase;
67-258 2.45e-19

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 85.95  E-value: 2.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYK-VETDIIVADFSS--GREIylpIREALKDK 143
Cdd:PRK09242   9 GQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPeREVHGLAADVSDdeDRRA---ILDWVEDH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DVG--ILVNNVGVfyPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSAS 221
Cdd:PRK09242  86 WDGlhILVNNAGG--NIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMT 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:PRK09242 164 KAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSG 200
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
67-256 7.43e-19

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: 84.52  E-value: 7.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKL-QVVAKDIADTYKVETDIIVADFSSGREIYlpIREALK-DKD 144
Cdd:cd08936   10 NKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVdRAVATLQGEGLSVTGTVCHVGKAEDRERL--VATAVNlHGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVfypYPQYFTQL-SEDKLWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASK 222
Cdd:cd08936   88 VDILVSNAAV---NPFFGNILdSTEEVWDkILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSK 164
                        170       180       190
                 ....*....|....*....|....*....|....
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:cd08936  165 TALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFS 198
PRK06181 PRK06181
SDR family oxidoreductase;
67-253 8.00e-19

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 84.26  E-value: 8.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADtYKVETDIIVADFSSGREIYLPIREALKDKD-V 145
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELAD-HGGEALVVPTDVSDAEACERLIEAAVARFGgI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVfyPYPQYFTQLSE-DKLWDIINVNIAAASLMVHVVLPGMVERkKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK06181  80 DILVNNAGI--TMWSRFDELTDlSVFERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKHA 156
                        170       180
                 ....*....|....*....|....*....
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK06181 157 LHGFFDSLRIELADDGVAVTVVCPGFVAT 185
PRK07060 PRK07060
short chain dehydrogenase; Provisional
67-257 8.85e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 84.00  E-value: 8.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADtykvetDIIVADFSSGREIylpiREALKDKDV- 145
Cdd:PRK07060   9 GKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC------EPLRLDVGDDAAI----RAALAAAGAf 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVG--VFYPYPQyftqLSEDKLWDIINVNIAAASLMVHVVLPGMVE-RKKGAIVTISSGSCCKPTPQLAAFSASK 222
Cdd:PRK07060  79 DGLVNCAGiaSLESALD----MTAEGFDRVMAVNARGAALVARHVARAMIAaGRGGSIVNVSSQAALVGLPDHLAYCASK 154
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK07060 155 AALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAA 189
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
70-257 9.84e-19

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: 83.94  E-value: 9.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQ---------------VVAKDIADTYKVEtdiivADFSSgreiyl 134
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAaevaaeieelggkavVVRADVSQPQDVE-----EMFAA------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 135 pIREALKDKDvgILVNNV--GVFYPypqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPT 212
Cdd:cd05359   70 -VKERFGRLD--VLVSNAaaGAFRP----LSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRAL 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 226371731 213 PQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:cd05359  143 PNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALA 187
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
67-256 1.09e-18

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: 83.69  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADtykvETDIIVADFSSGREIYLPIREALKD-KDV 145
Cdd:cd08944    3 GKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAG----GALALRVDVTDEQQVAALFERAVEEfGGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPQYFTQLSEDklWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:cd08944   79 DLLVNNAGAMHLTPAIIDTDLAV--WDqTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAA 156
                        170       180       190
                 ....*....|....*....|....*....|..
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:cd08944  157 IRNLTRTLAAELRHAGIRCNALAPGLIDTPLL 188
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
70-255 1.33e-18

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: 83.50  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKlQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKD-KDVGIL 148
Cdd:cd05323    3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENP-GAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKfGRVDIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKK---GAIVTISSGSCCKPTPQLAAFSASKAYL 225
Cdd:cd05323   82 INNAGILDEKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKGgkgGVIVNIGSVAGLYPAPQFPVYSASKHGV 161
                        170       180       190
                 ....*....|....*....|....*....|.
gi 226371731 226 DHFSRALQYEYASK-GIFVQSLIPFYVATSM 255
Cdd:cd05323  162 VGFTRSLADLLEYKtGVRVNAICPGFTNTPL 192
PRK06841 PRK06841
short chain dehydrogenase; Provisional
67-253 1.56e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 83.55  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADtykvETDIIVADFSSGREIYLPIREALKD-KDV 145
Cdd:PRK06841  15 GKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGG----NAKGLVCDVSDSQSVEAAVAAVISAfGRI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPQyfTQLSEDkLWDI-INVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK06841  91 DILVNSAGVALLAPA--EDVSEE-DWDKtIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAG 167
                        170       180
                 ....*....|....*....|....*....
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK06841 168 VVGMTKVLALEWGPYGITVNAISPTVVLT 196
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
67-241 1.66e-18

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 83.39  E-value: 1.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQ-----VVAKDIADTYKVETdiIVAdfssgreiylpiREALK 141
Cdd:PRK08220   8 GKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEdypfaTFVLDVSDAAAVAQ--VCQ------------RLLAE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDVGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSAS 221
Cdd:PRK08220  74 TGPLDVLVNAAGILRMGA--TDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGAS 151
                        170       180
                 ....*....|....*....|
gi 226371731 222 KAYLDHFSRALQYEYASKGI 241
Cdd:PRK08220 152 KAALTSLAKCVGLELAPYGV 171
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
70-258 1.88e-18

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: 82.73  E-value: 1.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLN-IILISRNEEKLQVVAKdIADTYKvETDIIVADFSS-GREIYLPIREALKDKDVGI 147
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNtVIATCRDPSAATELAA-LGASHS-RLHILELDVTDeIAESAEAVAERLGDAGLDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 148 LVNNVGVFYPYpQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS--GSCCKPTP-QLAAFSASKAY 224
Cdd:cd05325   79 LINNAGILHSY-GPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSrvGSIGDNTSgGWYSYRASKAA 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:cd05325  158 LNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGP 191
PRK07825 PRK07825
short chain dehydrogenase; Provisional
67-257 2.88e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 83.07  E-value: 2.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI--ADTYKVEtdiiVADFSSGREIYLPIREALKDKD 144
Cdd:PRK07825   5 GKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELglVVGGPLD----VTDPASFAAFLDAVEADLGPID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VgiLVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK07825  81 V--LVNNAGVMPVGP--FLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHA 156
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK07825 157 VVGFTDAARLELRGTGVHVSVVLPSFVNTELIA 189
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
70-247 3.32e-18

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: 82.05  E-value: 3.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIA-----DTYKVETDiiVADFSSGREIYLPIREALKDKD 144
Cdd:cd05373    2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIrdaggSAKAVPTD--ARDEDEVIALFDLIEEEIGPLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VgiLVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:cd05373   80 V--LVYNAGANVWFP--ILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFA 155
                        170       180
                 ....*....|....*....|...
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLI 247
Cdd:cd05373  156 LRALAQSMARELGPKGIHVAHVI 178
PRK06523 PRK06523
short chain dehydrogenase; Provisional
67-253 5.72e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 81.87  E-value: 5.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRN-----EEKLQVVAkdiADTYKVETDIIVADfssgreiylPIREALK 141
Cdd:PRK06523   9 GKRALVTGGTKGIGAATVARLLEAGARVVTTARSrpddlPEGVEFVA---ADLTTAEGCAAVAR---------AVLERLG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDvgILVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQ-LAAFSA 220
Cdd:PRK06523  77 GVD--ILVHVLGGSSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPEsTTAYAA 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK06523 155 AKAALSTYSKSLSKEVAPKGVRVNTVSPGWIET 187
PRK07814 PRK07814
SDR family oxidoreductase;
67-254 6.54e-18

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 81.75  E-value: 6.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKvETDIIVADFSSGREiylpiREALKDKDVG 146
Cdd:PRK07814  10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGR-RAHVVAADLAHPEA-----TAGLAGQAVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ------ILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERK-KGAIVTISSGSCCKPTPQLAAFS 219
Cdd:PRK07814  84 afgrldIVVNNVGGTMPNP--LLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYG 161
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 220 ASKAYLDHFSRALQYEYASKgIFVQSLIPFYVATS 254
Cdd:PRK07814 162 TAKAALAHYTRLAALDLCPR-IRVNAIAPGSILTS 195
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
67-271 8.27e-18

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: 81.23  E-value: 8.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREAL-KDKDV 145
Cdd:cd08930    2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLeKFGRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGV-FYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS--------------GSCCK 210
Cdd:cd08930   82 DILINNAYPsPKVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASiygviapdfriyenTQMYS 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226371731 211 PtpqlAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMtaPSNFLHRCSWLVPS 271
Cdd:cd08930  162 P----VEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQ--PSEFLEKYTKKCPL 216
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
67-258 9.82e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 81.26  E-value: 9.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKlqvVAKDIADtYK---VETDIIVADFSSGREiylpIREALK-- 141
Cdd:PRK07097  10 GKIALITGASYGIGFAIAKAYAKAGATIVFNDINQEL---VDKGLAA-YRelgIEAHGYVCDVTDEDG----VQAMVSqi 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDVG---ILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTIssgscCKPTPQL--- 215
Cdd:PRK07097  82 EKEVGvidILVNNAGIIKRIP--MLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINI-----CSMMSELgre 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 226371731 216 --AAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:PRK07097 155 tvSAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAP 199
PRK07023 PRK07023
SDR family oxidoreductase;
70-257 1.36e-17

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 80.44  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNE---------EKLQVVAKDIADTYKVETDI---IVADFSSGREIYLpir 137
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARSRhpslaaaagERLAEVELDLSDAAAAAAWLagdLLAAFVDGASRVL--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 138 ealkdkdvgiLVNNVGVFYPYPQyFTQLSEDKLWDIINVNIAAASLMVHVVL---PGMVERKkgaIVTISSGSCCKPTPQ 214
Cdd:PRK07023  81 ----------LINNAGTVEPIGP-LATLDAAAIARAVGLNVAAPLMLTAALAqaaSDAAERR---ILHISSGAARNAYAG 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226371731 215 LAAFSASKAYLDHFSRALQYEyASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK07023 147 WSVYCATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGMQA 188
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
67-256 1.53e-17

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 80.60  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNI-ILISRNEEKLQVVAKDIADTYKVEtdiiVADFSSGREIYLPIREALKDKDV 145
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVaVLYNSAENEAKELREKGVFTIKCD----VGNRDQVKKSKEVVEKEFGRVDV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 giLVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS----GSCCKPTpqlAAFSAS 221
Cdd:PRK06463  83 --LVNNAGIMYLMP--FEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASnagiGTAAEGT---TFYAIT 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMT 190
PRK06484 PRK06484
short chain dehydrogenase; Validated
67-253 1.68e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 82.97  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTY-KVETDIivADFSSGREIYLPIREALKDKDV 145
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHlSVQADI--TDEAAVESAFAQIQARWGRLDV 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 giLVNNVGVFYPYPQYFTQLSEDkLWDIINVNIAAASLMVHVVLPGMveRKKGAIVTISSGSCCKPTPQLAAFSASKAYL 225
Cdd:PRK06484 347 --LVNNAGIAEVFKPSLEQSAED-FTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAV 421
                        170       180
                 ....*....|....*....|....*...
gi 226371731 226 DHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK06484 422 TMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK06138 PRK06138
SDR family oxidoreductase;
67-259 3.16e-17

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 79.81  E-value: 3.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVEtdIIVADFSSGREIylpirEALKDKDVG 146
Cdd:PRK06138   5 GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGGRAF--ARQGDVGSAEAV-----EALVDFVAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ------ILVNNVGvFYPYPQYFTQLSEDklWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFS 219
Cdd:PRK06138  78 rwgrldVLVNNAG-FGCGGTVVTTDEAD--WDaVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYV 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226371731 220 ASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPS 259
Cdd:PRK06138 155 ASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRI 194
PRK07326 PRK07326
SDR family oxidoreductase;
67-253 3.56e-17

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 79.28  E-value: 3.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKV---ETDiiVADFSSGREIYLPIREALKDK 143
Cdd:PRK07326   6 GKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVlglAAD--VRDEADVQRAVDAIVAAFGGL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DvgILVNN--VGVFYPypqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVeRKKGAIVTISSGSCCKPTPQLAAFSAS 221
Cdd:PRK07326  84 D--VLIANagVGHFAP----VEELTPEEWRLVIDTNLTGAFYTIKAAVPALK-RGGGYIINISSLAGTNFFAGGAAYNAS 156
                        170       180       190
                 ....*....|....*....|....*....|..
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK07326 157 KFGLVGFSEAAMLDLRQYGIKVSTIMPGSVAT 188
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
67-257 3.94e-17

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: 79.16  E-value: 3.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSG-----REIYLPIREALK 141
Cdd:cd05340    4 DRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLLTCtsencQQLAQRIAVNYP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDvGILvNNVGVFYPyPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSAS 221
Cdd:cd05340   84 RLD-GVL-HNAGLLGD-VCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVS 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:cd05340  161 KFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRA 196
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
67-252 5.40e-17

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 79.56  E-value: 5.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIA----DTYKVETDiiVADFSSGREIYLPIREALKD 142
Cdd:PRK08277  10 GKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKaaggEALAVKAD--VLDKESLEQARQQILEDFGP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDvgILVNNVG-------------VFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCC 209
Cdd:PRK08277  88 CD--ILINGAGgnhpkattdnefhELIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAF 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226371731 210 KPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP-FYVA 252
Cdd:PRK08277 166 TPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPgFFLT 209
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
67-257 5.84e-17

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: 78.96  E-value: 5.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADtykvETDIIVADFSSGREIYLPIREALKDKD-V 145
Cdd:cd05341    5 GKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGD----AARFFHLDVTDEDGWTAVVDTAREAFGrL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPQYFTQLSEdklWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:cd05341   81 DVLVNNAGILTGGTVETTTLEE---WRrLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGA 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 225 LDHFSRALQYEYASK--GIFVQSLIPFYVATSMTA 257
Cdd:cd05341  158 VRGLTKSAALECATQgyGIRVNSVHPGYIYTPMTD 192
PRK08339 PRK08339
short chain dehydrogenase; Provisional
67-254 6.15e-17

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 79.13  E-value: 6.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKDKDVG 146
Cdd:PRK08339   8 GKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTKREDLERTVKELKNIGEPD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ILVNNVGvfYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:PRK08339  88 IFFFSTG--GPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRISMA 165
                        170       180
                 ....*....|....*....|....*...
gi 226371731 227 HFSRALQYEYASKGIFVQSLIPFYVATS 254
Cdd:PRK08339 166 GLVRTLAKELGPKGITVNGIMPGIIRTD 193
PRK05872 PRK05872
short chain dehydrogenase; Provisional
67-256 6.35e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 79.63  E-value: 6.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI---ADTYKVETDiiVADFSSGREIYLPIREALKDK 143
Cdd:PRK05872   9 GKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELggdDRVLTVVAD--VTDLAAMQAAAEEAVERFGGI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DVgiLVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERkKGAIVTISSGSCCKPTPQLAAFSASKA 223
Cdd:PRK05872  87 DV--VVANAGIASGGS--VAQVDPDAFRRVIDVNLLGVFHTVRATLPALIER-RGYVLQVSSLAAFAAAPGMAAYCASKA 161
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:PRK05872 162 GVEAFANALRLEVAHHGVTVGSAYLSWIDTDLV 194
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
70-253 1.01e-16

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: 77.93  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKL-QVVAKDIADTYKVETDiiVADFSSGREIYLPIREALKDKDvgIL 148
Cdd:cd08929    3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLaAAAAQELEGVLGLAGD--VRDEADVRRAVDAMEEAFGGLD--AL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNN--VGVFYPypqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:cd08929   79 VNNagVGVMKP----VEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLL 154
                        170       180
                 ....*....|....*....|....*..
gi 226371731 227 HFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:cd08929  155 GLSEAAMLDLREANIRVVNVMPGSVDT 181
PRK07577 PRK07577
SDR family oxidoreductase;
68-255 1.29e-16

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 77.84  E-value: 1.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKL---QVVAKDIADTYKVETdiivadfssgreiylPIREALKDKD 144
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGIARSAIDDfpgELFACDLADIEQTAA---------------TLAQINEIHP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGScCKPTPQLAAFSASKAY 224
Cdd:PRK07577  69 VDAIVNNVGIALPQP--LGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA-IFGALDRTSYSAAKSA 145
                        170       180       190
                 ....*....|....*....|....*....|.
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK07577 146 LVGCTRTWALELAEYGITVNAVAPGPIETEL 176
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
67-248 2.04e-16

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: 77.57  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETdiIVADFSSGREIYLPIREALKD-KDV 145
Cdd:cd08937    4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEILAAGDAAHV--HTADLETYAGAQGVVRAAVERfGRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVG--VFYPYPQYFTqlsEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGScckpTPQL--AAFSAS 221
Cdd:cd08937   82 DVLINNVGgtIWAKPYEHYE---EEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIA----TRGIyrIPYSAA 154
                        170       180
                 ....*....|....*....|....*..
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:cd08937  155 KGGVNALTASLAFEHARDGIRVNAVAP 181
PRK08264 PRK08264
SDR family oxidoreductase;
67-257 2.43e-16

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 76.85  E-value: 2.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLN-IILISRNEEKlqvVAKDIADTYKVETDiiVADFSSgreiylpIREALKD-KD 144
Cdd:PRK08264   6 GKVVLVTGANRGIGRAFVEQLLARGAAkVYAAARDPES---VTDLGPRVVPLQLD--VTDPAS-------VAAAAEAaSD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPQYFTQlSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK08264  74 VTILVNNAGIFRTGSLLLEG-DEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAA 152
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK08264 153 AWSLTQALRAELAPQGTRVLGVHPGPIDTDMAA 185
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
70-255 2.61e-16

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: 77.12  E-value: 2.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAkDIADTYKVEtdiiVADFSSGREIYLPIREALKDKDvgILV 149
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYG-DPLRLTPLD----VADAAAVREVCSRLLAEHGPID--ALV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 150 NNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDHFS 229
Cdd:cd05331   74 NCAGVLRPGA--TDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLS 151
                        170       180
                 ....*....|....*....|....*.
gi 226371731 230 RALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:cd05331  152 KCLGLELAPYGVRCNVVSPGSTDTAM 177
PRK07774 PRK07774
SDR family oxidoreductase;
67-261 6.18e-16

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 75.94  E-value: 6.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADT--YKVETDIIVADFSSGREIYLPIREALKDKD 144
Cdd:PRK07774   6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADggTAIAVQVDVSDPDSAKAMADATVSAFGGID 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 vgILVNNVGVFYPYPQYF-TQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGscckptpqlAAFSAS-- 221
Cdd:PRK07774  86 --YLVNNAAIYGGMKLDLlITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSST---------AAWLYSnf 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226371731 222 ----KAYLDHFSRALQYEYASKGIFVQSLIPFYV---ATSMTAPSNF 261
Cdd:PRK07774 155 yglaKVGLNGLTQQLARELGGMNIRVNAIAPGPIdteATRTVTPKEF 201
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
67-243 6.80e-16

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 75.91  E-value: 6.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILI-SRNEEKLQVVAKDI----ADTYKVETDiiVADFSSGREIYLPIREALK 141
Cdd:PRK08063   4 GKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIealgRKALAVKAN--VGDVEKIKEMFAQIDEEFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDVgiLVNNV--GVFYPypqyFTQLSEdKLWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAF 218
Cdd:PRK08063  82 RLDV--FVNNAasGVLRP----AMELEE-SHWDwTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTV 154
                        170       180
                 ....*....|....*....|....*
gi 226371731 219 SASKAYLDHFSRALQYEYASKGIFV 243
Cdd:PRK08063 155 GVSKAALEALTRYLAVELAPKGIAV 179
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
67-257 7.27e-16

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 75.92  E-value: 7.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKlqvVAKDIADTYKV---ETDIIVADFSSGREIYLPIREALKD- 142
Cdd:PRK08936   7 GKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEE---EANDVAEEIKKaggEAIAVKGDVTVESDVVNLIQTAVKEf 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDVGILVNNVGVFYPYPQYFTQLSEdklWD-IINVNIAAASLMVHVVLPGMVER-KKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:PRK08936  84 GTLDVMINNAGIENAVPSHEMSLED---WNkVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPLFVHYAA 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK08936 161 SKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINA 197
PRK12827 PRK12827
short chain dehydrogenase; Provisional
67-255 7.91e-16

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 75.91  E-value: 7.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILIS----RNEEKLQVVAKDI----ADTYKVETDiiVADFSSGREIYLPIRE 138
Cdd:PRK12827   6 SRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIeaagGKALGLAFD--VRDFAATRAALDAGVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 139 ALKDKDvgILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVE-RKKGAIVTISSGSCCKPTPQLAA 217
Cdd:PRK12827  84 EFGRLD--ILVNNAGIATDAA--FAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIASVAGVRGNRGQVN 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226371731 218 FSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK12827 160 YAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPM 197
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
67-256 8.06e-16

(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: 75.82  E-value: 8.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIIL-----ISRNEEKLQVVAKDIADTYKVETDIIVADFSS---GREIylpIRE 138
Cdd:cd05353    5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggDRKGSGKSSSAADKVVDEIKAAGGKAVANYDSvedGEKI---VKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 139 ALKD-KDVGILVNNVGVFypYPQYFTQLSEDkLWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLA 216
Cdd:cd05353   82 AIDAfGRVDILVNNAGIL--RDRSFAKMSEE-DWDlVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226371731 217 AFSASKAYLDHFSRALQYEYASKGIFVQSLIPfYVATSMT 256
Cdd:cd05353  159 NYSAAKLGLLGLSNTLAIEGAKYNITCNTIAP-AAGSRMT 197
PRK06139 PRK06139
SDR family oxidoreductase;
67-290 8.23e-16

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 77.07  E-value: 8.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI----ADTYKVETDIIVADFSsgreiylpirEALKD 142
Cdd:PRK06139   7 GAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECralgAEVLVVPTDVTDADQV----------KALAT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 K------DVGILVNNVGV-----FYPYPqyfTQLSEDklwdIINVNIAAASLMVHVVLPGMVERKKGAIV-TISSGSCCK 210
Cdd:PRK06139  77 QaasfggRIDVWVNNVGVgavgrFEETP---IEAHEQ----VIQTNLIGYMRDAHAALPIFKKQGHGIFInMISLGGFAA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 211 pTPQLAAFSASKAYLDHFSRALQYEYASK-GIFVQSLIPFYVAT-SMTAPSNFLHRCswLVPSPKVY----AHHAVSTLG 284
Cdd:PRK06139 150 -QPYAAAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDTpGFRHGANYTGRR--LTPPPPVYdprrVAKAVVRLA 226

                 ....*.
gi 226371731 285 ISKRTT 290
Cdd:PRK06139 227 DRPRAT 232
PRK05867 PRK05867
SDR family oxidoreductase;
61-274 9.05e-16

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 75.84  E-value: 9.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  61 DLIKQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIA----DTYKVETDIIVADFSSGreiyLPI 136
Cdd:PRK05867   3 DLFDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGtsggKVVPVCCDVSQHQQVTS----MLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 137 REALKDKDVGILVNNVGVFYPYPQYFTQLSEdkLWDIINVNIAAASLMVHVVLPGMVER-KKGAIVTIS--SGSCCKPTP 213
Cdd:PRK05867  79 QVTAELGGIDIAVCNAGIITVTPMLDMPLEE--FQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTAsmSGHIINVPQ 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226371731 214 QLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSNFLHRcSWlvpSPKV 274
Cdd:PRK05867 157 QVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQP-LW---EPKI 213
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
67-248 9.79e-16

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: 75.51  E-value: 9.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEklqvvakdiADTYKVETDIIVADFSSGREIY------LPIREAL 140
Cdd:cd05338    3 GKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTAS---------EGDNGSAKSLPGTIEETAEEIEaaggqaLPIVVDV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 141 KDKD---------------VGILVNNVGVFypypqyFTQLSED---KLWDII-NVNIAAASLMVHVVLPGMVERKKGAIV 201
Cdd:cd05338   74 RDEDqvralveatvdqfgrLDILVNNAGAI------WLSLVEDtpaKRFDLMqRVNLRGTYLLSQAALPHMVKAGQGHIL 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226371731 202 TISSGSCCKPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:cd05338  148 NISPPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWP 194
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
70-259 1.01e-15

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: 75.58  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNE-----EKLQVVAKDIADTYKVETDIivADFSSGREIYLPIREALKDKD 144
Cdd:cd05337    4 AIVTGASRGIGRAIATELAARGFDIAINDLPDddqatEVVAEVLAAGRRAIYFQADI--GELSDHEALLDQAWEDFGRLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VgiLVNNVGVFYPYPQYFTQLSEDKLWDIINVNI--------AAASLMVHVvlPGMVERKKGAIVTISSGSCCKPTPQLA 216
Cdd:cd05337   82 C--LVNNAGIAVRPRGDLLDLTEDSFDRLIAINLrgpffltqAVARRMVEQ--PDRFDGPHRSIIFVTSINAYLVSPNRG 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226371731 217 AFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPS 259
Cdd:cd05337  158 EYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPV 200
PRK07478 PRK07478
short chain dehydrogenase; Provisional
67-256 1.29e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 75.35  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSgrEIYlpiREALKDKDVG 146
Cdd:PRK07478   6 GKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAE-GGEAVALAGDVRD--EAY---AKALVALAVE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ------ILVNNVGVFYPyPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS--GSCCKpTPQLAAF 218
Cdd:PRK07478  80 rfggldIAFNNAGTLGE-MGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTfvGHTAG-FPGMAAY 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226371731 219 SASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:PRK07478 158 AASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMG 195
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
67-253 1.31e-15

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 75.31  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPIREALKD-KDV 145
Cdd:PRK12429   4 GKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKA-GGKAIGVAMDVTDEEAINAGIDYAVETfGGV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS-----GSCCKptpqlAAFSA 220
Cdd:PRK12429  83 DILVNNAGIQHVAP--IEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASvhglvGSAGK-----AAYVS 155
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK12429 156 AKHGLIGLTKVVALEGATHGVTVNAICPGYVDT 188
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
67-243 1.68e-15

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 77.19  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETdiIVADFSSGREiylpIREALKD--KD 144
Cdd:PRK08324 422 GKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRALG--VACDVTDEAA----VQAAFEEaaLA 495
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VG---ILVNNVGVFYPYPqyFTQLSeDKLWD-IINVNI--------AAASLMVHVVLPgmverkkGAIVTISSGSCCKPT 212
Cdd:PRK08324 496 FGgvdIVVSNAGIAISGP--IEETS-DEDWRrSFDVNAtghflvarEAVRIMKAQGLG-------GSIVFIASKNAVNPG 565
                        170       180       190
                 ....*....|....*....|....*....|.
gi 226371731 213 PQLAAFSASKAYLDHFSRALQYEYASKGIFV 243
Cdd:PRK08324 566 PNFGAYGAAKAAELHLVRQLALELGPDGIRV 596
PRK07890 PRK07890
short chain dehydrogenase; Provisional
67-251 1.72e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 74.99  E-value: 1.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADT----YKVETDIivADFSSGREIYLPIREALKD 142
Cdd:PRK07890   5 GKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLgrraLAVPTDI--TDEDQCANLVALALERFGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDVgiLVNNVGVfYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVErKKGAIVTISSGSCCKPTPQLAAFSASK 222
Cdd:PRK07890  83 VDA--LVNNAFR-VPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAE-SGGSIVMINSMVLRHSQPKYGAYKMAK 158
                        170       180
                 ....*....|....*....|....*....
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIPFYV 251
Cdd:PRK07890 159 GALLAASQSLATELGPQGIRVNSVAPGYI 187
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
67-248 2.02e-15

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: 74.74  E-value: 2.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKdiADTYKVETDIIVADFSSGREIYLPIREALKD-KDV 145
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAE--AAQGGPRALGVQCDVTSEAQVQSAFEQAVLEfGGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPqyFTQLSeDKLWDI-INVNIAAASLMVHVVLPGMVERKKGA-IVTISSGSCCKPTPQLAAFSASKA 223
Cdd:cd08943   79 DIVVSNAGIATSSP--IAETS-LEDWNRsMDINLTGHFLVSREAFRIMKSQGIGGnIVFNASKNAVAPGPNAAAYSAAKA 155
                        170       180
                 ....*....|....*....|....*
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:cd08943  156 AEAHLARCLALEGGEDGIRVNTVNP 180
PRK06124 PRK06124
SDR family oxidoreductase;
67-258 2.68e-15

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 74.36  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQ--------------VVAKDIADTYKVETDIIVADFSSGRei 132
Cdd:PRK06124  11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEaavaalraaggaaeALAFDIADEEAVAAAFARIDAEHGR-- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 133 ylpirealkdkdVGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPT 212
Cdd:PRK06124  89 ------------LDILVNNVGARDRRP--LAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVAR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226371731 213 PQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:PRK06124 155 AGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAA 200
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
67-257 2.69e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 74.42  E-value: 2.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREiylpIREALK--DKD 144
Cdd:PRK07523  10 GRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQ-GLSAHALAFDVTDHDA----VRAAIDafEAE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VG---ILVNNVGVfypypQYFTQLSE---DKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAF 218
Cdd:PRK07523  85 IGpidILVNNAGM-----QFRTPLEDfpaDAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPY 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226371731 219 SASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK07523 160 TATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNA 198
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
67-271 2.97e-15

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: 74.09  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIyLPIREALKDK--D 144
Cdd:cd05343    6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNEEQI-LSMFSAIRTQhqG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPqyftqLSEDKL--W-DIINVNIAAASLMVHVVLPGMVERK--KGAIVTISS--GSCCKPTPQLAA 217
Cdd:cd05343   85 VDVCINNAGLARPEP-----LLSGKTegWkEMFDVNVLALSICTREAYQSMKERNvdDGHIININSmsGHRVPPVSVFHF 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226371731 218 FSASKAYLDHFSRALQYE--YASKGIFVQSLIPFYVATsmtapsNFLHRCSWLVPS 271
Cdd:cd05343  160 YAATKHAVTALTEGLRQElrEAKTHIRATSISPGLVET------EFAFKLHDNDPE 209
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
67-257 3.43e-15

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 74.16  E-value: 3.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPI-REALKDKDV 145
Cdd:PRK13394   7 GKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKA-GGKAIGVAMDVTNEDAVNAGIdKVAERFGSV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMV-ERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK13394  86 DILVSNAGIQIVNP--IENYSFADWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSVHSHEASPLKSAYVTAKHG 163
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK13394 164 LLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVD 196
PRK06114 PRK06114
SDR family oxidoreductase;
61-255 4.76e-15

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 73.66  E-value: 4.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  61 DLIKQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEK-LQVVAKDIADTYKvETDIIVADFSSGREIYLPIreA 139
Cdd:PRK06114   2 QLFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAETAEHIEAAGR-RAIQIAADVTSKADLRAAV--A 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 140 LKDKDVGIL---VNNVGVFYPYPQyfTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS--GSCCKPTPQ 214
Cdd:PRK06114  79 RTEAELGALtlaVNAAGIANANPA--EEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASmsGIIVNRGLL 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226371731 215 LAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK06114 157 QAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPM 197
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
67-248 5.11e-15

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: 73.39  E-value: 5.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALK-DKDV 145
Cdd:cd05369    3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKeFGKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPqyFTQLSEdKLWD-IINVNIAAASLMVHVVLPGMVERKKGA-IVTISSGSCCKPTPQLAAFSASKA 223
Cdd:cd05369   83 DILINNAAGNFLAP--AESLSP-NGFKtVIDIDLNGTFNTTKAVGKRLIEAKHGGsILNISATYAYTGSPFQVHSAAAKA 159
                        170       180
                 ....*....|....*....|....*
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:cd05369  160 GVDALTRSLAVEWGPYGIRVNAIAP 184
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
67-248 7.34e-15

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 73.12  E-value: 7.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQvvakdiADTYK-VETDIivadfSSGREIYLPIREAL-KDKD 144
Cdd:PRK06171   9 GKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQ------HENYQfVPTDV-----SSAEEVNHTVAEIIeKFGR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYP---------YPQYftQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQL 215
Cdd:PRK06171  78 IDGLVNNAGINIPrllvdekdpAGKY--ELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQ 155
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 216 AAFSASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK06171 156 SCYAATKAALNSFTRSWAKELGKHNIRVVGVAP 188
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
71-257 7.99e-15

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 72.69  E-value: 7.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLniilisrneeklQVVAKDIADTYKVETDI--IVADFSSGREiylPIREALKDKDvgIL 148
Cdd:PRK06550   9 LITGAASGIGLAQARAFLAQGA------------QVYGVDKQDKPDLSGNFhfLQLDLSDDLE---PLFDWVPSVD--IL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGVFYPYpQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS--------GScckptpqlAAFSA 220
Cdd:PRK06550  72 CNTAGILDDY-KPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSiasfvaggGG--------AAYTA 142
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK06550 143 SKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTA 179
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
67-258 9.59e-15

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: 72.80  E-value: 9.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIIL-----ISRNEEKLQVVAKDIADTYKVETDI-----IVADFSSGREIYLPI 136
Cdd:cd05358    3 GKVALVTGASSGIGKAIAIRLATAGANVVVnyrskEDAAEEVVEEIKAVGGKAIAVQADVskeedVVALFQSAIKEFGTL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 137 realkdkdvGILVNNVGVFYPYPQYFTQLSEdklWD-IINVNIAAASLMVHVVLPGMVE-RKKGAIVTISSGSCCKPTPQ 214
Cdd:cd05358   83 ---------DILVNNAGLQGDASSHEMTLED---WNkVIDVNLTGQFLCAREAIKRFRKsKIKGKIINMSSVHEKIPWPG 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226371731 215 LAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:cd05358  151 HVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAE 194
PRK08589 PRK08589
SDR family oxidoreductase;
70-253 1.02e-14

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 72.89  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNeEKLQVVAKDI------ADTYKVEtdiiVADFSSGREIYLPIREALKDK 143
Cdd:PRK08589   9 AVITGASTGIGQASAIALAQEGAYVLAVDIA-EAVSETVDKIksnggkAKAYHVD----ISDEQQVKDFASEIKEQFGRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DVgiLVNNVGV------FYPYPQyftqlsedKLWD-IINVNIAAASLMVHVVLPGMVErKKGAIVTISSGSCCKPTPQLA 216
Cdd:PRK08589  84 DV--LFNNAGVdnaagrIHEYPV--------DVFDkIMAVDMRGTFLMTKMLLPLMME-QGGSIINTSSFSGQAADLYRS 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 217 AFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK08589 153 GYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIET 189
PRK06172 PRK06172
SDR family oxidoreductase;
66-255 1.06e-14

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 72.48  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  66 YGRWAVVSGATDGIGKAYAEELASRGLNIILISRN----EEKLQVVAKDIADTYKVETDIIVADfssgrEIylpirEALK 141
Cdd:PRK06172   6 SGKVALVTGGAAGIGRATALAFAREGAKVVVADRDaaggEETVALIREAGGEALFVACDVTRDA-----EV-----KALV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDVGIL------VNNVGVFYPYPQYFTQlSEDkLWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQ 214
Cdd:PRK06172  76 EQTIAAYgrldyaFNNAGIEIEQGRLAEG-SEA-EFDaIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPK 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226371731 215 LAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK06172 154 MSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM 194
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
67-257 1.08e-14

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 72.73  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIIL-ISRNEEKLQVVAKDIA----DTYKVEtdiivADFSSGREIYLPIREALK 141
Cdd:PRK12935   6 GKVAIVTGGAKGIGKAITVALAQEGAKVVInYNSSKEAAENLVNELGkeghDVYAVQ-----ADVSKVEDANRLVEEAVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 D-KDVGILVNNVGVfyPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:PRK12935  81 HfGKVDILVNNAGI--TRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSA 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK12935 159 AKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVA 195
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
61-258 1.10e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 72.48  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  61 DLIKQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADT-YKVETdiIVADFSSGREIYLPIREA 139
Cdd:PRK08085   3 DLFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEgIKAHA--APFNVTHKQEVEAAIEHI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 140 lkDKDVG---ILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLA 216
Cdd:PRK08085  81 --EKDIGpidVLINNAGIQRRHP--FTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTIT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226371731 217 AFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:PRK08085 157 PYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKA 198
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
60-258 1.29e-14

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 72.46  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  60 ADLIKQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRN---EEKLQVVAKdiaDTYKVEtdIIVADFSSGREIYLPI 136
Cdd:PRK06935   8 MDFFSLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGtnwDETRRLIEK---EGRKVT--FVQVDLTKPESAEKVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 137 REALKD-KDVGILVNNVGVFYPYPqyftqLSE--DKLWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPT 212
Cdd:PRK06935  83 KEALEEfGKIDILVNNAGTIRRAP-----LLEykDEDWNaVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGG 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226371731 213 PQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:PRK06935 158 KFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAP 203
PRK06398 PRK06398
aldose dehydrogenase; Validated
70-239 1.43e-14

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 72.56  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKlqvvakdiadtyKVETDIIVADFSSGREIYLPIREALKD-KDVGIL 148
Cdd:PRK06398   9 AIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS------------YNDVDYFKVDVSNKEQVIKGIDYVISKyGRIDIL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGVFYPYPQYFTQLSEdklWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDH 227
Cdd:PRK06398  77 VNNAGIESYGAIHAVEEDE---WDrIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVLG 153
                        170
                 ....*....|..
gi 226371731 228 FSRALQYEYASK 239
Cdd:PRK06398 154 LTRSIAVDYAPT 165
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
67-248 1.80e-14

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 71.90  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETdiIVAD---FSSGREIYLPIREALKDK 143
Cdd:PRK12823   8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHEVAAELRAAGGEALA--LTADletYAGAQAAMAAAVEAFGRI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DvgILVNNVG---VFYPYPQYftqlSEDKLWDIINvniaaASLM-----VHVVLPGMVERKKGAIVTISSgscckptpqL 215
Cdd:PRK12823  86 D--VLINNVGgtiWAKPFEEY----EEEQIEAEIR-----RSLFptlwcCRAVLPHMLAQGGGAIVNVSS---------I 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226371731 216 AA-------FSASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK12823 146 ATrginrvpYSAAKGGVNALTASLAFEYAEHGIRVNAVAP 185
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
67-261 1.97e-14

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: 72.32  E-value: 1.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLN--IILISRNEEKLQVVAKDI----ADTYKVETDIIVADFSsgREIYLPIREAL 140
Cdd:cd05355   26 GKKALITGGDSGIGRAVAIAFAREGADvaINYLPEEEDDAEETKKLIeeegRKCLLIPGDLGDESFC--RDLVKEVVKEF 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 141 KDKDvgILVNNVGVFYPYpQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMverKKGA-IVTISSGSCCKPTPQLAAFS 219
Cdd:cd05355  104 GKLD--ILVNNAAYQHPQ-ESIEDITTEQLEKTFRTNIFSMFYLTKAALPHL---KKGSsIINTTSVTAYKGSPHLLDYA 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226371731 220 ASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTaPSNF 261
Cdd:cd05355  178 ATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLI-PSSF 218
PRK07074 PRK07074
SDR family oxidoreductase;
68-253 2.41e-14

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 71.72  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVEtdiIVADFSSGREIYLPIREALKDKD-VG 146
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFVP---VACDLTDAASLAAALANAAAERGpVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ILVNNVGVfypypQYFTQLSED--KLWDIIN-VNIAAASLMVHVVLPGMVERKKGAIVTISS--GSCCKPTPqlaAFSAS 221
Cdd:PRK07074  80 VLVANAGA-----ARAASLHDTtpASWRADNaLNLEAAYLCVEAVLEGMLKRSRGAVVNIGSvnGMAALGHP---AYSAA 151
                        170       180       190
                 ....*....|....*....|....*....|..
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK07074 152 KAGLIHYTKLLAVEYGRFGIRANAVAPGTVKT 183
PRK07035 PRK07035
SDR family oxidoreductase;
67-248 2.45e-14

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 71.59  E-value: 2.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI-ADTYKVET--------DIIVADFSSgreiylpIR 137
Cdd:PRK07035   8 GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIvAAGGKAEAlachigemEQIDALFAH-------IR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 138 EALKDKDvgILVNNVGVfypYPQYFTQLSED-----KLWDiinVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPT 212
Cdd:PRK07035  81 ERHGRLD--ILVNNAAA---NPYFGHILDTDlgafqKTVD---VNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPG 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 213 PQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK07035 153 DFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLP 188
PRK12743 PRK12743
SDR family oxidoreductase;
68-256 2.46e-14

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 71.60  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNI-ILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYlPIREALKDK--D 144
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKETAEEVRSH-GVRAEIRQLDLSDLPEGA-QALDKLIQRlgR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGA-IVTISSGSCCKPTPQLAAFSASKA 223
Cdd:PRK12743  81 IDVLVNNAGAMTKAP--FLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQGGrIINITSVHEHTPLPGASAYTAAKH 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:PRK12743 159 ALGGLTKAMALELVEHGILVNAVAPGAIATPMN 191
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
68-255 2.66e-14

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 71.58  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIIL-----ISRNEEKLQVVAKDIADTYKVETDiiVADFSSGREIYLPIREALKD 142
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnSPRRVKWLEDQKALGFDFIASEGN--VGDWDSTKAAFDKVKAEVGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDVgiLVNNVGVfyPYPQYFTQLSEDKlWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSAS 221
Cdd:PRK12938  82 IDV--LVNNAGI--TRDVVFRKMTRED-WTaVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTA 156
                        170       180       190
                 ....*....|....*....|....*....|....
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK12938 157 KAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDM 190
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
67-255 2.68e-14

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: 71.64  E-value: 2.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKD-KDV 145
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKfGSF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERK-KGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:cd05366   82 DVMVNNAGIAPITP--LLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSASKFA 159
                        170       180       190
                 ....*....|....*....|....*....|.
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:cd05366  160 VRGLTQTAAQELAPKGITVNAYAPGIVKTEM 190
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
71-257 3.46e-14

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 71.14  E-value: 3.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADtYKVETDIIVADFSSGREIYLPIREALKD-KDVGILV 149
Cdd:PRK08217   9 VITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGA-LGTEVRGYAANVTDEEDVEATFAQIAEDfGQLNGLI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 150 NNVGVF-------YPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVE-RKKGAIVTISSGSCCKPTPQlAAFSAS 221
Cdd:PRK08217  88 NNAGILrdgllvkAKDGKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMIEsGSKGVIINISSIARAGNMGQ-TNYSAS 166
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK08217 167 KAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTA 202
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
68-257 6.90e-14

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 70.10  E-value: 6.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNE------------EKLQVVAKDIADTYKVETDIivadfssgREIYLP 135
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTEnkeltklaeqynSNLTFHSLDLQDVHELETNF--------NEILSS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 136 IRealKDKDVGI-LVNNVGVFYPYPQyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERK-KGAIVTISSGSCCKPTP 213
Cdd:PRK06924  74 IQ---EDNVSSIhLINNAGMVAPIKP-IEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKvDKRVINISSGAAKNPYF 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226371731 214 QLAAFSASKAYLDHFSRALQYEYASKGIFVQsLIPFY---VATSMTA 257
Cdd:PRK06924 150 GWSAYCSSKAGLDMFTQTVATEQEEEEYPVK-IVAFSpgvMDTNMQA 195
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
72-248 1.03e-13

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 69.79  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  72 VSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADT-YKVETDiiVADFSSGREIYLPIREALKDKDVgiLVN 150
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNlYIAQLD--VRNRAAIEEMLASLPAEWRNIDV--LVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 151 NVGVFYPYPQYFTQLSEDklWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDHFS 229
Cdd:PRK10538  81 NAGLALGLEPAHKASVED--WEtMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFS 158
                        170
                 ....*....|....*....
gi 226371731 230 RALQYEYASKGIFVQSLIP 248
Cdd:PRK10538 159 LNLRTDLHGTAVRVTDIEP 177
PRK06057 PRK06057
short chain dehydrogenase; Provisional
67-253 1.48e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 69.37  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYkVETDIIVAD-----FSSGREIYlpirealk 141
Cdd:PRK06057   7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLF-VPTDVTDEDavnalFDTAAETY-------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 dKDVGILVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS-----GSCckpTPQLa 216
Cdd:PRK06057  78 -GSVDIAFNNAGISPPEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASfvavmGSA---TSQI- 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 217 AFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK06057 153 SYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNT 189
PRK06125 PRK06125
short chain dehydrogenase; Provisional
67-253 1.66e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 69.30  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREiylpiREALKDK--D 144
Cdd:PRK06125   7 GKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVHALDLSSPEA-----REQLAAEagD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFypyPQYFTQLSEDKLWDiinvniAAASLMVH-------VVLPGMVERKKGAIVTISSGSCCKPTPQLAA 217
Cdd:PRK06125  82 IDILVNNAGAI---PGGGLDDVDDAAWR------AGWELKVFgyidltrLAYPRMKARGSGVIVNVIGAAGENPDADYIC 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 218 FSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK06125 153 GSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVAT 188
PRK06198 PRK06198
short chain dehydrogenase; Provisional
67-253 2.77e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 68.49  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGL-NIILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIYLPIREALKDKD- 144
Cdd:PRK06198   6 GKVALVTGGTQGLGAAIARAFAERGAaGLVICGRNAEKGEAQAAELEAL-GAKAVFVQADLSDVEDCRRVVAAADEAFGr 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVfypyPQYFTQLSED-KLWD-IINVNIAAASLMVHVVLPGMVERK-KGAIVTISSGSCCKPTPQLAAFSAS 221
Cdd:PRK06198  85 LDALVNAAGL----TDRGTILDTSpELFDrHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSMSAHGGQPFLAAYCAS 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK06198 161 KGALATLTRNAAYALLRNRIRVNGLNIGWMAT 192
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
67-255 3.64e-13

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: 68.25  E-value: 3.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI--ADTYKVETDIIVADfssgrEIYLPIREALKD-K 143
Cdd:cd05326    4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELgdPDISFVHCDVTVEA-----DVRAAVDTAVARfG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DVGILVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKA 223
Cdd:cd05326   79 RLDIMFNNAGVLGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKH 158
                        170       180       190
                 ....*....|....*....|....*....|..
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:cd05326  159 AVLGLTRSAATELGEHGIRVNCVSPYGVATPL 190
PRK07109 PRK07109
short chain dehydrogenase; Provisional
70-235 3.74e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 69.18  E-value: 3.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI----ADTYKVETDiiVADFSSGREIYLPIREALKDKDV 145
Cdd:PRK07109  11 VVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIraagGEALAVVAD--VADAEAVQAAADRAEEELGPIDT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 giLVNN--VGVFYPY----PQYFTQLSEDKLWDIINVNIAAaslmvhvvLPGMVERKKGAIVTISSGSCCKPTPQLAAFS 219
Cdd:PRK07109  89 --WVNNamVTVFGPFedvtPEEFRRVTEVTYLGVVHGTLAA--------LRHMRPRDRGAIIQVGSALAYRSIPLQSAYC 158
                        170
                 ....*....|....*.
gi 226371731 220 ASKAYLDHFSRALQYE 235
Cdd:PRK07109 159 AAKHAIRGFTDSLRCE 174
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
58-257 4.84e-13

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 67.95  E-value: 4.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  58 SRADLIKQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIAD----TYKVETDIivadfSSGREIY 133
Cdd:PRK06113   2 FNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQlggqAFACRCDI-----TSEQELS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 134 LPIREAL-KDKDVGILVNNVGVFYPYPqyFTQLSEDKLWdIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPT 212
Cdd:PRK06113  77 ALADFALsKLGKVDILVNNAGGGGPKP--FDMPMADFRR-AYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKN 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 226371731 213 PQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK06113 154 INMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALK 198
PRK08267 PRK08267
SDR family oxidoreductase;
72-264 6.79e-13

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 67.66  E-value: 6.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  72 VSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIAD----------TYKVETDIIVADFSSGreiylpirealK 141
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAgnawtgaldvTDRAAWDAALADFAAA-----------T 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDVGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPgMVERKKGA-IVTISSGSCCKPTPQLAAFSA 220
Cdd:PRK08267  75 GGRLDVLFNNAGILRGGP--FEDIPLEAHDRVIDINVKGVLNGAHAALP-YLKATPGArVINTSSASAIYGQPGLAVYSA 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSNFLHR 264
Cdd:PRK08267 152 TKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVD 195
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
71-240 7.49e-13

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: 67.02  E-value: 7.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI----ADTYKVETDiiVADFSSGREIYLPIREALKDKDVg 146
Cdd:cd05360    4 VITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVrelgGEAIAVVAD--VADAAQVERAADTAVERFGRIDT- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 iLVNN--VGVFYPY----PQYFTQLSEDKLWDIINVNIAAaslmvhvvLPGMVERKKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:cd05360   81 -WVNNagVAVFGRFedvtPEEFRRVFDVNYLGHVYGTLAA--------LPHLRRRGGGALINVGSLLGYRSAPLQAAYSA 151
                        170       180
                 ....*....|....*....|
gi 226371731 221 SKAYLDHFSRALQYEYASKG 240
Cdd:cd05360  152 SKHAVRGFTESLRAELAHDG 171
PRK05855 PRK05855
SDR family oxidoreductase;
67-261 2.23e-12

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 67.70  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI------ADTYKVetdiivaDFSSGREIylpirEAL 140
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIraagavAHAYRV-------DVSDADAM-----EAF 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 141 KDkDVG-------ILVNNVGVFYPYPqyFTQLSEDKlWD-IINVNIAAaslmvhvVLPG-------MVERKKGA-IVTIS 204
Cdd:PRK05855 383 AE-WVRaehgvpdIVVNNAGIGMAGG--FLDTSAED-WDrVLDVNLWG-------VIHGcrlfgrqMVERGTGGhIVNVA 451
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226371731 205 SGSCCKPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSNF 261
Cdd:PRK05855 452 SAAAYAPSRSLPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVATTRF 508
PRK06179 PRK06179
short chain dehydrogenase; Provisional
70-257 3.12e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 65.69  E-value: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQ------VVAKDIADTYKVETDIivadfssgREIylpIREAlkdK 143
Cdd:PRK06179   7 ALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAApipgveLLELDVTDDASVQAAV--------DEV---IARA---G 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DVGILVNNVGVFYPYPQYFTQLSEDKlwDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKA 223
Cdd:PRK06179  73 RIDVLVNNAGVGLAGAAEESSIAQAQ--ALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKH 150
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 224 YLDHFSRALQYEYASKGIFVqSLI-PFYVATSMTA 257
Cdd:PRK06179 151 AVEGYSESLDHEVRQFGIRV-SLVePAYTKTNFDA 184
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
66-255 4.04e-12

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 65.43  E-value: 4.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  66 YGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIAD-TYKVETDiiVADFSSgreIYLPIREALKDKD 144
Cdd:PRK07067   5 QGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPaAIAVSLD--VTRQDS---IDRIVAAAVERFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 -VGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGA-IVTISSGSCCKPTPQLAAFSASK 222
Cdd:PRK07067  80 gIDILFNNAALFDMAP--ILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGGkIINMASQAGRRGEALVSHYCATK 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK07067 158 AAVISYTQSAALALIRHGINVNAIAPGVVDTPM 190
PRK09291 PRK09291
SDR family oxidoreductase;
72-248 4.40e-12

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 65.02  E-value: 4.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  72 VSGATDGIGKAYAEELASRGLNIIliSRNEEKLQVVA-KDIADTYKVETDIIVADFSSGREIylpiREALkDKDVGILVN 150
Cdd:PRK09291   7 ITGAGSGFGREVALRLARKGHNVI--AGVQIAPQVTAlRAEAARRGLALRVEKLDLTDAIDR----AQAA-EWDVDVLLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 151 NVGVFYPYPqyftqlsedkLWDI--------INVNIAAASLMVHVVLPGMVERKKGAIVTISS-GSCCKPtPQLAAFSAS 221
Cdd:PRK09291  80 NAGIGEAGA----------VVDIpvelvrelFETNVFGPLELTQGFVRKMVARGKGKVVFTSSmAGLITG-PFTGAYCAS 148
                        170       180
                 ....*....|....*....|....*..
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK09291 149 KHALEAIAEAMHAELKPFGIQVATVNP 175
PRK07832 PRK07832
SDR family oxidoreductase;
70-256 6.10e-12

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 65.06  E-value: 6.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIAD-----TYKVETDIivADFSSGREIYLPIREALKDKD 144
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARAlggtvPEHRALDI--SDYDAVAAFAADIHAAHGSMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VgiLVNNVGV-FYPYPQyftQLSEDKLWDIINVNiaaasLM--VHVV---LPGMVE-RKKGAIVTISSGSCCKPTPQLAA 217
Cdd:PRK07832  81 V--VMNIAGIsAWGTVD---RLTHEQWRRMVDVN-----LMgpIHVIetfVPPMVAaGRGGHLVNVSSAAGLVALPWHAA 150
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226371731 218 FSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:PRK07832 151 YSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLV 189
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
70-255 6.24e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 64.75  E-value: 6.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKvETDIIVADFSSGREIYLPIREALKD-KDVGIL 148
Cdd:PRK08643   5 ALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGG-KAIAVKADVSDRDQVFAAVRQVVDTfGDLNVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAaslmvhvVLPGM---VERKK-----GAIVTISSGSCCKPTPQLAAFSA 220
Cdd:PRK08643  84 VNNAGVAPTTP--IETITEEQFDKVYNINVGG-------VIWGIqaaQEAFKklghgGKIINATSQAGVVGNPELAVYSS 154
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK08643 155 TKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPM 189
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
67-248 7.66e-12

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 64.42  E-value: 7.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGAT--DGIGKAYAEELASRGLNI---------------------ILISRNEEKLQVVAKDIadtykvETDIIV 123
Cdd:PRK12859   6 NKVAVVTGVSrlDGIGAAICKELAEAGADIfftywtaydkempwgvdqdeqIQLQEELLKNGVKVSSM------ELDLTQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 124 ADfsSGREIYLPIREALKDKDvgILVNNVGvfYPYPQYFTQLSEDKLWDIINVNIAAaSLMVHVVLPGMVERKKGA-IVT 202
Cdd:PRK12859  80 ND--APKELLNKVTEQLGYPH--ILVNNAA--YSTNNDFSNLTAEELDKHYMVNVRA-TTLLSSQFARGFDKKSGGrIIN 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226371731 203 ISSGSCCKPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK12859 153 MTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINP 198
PRK07856 PRK07856
SDR family oxidoreductase;
67-253 7.70e-12

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 64.18  E-value: 7.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNE------EKLQVVAKDIADTYKVET--DIIVADFssGReiylpire 138
Cdd:PRK07856   6 GRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRApetvdgRPAEFHAADVRDPDQVAAlvDAIVERH--GR-------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 139 alkdkdVGILVNNVG--VFYPYPQYFTQLSEDklwdIINVNIAAASLM---VHVVLPGMVERkkGAIVTISSGSCCKPTP 213
Cdd:PRK07856  76 ------LDVLVNNAGgsPYALAAEASPRFHEK----IVELNLLAPLLVaqaANAVMQQQPGG--GSIVNIGSVSGRRPSP 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226371731 214 QLAAFSASKAYLDHFSRALQYEYASKgIFVQSLIPFYVAT 253
Cdd:PRK07856 144 GTAAYGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRT 182
PRK12937 PRK12937
short chain dehydrogenase; Provisional
67-255 8.34e-12

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 63.99  E-value: 8.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIIL--ISRNEEKLQVVAKDIADTYK---VETDiiVADFSSGREIYLPIREALK 141
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVnyAGSAAAADELVAEIEAAGGRaiaVQAD--VADAAAVTRLFDAAETAFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDVgiLVNNVGVFYPYPqyfTQLSEDKLWD-IINVNIAAASLMVHVVLPGMveRKKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:PRK12937  83 RIDV--LVNNAGVMPLGT---IADFDLEDFDrTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAA 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK12937 156 SKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
70-255 1.05e-11

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 63.97  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRN-----EEKLQVVAKDIADTYKVETDiiVADFSSGREIylpIREALKD-K 143
Cdd:PRK06077   9 VVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKraeemNETLKMVKENGGEGIGVLAD--VSTREGCETL---AKATIDRyG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DVGILVNN--VGVFYPYPQyftqlSEDKLWD-IINVNIAAASLMVHVVLPGMveRKKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:PRK06077  84 VADILVNNagLGLFSPFLN-----VDDKLIDkHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGA 156
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 221 SKAYLDHFSRALQYEYASKgIFVQSLIPFYVATSM 255
Cdd:PRK06077 157 MKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKL 190
PRK12747 PRK12747
short chain dehydrogenase; Provisional
67-257 1.08e-11

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 63.94  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRG--LNIILISRNEEKLQVVakdiadtYKVETD-----IIVADFSS--GRE-IYLPI 136
Cdd:PRK12747   4 GKVALVTGASRGIGRAIAKRLANDGalVAIHYGNRKEEAEETV-------YEIQSNggsafSIGANLESlhGVEaLYSSL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 137 REALKDK----DVGILVNNVGVfypYPQYFTQLSEDKLWD-IINVNIAAASLMVHVVLPGMveRKKGAIVTISSGSCCKP 211
Cdd:PRK12747  77 DNELQNRtgstKFDILINNAGI---GPGAFIEETTEQFFDrMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRIS 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226371731 212 TPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK12747 152 LPDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNA 197
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
68-239 1.41e-11

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: 63.45  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKD-KDVG 146
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAfGRCD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:cd05357   81 VLVNNASAFYPTP--LGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALE 158
                        170
                 ....*....|...
gi 226371731 227 HFSRALQYEYASK 239
Cdd:cd05357  159 GLTRSAALELAPN 171
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
70-261 1.44e-11

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: 63.63  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIIL-ISRNEEKLQVVAKDIAD-TYKVETDIIVADfssgrEIYLPIREALKD-KDVG 146
Cdd:cd05349    3 VLVTGASRGLGAAIARSFAREGARVVVnYYRSTESAEAVAAEAGErAIAIQADVRDRD-----QVQAMIEEAKNHfGPVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ILVNNVGVFYPYPQYFTQLSEDKLW----DIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASK 222
Cdd:cd05349   78 TIVNNALIDFPFDPDQRKTFDTIDWedyqQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAK 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQ----SLIPFYVATSMTAPSNF 261
Cdd:cd05349  158 AALLGFTRNMAKELGPYGITVNmvsgGLLKVTDASAATPKEVF 200
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
72-255 1.54e-11

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: 63.24  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  72 VSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIAD----------TYKVETDIIVADF---SSGReiylpire 138
Cdd:cd08931    5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAenvvagaldvTDRAAWAAALADFaaaTGGR-------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 139 alkdkdVGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAF 218
Cdd:cd08931   77 ------LDALFNNAGVGRGGP--FEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVY 148
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 219 SASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:cd08931  149 SATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPI 185
PRK06914 PRK06914
SDR family oxidoreductase;
70-243 2.22e-11

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 63.50  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKL-----QVVAKDIADTYKVeTDIIVADFSSGREIYLPIREALKdkd 144
Cdd:PRK06914   6 AIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQenllsQATQLNLQQNIKV-QQLDVTDQNSIHNFQLVLKEIGR--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGvfYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK06914  82 IDLLVNNAG--YANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYA 159
                        170
                 ....*....|....*....
gi 226371731 225 LDHFSRALQYEYASKGIFV 243
Cdd:PRK06914 160 LEGFSESLRLELKPFGIDV 178
PRK08219 PRK08219
SDR family oxidoreductase;
70-255 2.58e-11

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 62.26  E-value: 2.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELAsRGLNIILISRNEEKLqvvaKDIADTYKVETDiIVADFSSGREIYLPIrEALKDKDVgiLV 149
Cdd:PRK08219   6 ALITGASRGIGAAIARELA-PTHTLLLGGRPAERL----DELAAELPGATP-FPVDLTDPEAIAAAV-EQLGRLDV--LV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 150 NNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERkKGAIVTISSGSCCKPTPQLAAFSASKAYLDHFS 229
Cdd:PRK08219  77 HNAGVADLGP--VAESTVDEWRATLEVNVVAPAELTRLLLPALRAA-HGHVVFINSGAGLRANPGWGSYAASKFALRALA 153
                        170       180
                 ....*....|....*....|....*.
gi 226371731 230 RALQYEYASKgIFVQSLIPFYVATSM 255
Cdd:PRK08219 154 DALREEEPGN-VRVTSVHPGRTDTDM 178
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
70-256 3.04e-11

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: 62.62  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731   70 AVVSGATDGIGKAYAEELASRGLN----IILISRNEEKLQVVAKDI-ADTYKVETDIIVADFSS--GREIYLPIREAL-- 140
Cdd:TIGR01500   3 CLVTGASRGFGRTIAQELAKCLKSpgsvLVLSARNDEALRQLKAEIgAERSGLRVVRVSLDLGAeaGLEQLLKALRELpr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  141 -KDKDVGILVNNVGVFYPYPQYFTQLSE----DKLWDIiNVN--IAAASLMVHVV--LPGmVERkkgAIVTISSGSCCKP 211
Cdd:TIGR01500  83 pKGLQRLLLINNAGTLGDVSKGFVDLSDstqvQNYWAL-NLTsmLCLTSSVLKAFkdSPG-LNR---TVVNISSLCAIQP 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 226371731  212 TPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMT 256
Cdd:TIGR01500 158 FKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQ 202
PRK06180 PRK06180
short chain dehydrogenase; Provisional
72-267 4.58e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 62.24  E-value: 4.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  72 VSGATDGIGKAYAEELASRGLNIILISRNEEKLQ-VVAKDIADTYKVETDiiVADFSSgreiylpIREALKD--KDVG-- 146
Cdd:PRK06180   9 ITGVSSGFGRALAQAALAAGHRVVGTVRSEAARAdFEALHPDRALARLLD--VTDFDA-------IDAVVADaeATFGpi 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 -ILVNNVGvfYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYL 225
Cdd:PRK06180  80 dVLVNNAG--YGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFAL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226371731 226 DHFSRALQYEYASKGIFVQSLipfyvatsmtAPSNFlhRCSW 267
Cdd:PRK06180 158 EGISESLAKEVAPFGIHVTAV----------EPGSF--RTDW 187
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
67-257 6.85e-11

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: 61.54  E-value: 6.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDiiVADFSSGREIYlpirEALKDK--D 144
Cdd:cd05371    2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGDNCRFVPVD--VTSEKDVKAAL----ALAKAKfgR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPQY-FTQLSEDKL--WD-IINVNIAAASLMVHVVLPGMVER------KKGAIVTISSGSCCKPTPQ 214
Cdd:cd05371   76 LDIVVNCAGIAVAAKTYnKKGQQPHSLelFQrVINVNLIGTFNVIRLAAGAMGKNepdqggERGVIINTASVAAFEGQIG 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226371731 215 LAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:cd05371  156 QAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLA 198
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
67-257 7.33e-11

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 61.46  E-value: 7.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRN---EEKLQVVAKDIADTYkvetdiIVADFSSGREIYLPIREALKDK 143
Cdd:PRK12481   8 GKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAeapETQAQVEALGRKFHF------ITADLIQQKDIDSIVSQAVEVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 -DVGILVNNVGVFYPypQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGA-IVTISSGSCCKPTPQLAAFSAS 221
Cdd:PRK12481  82 gHIDILINNAGIIRR--QDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNGGkIINIASMLSFQGGIRVPSYTAS 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK12481 160 KSAVMGLTRALATELSQYNINVNAIAPGYMATDNTA 195
PRK08703 PRK08703
SDR family oxidoreductase;
67-236 7.48e-11

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 61.49  E-value: 7.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIA-----DTYKVETDIIVADFSSGREIYLPIREALK 141
Cdd:PRK08703   6 DKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVeaghpEPFAIRFDLMSAEEKEFEQFAATIAEATQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDVGIlVNNVGVFYPY-PQYFTQLSEdklW-DIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFS 219
Cdd:PRK08703  86 GKLDGI-VHCAGYFYALsPLDFQTVAE---WvNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFG 161
                        170
                 ....*....|....*..
gi 226371731 220 ASKAYLDHFSRALQYEY 236
Cdd:PRK08703 162 ASKAALNYLCKVAADEW 178
PRK08340 PRK08340
SDR family oxidoreductase;
71-241 7.61e-11

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 61.74  E-value: 7.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETdiIVADFSSGREIYLPIREALKDKD-VGILV 149
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGEVYA--VKADLSDKDDLKNLVKEAWELLGgIDALV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 150 NNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERK-KGAIVTISSGSCCKPTPQLAAFSASKAYLDHF 228
Cdd:PRK08340  82 WNAGNVRCEPCMLHEAGYSDWLEAALLHLVAPGYLTTLLIQAWLEKKmKGVLVYLSSVSVKEPMPPLVLADVTRAGLVQL 161
                        170
                 ....*....|...
gi 226371731 229 SRALQYEYASKGI 241
Cdd:PRK08340 162 AKGVSRTYGGKGI 174
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
70-259 7.80e-11

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 61.52  E-value: 7.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEK-----LQVVAKDIADTYKVETDiiVADFSSGREIYLPIREALKDKD 144
Cdd:PRK12745   5 ALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEelaatQQELRALGVEVIFFPAD--VADLSAHEAMLDAAQAAWGRID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VgiLVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKK------GAIVTISSGSCCKPTPQLAAF 218
Cdd:PRK12745  83 C--LVNNAGVGVKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVSPNRGEY 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226371731 219 SASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPS 259
Cdd:PRK12745 161 CISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPV 201
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
59-257 1.02e-10

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 61.04  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  59 RADLIKqyGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSG-REIYLPIR 137
Cdd:PRK08945   6 KPDLLK--DRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLDLLTAtPQNYQQLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 138 EALKDK----DvGILVNN--VGVFYPypqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKP 211
Cdd:PRK08945  84 DTIEEQfgrlD-GVLHNAglLGELGP----MEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQG 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226371731 212 TPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK08945 159 RANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMRA 204
PRK07985 PRK07985
SDR family oxidoreductase;
67-255 1.31e-10

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 61.16  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIIL--ISRNEEKLQVVAKDIADTYKvETDIIVADFSS---GREIYLPIREALK 141
Cdd:PRK07985  49 DRKALVTGGDSGIGRAAAIAYAREGADVAIsyLPVEEEDAQDVKKIIEECGR-KAVLLPGDLSDekfARSLVHEAHKALG 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDVGILVNNVGVFYPYpqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMverKKGA-IVTISSGSCCKPTPQLAAFSA 220
Cdd:PRK07985 128 GLDIMALVAGKQVAIPD---IADLTSEQFQKTFAINVFALFWLTQEAIPLL---PKGAsIITTSSIQAYQPSPHLLDYAA 201
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK07985 202 TKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
72-260 1.75e-10

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: 60.75  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  72 VSGATDGIGKAYAEELASRGLNII-------------LISRNEEKLQVVAKDIADTYKVEtdiivadfssgrEIYLPIRE 138
Cdd:cd09805    5 ITGCDSGFGNLLAKKLDSLGFTVLagcltkngpgakeLRRVCSDRLRTLQLDVTKPEQIK------------RAAQWVKE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 139 ALKDKDVGILVNNVGVFYPyPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPgMVERKKGAIVTISSGSCCKPTPQLAAF 218
Cdd:cd09805   73 HVGEKGLWGLVNNAGILGF-GGDEELLPMDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAY 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226371731 219 SASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSN 260
Cdd:cd09805  151 CASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSE 192
PRK08265 PRK08265
short chain dehydrogenase; Provisional
67-248 1.80e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 60.41  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI-ADTYKVETDIivadfSSGREIYLPIREALKD-KD 144
Cdd:PRK08265   6 GKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLgERARFIATDI-----TDDAAIERAVATVVARfGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVfypYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVeRKKGAIVTISS-GSCCKPTPQlAAFSASKA 223
Cdd:PRK08265  81 VDILVNLACT---YLDDGLASSRADWLAALDVNLVSAAMLAQAAHPHLA-RGGGAIVNFTSiSAKFAQTGR-WLYPASKA 155
                        170       180
                 ....*....|....*....|....*
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK08265 156 AIRQLTRSMAMDLAPDGIRVNSVSP 180
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
71-259 2.82e-10

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: 59.84  E-value: 2.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTY-KVETDIIVADFSSGREIylpirEALKDKDVGI-- 147
Cdd:cd05330    7 LITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIApDAEVLLIKADVSDEAQV-----EAYVDATVEQfg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 148 ----LVNNVGVfyPYPQYFTQ-LSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASK 222
Cdd:cd05330   82 ridgFFNNAGI--EGKQNLTEdFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAK 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPS 259
Cdd:cd05330  160 HGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGS 196
PRK05650 PRK05650
SDR family oxidoreductase;
71-264 2.85e-10

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 60.05  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAK----DIADTYKVETDiiVADFSSGREIylpiREALKDK--D 144
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKllreAGGDGFYQRCD--VRDYSQLTAL----AQACEEKwgG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVfyPYPQYFTQLS-EDklWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASK 222
Cdd:PRK05650  78 IDVIVNNAGV--ASGGFFEELSlED--WDwQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAK 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIPFYVAT----SMTAPSNFLHR 264
Cdd:PRK05650 154 AGVVALSETLLVELADDEIGVHVVCPSFFQTnlldSFRGPNPAMKA 199
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
67-257 3.14e-10

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 59.50  E-value: 3.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNE-----EKLQVVAKDIADtykvetdiIVADFSSGREIYLPIREALK 141
Cdd:PRK08993  10 GKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEptetiEQVTALGRRFLS--------LTADLRKIDGIPALLERAVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 D-KDVGILVNNVGVFYPypQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGA-IVTISSGSCCKPTPQLAAFS 219
Cdd:PRK08993  82 EfGHIDILVNNAGLIRR--EDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGkIINIASMLSFQGGIRVPSYT 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226371731 220 ASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK08993 160 ASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQ 197
PRK09730 PRK09730
SDR family oxidoreductase;
70-257 3.18e-10

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 59.48  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIIL-ISRNEEKLQVVAKDI----ADTYKVETDI-----IVADFSSGREiylpirea 139
Cdd:PRK09730   4 ALVTGGSRGIGRATALLLAQEGYTVAVnYQQNLHAAQEVVNLItqagGKAFVLQADIsdenqVVAMFTAIDQ-------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 140 lKDKDVGILVNNVGVFYPYPQyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVER---KKGAIVTISSGSCCKPTP-QL 215
Cdd:PRK09730  76 -HDEPLAALVNNAGILFTQCT-VENLTAERINRVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPgEY 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226371731 216 AAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK09730 154 VDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHA 195
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
70-258 6.03e-10

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 58.30  E-value: 6.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDiadtykVETDIIVADFSSGREIYLPIREAlkdKDVGILV 149
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAE------VGALARPADVAAELEVWALAQEL---GPLDLLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 150 NNVGVFYPYPqyftqLSEDK--LWD-IINVNIAAASLMVHVVLPGMVErkKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:cd11730   72 YAAGAILGKP-----LARTKpaAWRrILDANLTGAALVLKHALALLAA--GARLVFLGAYPELVMLPGLSAYAAAKAALE 144
                        170       180       190
                 ....*....|....*....|....*....|..
gi 226371731 227 HFSRALQYEYasKGIFVQSLIPFYVATSMTAP 258
Cdd:cd11730  145 AYVEVARKEV--RGLRLTLVRPPAVDTGLWAP 174
PRK07102 PRK07102
SDR family oxidoreductase;
74-257 7.52e-10

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 58.40  E-value: 7.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  74 GATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDII---VADFSSGREIYLPIREALkdkDVGILVn 150
Cdd:PRK07102   8 GATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSTHeldILDTASHAAFLDSLPALP---DIVLIA- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 151 nVGvfYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS--GSCCKPTPQLaaFSASKAYLDHF 228
Cdd:PRK07102  84 -VG--TLGDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSvaGDRGRASNYV--YGSAKAALTAF 158
                        170       180
                 ....*....|....*....|....*....
gi 226371731 229 SRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK07102 159 LSGLRNRLFKSGVHVLTVKPGFVRTPMTA 187
PRK12746 PRK12746
SDR family oxidoreductase;
67-257 8.41e-10

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 58.51  E-value: 8.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRG-LNIILISRN----EEKLQVVAKDIADTYKVETDIIVADfsSGREIYLPIREALK 141
Cdd:PRK12746   6 GKVALVTGASRGIGRAIAMRLANDGaLVAIHYGRNkqaaDETIREIESNGGKAFLIEADLNSID--GVKKLVEQLKNELQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DK----DVGILVNNVGVfyPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMveRKKGAIVTISSGSCCKPTPQLAA 217
Cdd:PRK12746  84 IRvgtsEIDILVNNAGI--GTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSIA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226371731 218 FSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK12746 160 YGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINA 199
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
67-248 8.83e-10

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 58.23  E-value: 8.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVEtdIIVADFSSgREIYLPIREALKDKDVG 146
Cdd:PRK05786   5 GKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIH--YVVGDVSS-TESARNVIEKAAKVLNA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 I--LVNNVGvfypypQYFTQLSED--KLWDIINVNIAAASLMVHVVLPGMveRKKGAIVTISS-GSCCKPTPQLAAFSAS 221
Cdd:PRK05786  82 IdgLVVTVG------GYVEDTVEEfsGLEEMLTNHIKIPLYAVNASLRFL--KEGSSIVLVSSmSGIYKASPDQLSYAVA 153
                        170       180
                 ....*....|....*....|....*..
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK05786 154 KAGLAKAVEILASELLGRGIRVNGIAP 180
PRK08263 PRK08263
short chain dehydrogenase; Provisional
72-258 8.93e-10

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 58.51  E-value: 8.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  72 VSGATDGIGKAYAEELASRGLNIILISRNEEKLqvvaKDIADTYKvetdiivadfssgrEIYLPIREALKDKDVG----- 146
Cdd:PRK08263   8 ITGASRGFGRAWTEAALERGDRVVATARDTATL----ADLAEKYG--------------DRLLPLALDVTDRAAVfaave 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ----------ILVNNVGvfypYPQY--FTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQ 214
Cdd:PRK08263  70 tavehfgrldIVVNNAG----YGLFgmIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPM 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 226371731 215 LAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP------FYvATSMTAP 258
Cdd:PRK08263 146 SGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPggystdWA-GTSAKRA 194
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
67-273 1.00e-09

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: 58.25  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIadtyKVET---DIIV--ADFSSGREIYLPIREALK 141
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEI----RRDTlnhEVIVrhLDLASLKSIRAFAAEFLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKD-VGILVNNVGVFY-PYpqyftQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCC---------- 209
Cdd:cd09807   77 EEDrLDVLINNAGVMRcPY-----SKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKagkinfddln 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226371731 210 --KPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM--------TAPSNFLHRCSW-LVPSPK 273
Cdd:cd09807  152 seKSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELgrhtgihhLFLSTLLNPLFWpFVKTPR 226
PRK08251 PRK08251
SDR family oxidoreductase;
71-260 1.08e-09

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 58.02  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTY---KVETDII-VADFSSGREIYlpirEALKDKDVG 146
Cdd:PRK08251   6 LITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYpgiKVAVAALdVNDHDQVFEVF----AEFRDELGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 I--LVNNVGVFYPYPqyftqLSEDKLW---DIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQ-LAAFSA 220
Cdd:PRK08251  82 LdrVIVNAGIGKGAR-----LGTGKFWankATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGvKAAYAA 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSN 260
Cdd:PRK08251 157 SKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKAK 196
PRK07024 PRK07024
SDR family oxidoreductase;
71-282 1.97e-09

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 57.25  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVEtdIIVADFSSGREIylpiREALKD--KDVG-- 146
Cdd:PRK07024   6 FITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARVS--VYAADVRDADAL----AAAAADfiAAHGlp 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 -ILVNNVGVFYpypQYFTQLSEDK--LWDIINVNIAAaslMVHVVLP---GMVERKKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:PRK07024  80 dVVIANAGISV---GTLTEEREDLavFREVMDTNYFG---MVATFQPfiaPMRAARRGTLVGIASVAGVRGLPGAGAYSA 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226371731 221 SKA----YLDhfsrALQYEYASKGIFVQSLIPFYVATSMTAPSNFlhRCSWLVPsPKVYAHHAVST 282
Cdd:PRK07024 154 SKAaaikYLE----SLRVELRPAGVRVVTIAPGYIRTPMTAHNPY--PMPFLMD-ADRFAARAARA 212
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
67-254 2.02e-09

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: 57.20  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIA-DTYKVETDiiVADFSSGREIYLPIREALKDKDV 145
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGpNLFFVHGD--VADETLVKFVVYAMLEKLGRIDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 giLVNNVGVFYPYPQYFTQLSEdklWD-IINVNIAAASLMVHVVLPGMVeRKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:cd09761   79 --LVNNAARGSKGILSSLLLEE---WDrILSVNLTGPYELSRYCRDELI-KNKGRIINIASTRAFQSEPDSEAYAASKGG 152
                        170       180       190
                 ....*....|....*....|....*....|
gi 226371731 225 LDHFSRALQYEYaSKGIFVQSLIPFYVATS 254
Cdd:cd09761  153 LVALTHALAMSL-GPDIRVNCISPGWINTT 181
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
70-248 2.36e-09

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 56.97  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTY-KVETDIIVADFSSGREIYLPIREALKD-KDVGI 147
Cdd:PRK12384   5 AVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYgEGMAYGFGADATSEQSVLALSRGVDEIfGRVDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 148 LVNNVGVFYPYPQYFTQLSEdklWD-IINVNI--------AAASLMVHvvlpgmvERKKGAIVTISSGSCCKPTPQLAAF 218
Cdd:PRK12384  85 LVYNAGIAKAAFITDFQLGD---FDrSLQVNLvgyflcarEFSRLMIR-------DGIQGRIIQINSKSGKVGSKHNSGY 154
                        170       180       190
                 ....*....|....*....|....*....|
gi 226371731 219 SASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK12384 155 SAAKFGGVGLTQSLALDLAEYGITVHSLML 184
PRK07062 PRK07062
SDR family oxidoreductase;
67-247 2.44e-09

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 56.97  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVET------DII----VADFSSGREIYLpi 136
Cdd:PRK07062   8 GRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFPGARllaarcDVLdeadVAAFAAAVEARF-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 137 realkdKDVGILVNNVGVFYPYPQYFTQLS------EDKLWDIINvniaaaslMVHVVLPGMVERKKGAIVTISSGSCCK 210
Cdd:PRK07062  86 ------GGVDMLVNNAGQGRVSTFADTTDDawrdelELKYFSVIN--------PTRAFLPLLRASAAASIVCVNSLLALQ 151
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226371731 211 PTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLI 247
Cdd:PRK07062 152 PEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSIL 188
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
67-253 3.67e-09

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: 56.69  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEE-KLQVVAKDIADTYKvETDIIVADFSSGREIYLPIREALKDKD- 144
Cdd:cd09763    3 GKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEARGG-KCIPVRCDHSDDDEVEALFERVAREQQg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 -VGILVNNV-----GVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLaAF 218
Cdd:cd09763   82 rLDILVNNAyaavqLILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNV-AY 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 219 SASKAYLDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:cd09763  161 GVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRT 195
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
67-257 4.54e-09

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 57.15  E-value: 4.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIIL--ISRNEEKLQVVAKDIADTyKVETDIIVADfsSGREiylpIREALKDKD 144
Cdd:PRK08261 210 GKVALVTGAARGIGAAIAEVLARDGAHVVCldVPAAGEALAAVANRVGGT-ALALDITAPD--APAR----IAEHLAERH 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VG--ILVNNVGVfypypqyftqlSEDKL--------WD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGScckptp 213
Cdd:PRK08261 283 GGldIVVHNAGI-----------TRDKTlanmdearWDsVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSIS------ 345
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 226371731 214 QLAA------FSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK08261 346 GIAGnrgqtnYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMTA 395
PRK06182 PRK06182
short chain dehydrogenase; Validated
70-243 5.07e-09

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 56.12  E-value: 5.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQ--------VVAKDIADTYKVET--DIIVADfsSGReiylpirea 139
Cdd:PRK06182   6 ALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEdlaslgvhPLSLDVTDEASIKAavDTIIAE--EGR--------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 140 lkdkdVGILVNNVGvfypYPQY--FTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAA 217
Cdd:PRK06182  75 -----IDVLVNNAG----YGSYgaIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAW 145
                        170       180
                 ....*....|....*....|....*.
gi 226371731 218 FSASKAYLDHFSRALQYEYASKGIFV 243
Cdd:PRK06182 146 YHATKFALEGFSDALRLEVAPFGIDV 171
PRK06197 PRK06197
short chain dehydrogenase; Provisional
60-157 5.33e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 56.57  E-value: 5.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  60 ADLIKQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKvETDIIV-----ADFSSGREiyl 134
Cdd:PRK06197   9 ADIPDQSGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATP-GADVTLqeldlTSLASVRA--- 84
                         90       100
                 ....*....|....*....|....*
gi 226371731 135 pIREALKDKDVGI--LVNNVGVFYP 157
Cdd:PRK06197  85 -AADALRAAYPRIdlLINNAGVMYT 108
PRK08177 PRK08177
SDR family oxidoreductase;
68-255 7.11e-09

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 55.42  E-value: 7.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNEEK---LQVVAK------DIADTYKVETdiivadfssgreiylpIRE 138
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQdtaLQALPGvhieklDMNDPASLDQ----------------LLQ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 139 ALKDKDVGILVNNVGVFYPYPQYFTQLSEDKLWDIINVNiAAASLMVHVVLPGMVERKKGAIVTISS--GSC-CKPTPQL 215
Cdd:PRK08177  66 RLQGQRFDLLFVNAGISGPAHQSAADATAAEIGQLFLTN-AIAPIRLARRLLGQVRPGQGVLAFMSSqlGSVeLPDGGEM 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 226371731 216 AAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:PRK08177 145 PLYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
PRK08416 PRK08416
enoyl-ACP reductase;
67-243 9.58e-09

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 55.16  E-value: 9.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILI-SRNEEKLQVVAKDIADTYKVET-----DIIVADfsSGREIYLPIreal 140
Cdd:PRK08416   8 GKTLVISGGTRGIGKAIVYEFAQSGVNIAFTyNSNVEEANKIAEDLEQKYGIKAkayplNILEPE--TYKELFKKI---- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 141 kDKD---VGILVNN--------VGVFYPypqyFTQLSEDKLwdiinVNIAAASLMVHVVlpGMVERKK-------GAIVT 202
Cdd:PRK08416  82 -DEDfdrVDFFISNaiisgravVGGYTK----FMRLKPKGL-----NNIYTATVNAFVV--GAQEAAKrmekvggGSIIS 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226371731 203 ISSGSCCKPTPQLAAFSASKAYLDHFSRALQYEYASKGIFV 243
Cdd:PRK08416 150 LSSTGNLVYIENYAGHGTSKAAVETMVKYAATELGEKNIRV 190
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
67-248 1.23e-08

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 55.08  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGAT--DGIGKAYAEELASRGLNIIL------------ISRNEEKLqVVAKDIADtYKVETDIIVADFS---SG 129
Cdd:PRK12748   5 KKIALVTGASrlNGIGAAVCRRLAAKGIDIFFtywspydktmpwGMHDKEPV-LLKEEIES-YGVRCEHMEIDLSqpyAP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 130 REIYLPIREALKDKDvgILVNN--VGVFYPYPQyFTQLSEDKLWdiiNVNIAAASLMVHVVLPGMVERKKGAIVTISSGS 207
Cdd:PRK12748  83 NRVFYAVSERLGDPS--ILINNaaYSTHTRLEE-LTAEQLDKHY---AVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQ 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226371731 208 CCKPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK12748 157 SLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNP 197
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
70-260 1.28e-08

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: 54.06  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGlniilisrnEEKLQVVAKDiadtykvetDIIV---ADFSSGREIylpirealkdkdvg 146
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRG---------SPKVLVVSRR---------DVVVhnaAILDDGRLI-------------- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ilvnnvgvfypypqyftQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:cd02266   49 -----------------DLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALD 111
                        170       180       190
                 ....*....|....*....|....*....|....
gi 226371731 227 HFSRALQYEYASKGIFVQSLIPFYVATSMTAPSN 260
Cdd:cd02266  112 GLAQQWASEGWGNGLPATAVACGTWAGSGMAKGP 145
PRK07576 PRK07576
short chain dehydrogenase; Provisional
67-248 1.51e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 54.96  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADT----YKVETDiiVADFSSGREIYLPIREALKD 142
Cdd:PRK07576   9 GKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAgpegLGVSAD--VRDYAAVEAAFAQIADEFGP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDVgiLVNNVGVFYPYPQyfTQLSED---KLWDI-----INVNIAAASLMvhvvlpgmveRKKGA-IVTISSGSCCKPTP 213
Cdd:PRK07576  87 IDV--LVSGAAGNFPAPA--AGMSANgfkTVVDIdllgtFNVLKAAYPLL----------RRPGAsIIQISAPQAFVPMP 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 214 QLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK07576 153 MQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVP 187
PRK06101 PRK06101
SDR family oxidoreductase;
72-261 1.81e-08

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 54.49  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  72 VSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDiiVADFSSGREIY--LPIRealkdKDVGILv 149
Cdd:PRK06101   6 ITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHTQSANIFTLAFD--VTDHPGTKAALsqLPFI-----PELWIF- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 150 nNVGVfypypqyfTQLSEDKLWD------IINVNIAAASLMVHVVLPGMVERKKGAIV-TISSGSCckpTPQLAAFSASK 222
Cdd:PRK06101  78 -NAGD--------CEYMDDGKVDatlmarVFNVNVLGVANCIEGIQPHLSCGHRVVIVgSIASELA---LPRAEAYGASK 145
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSNF 261
Cdd:PRK06101 146 AAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTF 184
PRK06128 PRK06128
SDR family oxidoreductase;
67-248 1.98e-08

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 54.87  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEklQVVAKDIADTYKVETDIIVA---DFSSGREIYLPIREALKD- 142
Cdd:PRK06128  55 GRKALITGADSGIGRATAIAFAREGADIALNYLPEE--EQDAAEVVQLIQAEGRKAVAlpgDLKDEAFCRQLVERAVKEl 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 KDVGILVNNVGVfYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMverKKGA-IVTISSGSCCKPTPQLAAFSAS 221
Cdd:PRK06128 133 GGLDILVNIAGK-QTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL---PPGAsIINTGSIQSYQPSPTLLDYAST 208
                        170       180
                 ....*....|....*....|....*..
gi 226371731 222 KAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK06128 209 KAAIVAFTKALAKQVAEKGIRVNAVAP 235
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
68-243 2.05e-08

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 54.33  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIIL-ISRNEEKLQVVAKDIADtykvETDIIVADFSSGREIYLPIREALK--DKD 144
Cdd:PRK08642   6 QTVLVTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADELGD----RAIALQADVTDREQVQAMFATATEhfGKP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPQYFTQLSEDKLWD----IINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:PRK08642  82 ITTVVNNALADFSFDGDARKKADDITWEdfqqQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHDYTT 161
                        170       180
                 ....*....|....*....|...
gi 226371731 221 SKAYLDHFSRALQYEYASKGIFV 243
Cdd:PRK08642 162 AKAALLGLTRNLAAELGPYGITV 184
PRK06500 PRK06500
SDR family oxidoreductase;
67-253 3.66e-08

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 53.42  E-value: 3.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI-ADTYKVETDiiVADFSSGREIYLPIREALKDKDV 145
Cdd:PRK06500   6 GKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELgESALVIRAD--AGDVAAQKALAQALAEAFGRLDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPypqyFTQLSEDkLWD-IINVNIAAASLMVHVVLPgmVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK06500  84 VFINAGVAKFAP----LEDWDEA-MFDrSFNTNVKGPYFLIQALLP--LLANPASIVLNGSINAHIGMPNSSVYAASKAA 156
                        170       180
                 ....*....|....*....|....*....
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVAT 253
Cdd:PRK06500 157 LLSLAKTLSGELLPRGIRVNAVSPGPVQT 185
PRK07069 PRK07069
short chain dehydrogenase; Validated
70-258 4.26e-08

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 53.18  E-value: 4.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEK-LQVVAKDIADTYKVET------DiiVADFSSGREIYLPIREALKD 142
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAgLDAFAAEINAAHGEGVafaavqD--VTDEAQWQALLAQAADAMGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 143 kdVGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASK 222
Cdd:PRK07069  80 --LSVLVNNAGVGSFGA--IEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASK 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 226371731 223 AYLDHFSRALQYEYASKGIFVQ--SLIPFYVATSMTAP 258
Cdd:PRK07069 156 AAVASLTKSIALDCARRGLDVRcnSIHPTFIRTGIVDP 193
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
67-257 4.31e-08

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: 53.25  E-value: 4.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIAdTYKvETDIIVADFSSGREIY-LPIREALKDKDV 145
Cdd:cd08942    6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELS-AYG-ECIAIPADLSSEEGIEaLVARVAERSDRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYP-QYFTQLSEDKLWDIinvNIAAASLMVHVVLPgMVERKKGA-----IVTISS-GSCCKPTPQLAAF 218
Cdd:cd08942   84 DVLVNNAGATWGAPlEAFPESGWDKVMDI---NVKSVFFLTQALLP-LLRAAATAenparVINIGSiAGIVVSGLENYSY 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226371731 219 SASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:cd08942  160 GASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTA 198
PRK05876 PRK05876
short chain dehydrogenase; Provisional
67-259 1.30e-07

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 52.27  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKL-QVVAKDIADTYKVETdiIVADFSSGREIYLPIREALK-DKD 144
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLrQAVNHLRAEGFDVHG--VMCDVRHREEVTHLADEAFRlLGH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGA-IVTISSGSCCKPTPQLAAFSASKA 223
Cdd:PRK05876  84 VDVVFSNAGIVVGGP--IVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGhVVFTASFAGLVPNAGLGAYGVAKY 161
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPS 259
Cdd:PRK05876 162 GVVGLAETLAREVTADGIGVSVLCPMVVETNLVANS 197
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
67-255 1.44e-07

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: 51.77  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKD-KDV 145
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTKEEDIKTLISVTVERfGRI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGvFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMvERKKGAIVTISSGSCCKPTPQLAAFSASKAYL 225
Cdd:cd08933   89 DCLVNNAG-WHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHL-RKSQGNIINLSSLVGSIGQKQAAPYVATKGAI 166
                        170       180       190
                 ....*....|....*....|....*....|
gi 226371731 226 DHFSRALQYEYASKGIFVQSLIPFYVATSM 255
Cdd:cd08933  167 TAMTKALAVDESRYGVRVNCISPGNIWTPL 196
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
67-145 1.60e-07

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 52.15  E-value: 1.60e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226371731  67 GRWAVVsGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETdiivadfssgrEIYLPIREALKDKDV 145
Cdd:COG5322  152 ATVAVV-GATGSIGSVCARLLAREVKRLTLVARNLERLEELAEEILRNPGGKV-----------TITTDIDEALREADI 218
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
71-258 1.63e-07

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: 51.69  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELA---SRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIyLPIREALKDKDVGI 147
Cdd:cd09806    4 LITGCSSGIGLHLAVRLAsdpSKRFKVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSV-AAAVERVTERHVDV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 148 LVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDH 227
Cdd:cd09806   83 LVCNAGVGLLGP--LEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEG 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 226371731 228 F--SRALQyeyaskgifvqsLIPFYVATSMTAP 258
Cdd:cd09806  161 LceSLAVQ------------LLPFNVHLSLIEC 181
PRK12744 PRK12744
SDR family oxidoreductase;
67-248 4.56e-07

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 50.12  E-value: 4.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYK---VETDIIVADFSSGREIylpirEALKDK 143
Cdd:PRK12744   8 GKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEETVAAVKaagAKAVAFQADLTTAAAV-----EKLFDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 144 DVG------ILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMV-----HVvlpgmveRKKGAIVTISSGSCCKPT 212
Cdd:PRK12744  83 AKAafgrpdIAINTVGKVLKKP--IVEISEAEYDEMFAVNSKSAFFFIkeagrHL-------NDNGKIVTLVTSLLGAFT 153
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 226371731 213 PQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK12744 154 PFYSAYAGSKAPVEHFTRAASKEFGARGISVTAVGP 189
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
67-206 4.61e-07

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: 50.29  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI-ADTYKVETDIIVADFSSGREIYLPIRE-ALKDKD 144
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIeTESGNQNIFLHIVDMSDPKQVWEFVEEfKEEGKK 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226371731 145 VGILVNNVGVFYPYpqyfTQLSEDKLwdiiNVNIAAASLMVHV----VLPGMVERKKGAIVTISSG 206
Cdd:cd09808   81 LHVLINNAGCMVNK----RELTEDGL----EKNFATNTLGTYIltthLIPVLEKEEDPRVITVSSG 138
PRK05875 PRK05875
short chain dehydrogenase; Provisional
68-282 4.81e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 50.19  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  68 RWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI-ADTYKVETDIIVADFSSGREIYLPIREAL--KDKD 144
Cdd:PRK05875   8 RTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIeALKGAGAVRYEPADVTDEDQVARAVDAATawHGRL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAY 224
Cdd:PRK05875  88 HGVVHCAGGSETIGP--ITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKSA 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226371731 225 LDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPsnflhrcswLVPSPKVYAHHAVST 282
Cdd:PRK05875 166 VDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAP---------ITESPELSADYRACT 214
PRK06701 PRK06701
short chain dehydrogenase; Provisional
64-261 5.65e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 50.42  E-value: 5.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  64 KQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKlqvvakDIADTYK-VETD-----IIVADFSSgrEIYlpIR 137
Cdd:PRK06701  43 KLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHE------DANETKQrVEKEgvkclLIPGDVSD--EAF--CK 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 138 EALKD--KDVG---ILVNNVGVFYPyPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMverKKG-AIVTISSGSCCKP 211
Cdd:PRK06701 113 DAVEEtvRELGrldILVNNAAFQYP-QQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL---KQGsAIINTGSITGYEG 188
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 226371731 212 TPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTaPSNF 261
Cdd:PRK06701 189 NETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLI-PSDF 237
PRK06194 PRK06194
hypothetical protein; Provisional
63-253 1.17e-06

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 49.24  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  63 IKQY-GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI----ADTYKVETDiiVADFSSgreiylpiR 137
Cdd:PRK06194   1 MKDFaGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELraqgAEVLGVRTD--VSDAAQ--------V 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 138 EALKDK------DVGILVNNVGVFYPYPQYFTQLSEdklWD-IINVNIAAASLMVHVVLPGMVERKK------GAIVTIS 204
Cdd:PRK06194  71 EALADAalerfgAVHLLFNNAGVGAGGLVWENSLAD---WEwVLGVNLWGVIHGVRAFTPLMLAAAEkdpayeGHIVNTA 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226371731 205 SGSCCKPTPQLAAFSASKAYLDHFSRALQYEYASKG--IFVQSLIPFYVAT 253
Cdd:PRK06194 148 SMAGLLAPPAMGIYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPT 198
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
70-263 2.35e-06

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: 47.58  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVvakDIADTYKVET--------DIIVAdfSSGREIYLPIrEALK 141
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQV---DITDEASIKAlfekvghfDAIVS--TAGDAEFAPL-AELT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DKDvgilvNNVGVfypypqyftqlsEDKLWDIINVNIAAASLMvhvvlpgmveRKKGAIVTISSGSCCKPTPQLAAFSAS 221
Cdd:cd11731   75 DAD-----FQRGL------------NSKLLGQINLVRHGLPYL----------NDGGSITLTSGILAQRPIPGGAAAATV 127
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 226371731 222 KAYLDHFSRALQYEYaSKGIFVQSLIPFYVATSMTAPSNFLH 263
Cdd:cd11731  128 NGALEGFVRAAAIEL-PRGIRINAVSPGVVEESLEAYGDFFP 168
PRK08017 PRK08017
SDR family oxidoreductase;
71-247 2.92e-06

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 47.77  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEklqvvakDIADTYKVETDIIVADFSSGREIYLPIRE--ALKDKDVGIL 148
Cdd:PRK08017   6 LITGCSSGIGLEAALELKRRGYRVLAACRKPD-------DVARMNSLGFTGILLDLDDPESVERAADEviALTDNRLYGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNN--VGVFYPypqyFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:PRK08017  79 FNNagFGVYGP----LSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALE 154
                        170       180
                 ....*....|....*....|.
gi 226371731 227 HFSRALQYEYASKGIFVqSLI 247
Cdd:PRK08017 155 AWSDALRMELRHSGIKV-SLI 174
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
70-272 3.25e-06

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: 47.73  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYK-VETDiiVADFSSGREIYLPIREALKDKDvgIL 148
Cdd:cd05348    7 ALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVgVEGD--VRSLADNERAVARCVERFGKLD--CF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGVFypypQYFTQL---SEDKLW----DIINVNIAAASLMVHVVLPGMVERKKGAIVTISS--------GSCckptp 213
Cdd:cd05348   83 IGNAGIW----DYSTSLvdiPEEKLDeafdELFHINVKGYILGAKAALPALYATEGSVIFTVSNagfypgggGPL----- 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226371731 214 qlaaFSASKAYLDHFSRALQYEYASKgIFVQSLIPFYVATSMTAPSN--FLHRCSWLVPSP 272
Cdd:cd05348  154 ----YTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLRGPASlgQGETSISTPPLD 209
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
71-161 3.85e-06

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 47.92  E-value: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTykvETDIIVADFSSGREiylpIREALKDKDVgiLVN 150
Cdd:COG3268    9 VVYGATGYTGRLVAEYLARRGLRPALAGRNAAKLEAVAAELGAA---DLPLRVADLDDPAS----LAALLAGTRV--VLN 79
                         90
                 ....*....|.
gi 226371731 151 NVGvfyPYPQY 161
Cdd:COG3268   80 TVG---PFART 87
PRK09135 PRK09135
pteridine reductase; Provisional
70-237 6.14e-06

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 46.84  E-value: 6.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRN-EEKLQVVAKDIADTYKVETDIIVADFSSGREIylpirEALKDKDVG-- 146
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELNALRPGSAAALQADLLDPDAL-----PELVAACVAaf 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 147 ----ILVNNVGVFYPYPqyFTQLSEDKLWDIINVNIAAASLMVHVVLPgMVERKKGAIVTISSGSCCKPTPQLAAFSASK 222
Cdd:PRK09135  84 grldALVNNASSFYPTP--LGSITEAQWDDLFASNLKAPFFLSQAAAP-QLRKQRGAIVNITDIHAERPLKGYPVYCAAK 160
                        170
                 ....*....|....*
gi 226371731 223 AYLDHFSRALQYEYA 237
Cdd:PRK09135 161 AALEMLTRSLALELA 175
PRK05854 PRK05854
SDR family oxidoreductase;
67-157 6.16e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 47.37  E-value: 6.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVA-DFSSGREIylpirEALKD--- 142
Cdd:PRK05854  14 GKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVPDAKLSLRAlDLSSLASV-----AALGEqlr 88
                         90
                 ....*....|....*...
gi 226371731 143 ---KDVGILVNNVGVFYP 157
Cdd:PRK05854  89 aegRPIHLLINNAGVMTP 106
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
70-248 1.09e-05

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: 46.30  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKD-KDVGIL 148
Cdd:cd05322    5 AVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIfKRVDLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 149 VNNVGVFYPYPQYFTQLSEdklWD-IINVNIAAASLMVHVVLPGMVERK-KGAIVTISSGSCCKPTPQLAAFSASKAYLD 226
Cdd:cd05322   85 VYSAGIAKSAKITDFELGD---FDrSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFGGV 161
                        170       180
                 ....*....|....*....|..
gi 226371731 227 HFSRALQYEYASKGIFVQSLIP 248
Cdd:cd05322  162 GLTQSLALDLAEHGITVNSLML 183
PRK05717 PRK05717
SDR family oxidoreductase;
67-232 1.37e-05

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 45.65  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTykveTDIIVADFSSGREIYLPIREALKD-KDV 145
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGEN----AWFIAMDVADEAQVAAGVAEVLGQfGRL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GILVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPgMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYL 225
Cdd:PRK05717  86 DALVCNAAIADPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAP-YLRAHNGAIVNLASTRARQSEPDTEAYAASKGGL 164

                 ....*..
gi 226371731 226 DHFSRAL 232
Cdd:PRK05717 165 LALTHAL 171
NAD_binding_10 pfam13460
NAD(P)H-binding;
74-145 1.40e-05

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 44.90  E-value: 1.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226371731   74 GATDGIGKAYAEELASRGLNIILISRNEEKLQvvakDIADTYKVEtdIIVADFSSGREiylpIREALKDKDV 145
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALVRNPEKLA----DLEDHPGVE--VVDGDVLDPDD----LAEALAGQDA 62
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
67-154 2.10e-05

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: 44.69  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGReiylpiREALKDKDVG 146
Cdd:cd01078   28 GKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRARFGEGVGAVETSDDAAR------AAAIKGADVV 101

                 ....*...
gi 226371731 147 ILVNNVGV 154
Cdd:cd01078  102 FAAGAAGV 109
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
67-259 2.18e-05

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 45.33  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYK-VETDiiVADFSSGREIYLPIREALKDKDV 145
Cdd:PRK06200   6 GQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLvVEGD--VTSYADNQRAVDQTVDAFGKLDC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 giLVNNVGVFypypQYFTQLSE------DKLWD-IINVNIAAASLMVHVVLPGMVERKKGAIVTISS--------GSCck 210
Cdd:PRK06200  84 --FVGNAGIW----DYNTSLVDipaetlDTAFDeIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNssfypgggGPL-- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 226371731 211 ptpqlaaFSASKAYLDHFSRALQYEYASKgIFVQSLIPFYVATSMTAPS 259
Cdd:PRK06200 156 -------YTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLRGPA 196
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
53-233 2.31e-05

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: 45.82  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  53 IPRLGSRADLIKQYGRWaVVSGATDGIGKAYAEELASR-GLNIILISR---------NEEKLQVVAKDIADTYKVETDii 122
Cdd:cd08953  192 LPAGAAASAPLKPGGVY-LVTGGAGGIGRALARALARRyGARLVLLGRsplppeeewKAQTLAALEALGARVLYISAD-- 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 123 VADFSSGREIYLPIREALKDKDvgilvnnvGVFY----PYPQYFTQLSEDKLWDIINVNIAAASLMVHVVlpgmVERKKG 198
Cdd:cd08953  269 VTDAAAVRRLLEKVRERYGAID--------GVIHaagvLRDALLAQKTAEDFEAVLAPKVDGLLNLAQAL----ADEPLD 336
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 226371731 199 AIVTISSGSCCKPTPQLAAFSASKAYLDHFSRALQ 233
Cdd:cd08953  337 FFVLFSSVSAFFGGAGQADYAAANAFLDAFAAYLR 371
PRK06947 PRK06947
SDR family oxidoreductase;
71-257 7.70e-05

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 43.64  E-value: 7.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNI-ILISRNEEKLQVVAKDIADTyKVETDIIVADFSSGREIyLPIREALKDKDVGI-- 147
Cdd:PRK06947   6 LITGASRGIGRATAVLAAARGWSVgINYARDAAAAEETADAVRAA-GGRACVVAGDVANEADV-IAMFDAVQSAFGRLda 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 148 LVNNVGVFYPyPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERK---KGAIVTISSGSCCKPTP-QLAAFSASKA 223
Cdd:PRK06947  84 LVNNAGIVAP-SMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrGGAIVNVSSIASRLGSPnEYVDYAGSKG 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 226371731 224 YLDHFSRALQYEYASKGIFVQSLIPFYVATSMTA 257
Cdd:PRK06947 163 AVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHA 196
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
67-268 8.08e-05

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 43.74  E-value: 8.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTY-KVETDIIVADFSSGREIYlPIREALKDKDV 145
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWhKARVEAMTLDLASLRSVQ-RFAEAFKAKNS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 146 GI--LVNNVGVF-YPYpqyftQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGS---------CCK--- 210
Cdd:cd09809   80 PLhvLVCNAAVFaLPW-----TLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSEShrftdlpdsCGNldf 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226371731 211 ----PTPQ----LAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPfyvaTSMTAPSnfLHRCSWL 268
Cdd:cd09809  155 sllsPPKKkywsMLAYNRAKLCNILFSNELHRRLSPRGITSNSLHP----GNMMYSS--IHRNWWV 214
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
70-259 8.81e-05

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 43.53  E-value: 8.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEEL-----ASRGLNIILISRNEEKLQVVAKDIADTY---KVETDIIVADFSSGREIYLPIREaLK 141
Cdd:cd08941    4 VLVTGANSGLGLAICERLlaeddENPELTLILACRNLQRAEAACRALLASHpdaRVVFDYVLVDLSNMVSVFAAAKE-LK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 142 DK---------DVGILVN--------NVGVFY------PYPQYFTQL----------SEDKLWDIINVNIAAASLMVHVV 188
Cdd:cd08941   83 KRyprldylylNAGIMPNpgidwigaIKEVLTnplfavTNPTYKIQAegllsqgdkaTEDGLGEVFQTNVFGHYYLIREL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 189 LPGMVERKKGA-IVTISSGSC-----------CKPTPqlAAFSASKAYLDHFSRALQYEYASKGIFvQSLI-PFYVATSM 255
Cdd:cd08941  163 EPLLCRSDGGSqIIWTSSLNAspkyfslediqHLKGP--APYSSSKYLVDLLSLALNRKFNKLGVY-SYVVhPGICTTNL 239

                 ....
gi 226371731 256 TAPS 259
Cdd:cd08941  240 TYGI 243
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
71-121 9.47e-05

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 42.92  E-value: 9.47e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEK-------LQVVAKDIADTYKVETDI 121
Cdd:COG2910    3 AVIGATGRVGSLIVREALARGHEVTALVRNPEKlpdehpgLTVVVGDVLDPAAVAEAL 60
PRK07791 PRK07791
short chain dehydrogenase; Provisional
67-256 9.82e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 43.51  E-value: 9.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIIL---------ISRNEEKLQVVAKDI--ADTYKVETDIIVADFSSGREIylp 135
Cdd:PRK07791   6 GRVVIVTGAGGGIGRAHALAFAAEGARVVVndigvgldgSASGGSAAQAVVDEIvaAGGEAVANGDDIADWDGAANL--- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 136 IREALKD-KDVGILVNNVGVFypYPQYFTQLSEDKlWD-IINVNIAA-ASLMVHVVLPGMVERKKG-----AIVTISSGS 207
Cdd:PRK07791  83 VDAAVETfGGLDVLVNNAGIL--RDRMIANMSEEE-WDaVIAVHLKGhFATLRHAAAYWRAESKAGravdaRIINTSSGA 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 226371731 208 CCKPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPfyVA-TSMT 256
Cdd:PRK07791 160 GLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP--AArTRMT 207
PRK06196 PRK06196
oxidoreductase; Provisional
67-154 1.19e-04

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 43.13  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIivADFSSGREIYLPIREALKDKDvg 146
Cdd:PRK06196  26 GKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDGVEVVMLDL--ADLESVRAFAERFLDSGRRID-- 101

                 ....*...
gi 226371731 147 ILVNNVGV 154
Cdd:PRK06196 102 ILINNAGV 109
PRK07677 PRK07677
short chain dehydrogenase; Provisional
71-112 1.52e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 42.74  E-value: 1.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIA 112
Cdd:PRK07677   5 IITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIE 46
PLN02253 PLN02253
xanthoxin dehydrogenase
67-258 1.83e-04

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 42.50  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYK---------VETDIIVA-DFSsgreiylpi 136
Cdd:PLN02253  18 GKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNvcffhcdvtVEDDVSRAvDFT--------- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 137 reALKDKDVGILVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASL-MVHVVLPgMVERKKGAIVTISSGSCCKPTPQL 215
Cdd:PLN02253  89 --VDKFGTLDIMVNNAGLTGPPCPDIRNVELSEFEKVFDVNVKGVFLgMKHAARI-MIPLKKGSIVSLCSVASAIGGLGP 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226371731 216 AAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAP 258
Cdd:PLN02253 166 HAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALA 208
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
67-232 2.70e-04

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: 41.54  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILISRN------------------EEKLQVVAKDIADTYKVETDIIVADFSS 128
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAeneeadasiivldsdsftEQAKQVVASVARLSGKVDALICVAGGWA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 129 GreiylpirEALKDKDvgiLVNNVgvfypypqyftqlseDKLWDIiNVNIAAASlmVHVVLPGMveRKKGAIVTISSGSC 208
Cdd:cd05334   81 G--------GSAKSKS---FVKNW---------------DLMWKQ-NLWTSFIA--SHLATKHL--LSGGLLVLTGAKAA 129
                        170       180
                 ....*....|....*....|....
gi 226371731 209 CKPTPQLAAFSASKAYLDHFSRAL 232
Cdd:cd05334  130 LEPTPGMIGYGAAKAAVHQLTQSL 153
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
70-248 2.89e-04

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: 41.84  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731   70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIV-ADFSSGREiyLPIR-EALKDK---- 143
Cdd:TIGR02685   4 AVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARRPNSAVTCqADLSNSAT--LFSRcEAIIDAcfra 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  144 ----DVgiLVNNVGVFYPYPqYFTQLSEDKLWDIINVNIAAASLM-VHVVLP-----GMVERKKG----------AIVTI 203
Cdd:TIGR02685  82 fgrcDV--LVNNASAFYPTP-LLRGDAGEGVGDKKSLEVQVAELFgSNAIAPyflikAFAQRQAGtraeqrstnlSIVNL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 226371731  204 SSGSCCKPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:TIGR02685 159 CDAMTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAP 203
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
71-205 3.05e-04

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: 41.71  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVvakDIADTYKVETdiIVADfssgreiyLPireALKDKDVGILVN 150
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHTVIGIDLREADVIA---DLSTPEGRAA--AIAD--------VL---ARCSGVLDGLVN 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226371731 151 NVGVFYPYPqyftqlsedkLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS 205
Cdd:cd05328   67 CAGVGGTTV----------AGLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSS 111
PRK12742 PRK12742
SDR family oxidoreductase;
67-260 4.32e-04

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 41.28  E-value: 4.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILIsrneeklQVVAKDIADTYKVET--DIIVADFSSGREIYLPIREAlkdKD 144
Cdd:PRK12742   6 GKKVLVLGGSRGIGAAIVRRFVTDGANVRFT-------YAGSKDAAERLAQETgaTAVQTDSADRDAVIDVVRKS---GA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 145 VGILVNNVGVFY---PYpqyftQLSEDKLWDIINVNIAAAslmVHVVLPGMVERKKGA-IVTISSGSCCK-PTPQLAAFS 219
Cdd:PRK12742  76 LDILVVNAGIAVfgdAL-----ELDADDIDRLFKINIHAP---YHASVEAARQMPEGGrIIIIGSVNGDRmPVAGMAAYA 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226371731 220 ASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTaPSN 260
Cdd:PRK12742 148 ASKSALQGMARGLARDFGPRGITINVVQPGPIDTDAN-PAN 187
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
70-249 5.84e-04

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: 40.74  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731   70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEklQVVAKDIADTYKVETDIivADFSSgreiylpIREALKDKDVGILV 149
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTS--ASNTARLADLRFVEGDL--TDRDA-------LEKLLADVRPDAVI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  150 NNVGVFYPypqyftQLSEDKLWDIINVNIAAASLMVHVVlpgmveRKKGAIVTISSGSCC----------------KPTP 213
Cdd:pfam01370  70 HLAAVGGV------GASIEDPEDFIEANVLGTLNLLEAA------RKAGVKRFLFASSSEvygdgaeipqeettltGPLA 137
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 226371731  214 QLAAFSASKAYLDHFSRALQYEYaskGIFVQSLIPF 249
Cdd:pfam01370 138 PNSPYAAAKLAGEWLVLAYAAAY---GLRAVILRLF 170
PRK06953 PRK06953
SDR family oxidoreductase;
70-255 6.73e-04

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 40.44  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVetDIIVADFSSGREIYLPiREALkdkDVGILV 149
Cdd:PRK06953   4 VLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGAEALAL--DVADPASVAGLAWKLD-GEAL---DAAVYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 150 NnvGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPgMVERKKGAIVTISS-----GSCCKPTPQLaaFSASKAY 224
Cdd:PRK06953  78 A--GVYGPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLP-LVEAAGGVLAVLSSrmgsiGDATGTTGWL--YRASKAA 152
                        170       180       190
                 ....*....|....*....|....*....|.
gi 226371731 225 LDHFSRALQYEYasKGIFVQSLIPFYVATSM 255
Cdd:PRK06953 153 LNDALRAASLQA--RHATCIALHPGWVRTDM 181
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
67-154 8.00e-04

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 40.54  E-value: 8.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIIL--ISRNEEKLQVVAKDIADTYKVET---DIivADFSSGREIylpIREALK 141
Cdd:PRK07792  12 GKVAVVTGAAAGLGRAEALGLARLGATVVVndVASALDASDVLDEIRAAGAKAVAvagDI--SQRATADEL---VATAVG 86
                         90
                 ....*....|...
gi 226371731 142 DKDVGILVNNVGV 154
Cdd:PRK07792  87 LGGLDIVVNNAGI 99
PRK07041 PRK07041
SDR family oxidoreductase;
71-119 8.85e-04

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 40.02  E-value: 8.85e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVET 119
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPVRT 49
PRK08278 PRK08278
SDR family oxidoreductase;
67-262 1.85e-03

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 39.50  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  67 GRWAVVSGATDGIGKAYAEELASRGLNIILIsrneeklqvvAKDIADTYKVETDIivadFSSGREI------YLPIREAL 140
Cdd:PRK08278   6 GKTLFITGASRGIGLAIALRAARDGANIVIA----------AKTAEPHPKLPGTI----HTAAEEIeaaggqALPLVGDV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 141 KDKD---------------VGILVNNVGVFYPYPqyfTQLSEDKLWDIIN-VNIAAASLMVHVVLPGMVERKKGAIVTIS 204
Cdd:PRK08278  72 RDEDqvaaavakaverfggIDICVNNASAINLTG---TEDTPMKRFDLMQqINVRGTFLVSQACLPHLKKSENPHILTLS 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226371731 205 SGSCCKPT--PQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIP-FYVATSmtAPSNFL 262
Cdd:PRK08278 149 PPLNLDPKwfAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPrTTIATA--AVRNLL 207
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
70-157 1.89e-03

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 39.42  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGL-NIILISRNEEKLQVVAKDI---ADTYKV-ETDIivADFSSGREIYLPIREALKDKD 144
Cdd:cd09810    4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVgmpKDSYSVlHCDL--ASLDSVRQFVDNFRRTGRPLD 81
                         90
                 ....*....|...
gi 226371731 145 VgiLVNNVGVFYP 157
Cdd:cd09810   82 A--LVCNAAVYLP 92
PRK09186 PRK09186
flagellin modification protein A; Provisional
71-248 3.05e-03

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 38.82  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYK------VETDIIVAD-----FSSGREIYLPIREA 139
Cdd:PRK09186   8 LITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKskklslVELDITDQEsleefLSKSAEKYGKIDGA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 140 lkdkdvgilVNNVgvfYPYP-QY---FTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISS---------- 205
Cdd:PRK09186  88 ---------VNCA---YPRNkDYgkkFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSiygvvapkfe 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226371731 206 ----GSCCKPTpqlaAFSASKAYLDHFSRALQYEYASKGIFVQSLIP 248
Cdd:PRK09186 156 iyegTSMTSPV----EYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSP 198
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
74-111 3.33e-03

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 38.81  E-value: 3.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 226371731  74 GATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDI 111
Cdd:PRK08655   7 GGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKEL 44
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
72-119 4.35e-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: 38.41  E-value: 4.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 226371731  72 VSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKD-----IADTYKVET 119
Cdd:cd05269    3 VTGATGKLGTAVVELLLAKVASVVALVRNPEKAKAFAADgvevrQGDYDDPET 55
PRK06482 PRK06482
SDR family oxidoreductase;
72-241 4.37e-03

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 38.17  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  72 VSGATDGIGKAYAEELASRGLNII-----------LISRNEEKLQVVAKDIADTYKVETDIIVADFSSGReiylpireal 140
Cdd:PRK06482   7 ITGASSGFGRGMTERLLARGDRVAatvrrpdalddLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGR---------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731 141 kdkdVGILVNNVGvfYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSA 220
Cdd:PRK06482  77 ----IDVVVSNAG--YGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHA 150
                        170       180
                 ....*....|....*....|.
gi 226371731 221 SKAYLDHFSRALQYEYASKGI 241
Cdd:PRK06482 151 TKWGIEGFVEAVAQEVAPFGI 171
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
72-126 4.79e-03

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: 37.98  E-value: 4.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226371731  72 VSGATDGIGKAYAEELASRGLN-IILISRNEEKLQVVAKDIADTYKVETDI-IVADF 126
Cdd:cd05237    7 VTGGAGSIGSELVRQILKFGPKkLIVFDRDENKLHELVRELRSRFPHDKLRfIIGDV 63
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
70-193 5.01e-03

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. 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: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 38.08  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  70 AVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDiadtykvetDIIVADFSSGREiylpIREALkdKDVGILV 149
Cdd:cd05229    2 AHVLGASGPIGREVARELRRRGWDVRLVSRSGSKLAWLPGV---------EIVAADAMDASS----VIAAA--RGADVIY 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 226371731 150 NNVGVFYP-YPQYFTQLSEdklwdiiNVNIAAASLMVHVVLPGMV 193
Cdd:cd05229   67 HCANPAYTrWEELFPPLME-------NVVAAAEANGAKLVLPGNV 104
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
71-153 6.44e-03

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 37.52  E-value: 6.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIAdtykvetDIIVADFSSGREiylpIREALKDKDVGILVN 150
Cdd:COG0702    3 LVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAAGV-------EVVQGDLDDPES----LAAALAGVDAVFLLV 71

                 ...
gi 226371731 151 NVG 153
Cdd:COG0702   72 PSG 74
PRK06940 PRK06940
short chain dehydrogenase; Provisional
71-207 6.44e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 37.69  E-value: 6.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371731  71 VVSGAtDGIGKAYAEELASrGLNIILISRNEEKLQVVAKDIADT-YKVETdiIVADFSSGREIYLPIREALKDKDVGILV 149
Cdd:PRK06940   6 VVIGA-GGIGQAIARRVGA-GKKVLLADYNEENLEAAAKTLREAgFDVST--QEVDVSSRESVKALAATAQTLGPVTGLV 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226371731 150 NNVGVfYPypqyfTQLSEDklwDIINVNIAAASLMVHVVlpGMVERKKGAIVTISSGS 207
Cdd:PRK06940  82 HTAGV-SP-----SQASPE---AILKVDLYGTALVLEEF--GKVIAPGGAGVVIASQS 128
 
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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