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Conserved domains on  [gi|809662|emb|CAA29533|]
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unnamed protein product, partial [Bacillus subtilis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
fabG super family cl35604
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-177 1.74e-126

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


The actual alignment was detected with superfamily member PRK07666:

Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 355.15  E-value: 1.74e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK07666  63 ADVSDYEEVTAAIEQLKNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINIS 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQPEDLAEYMVAQLK 160
Cdd:PRK07666 143 STAGQKGAAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDGNPDKVMQPEDLAEFIVAQLK 222
                        170
                 ....*....|....*..
gi 809662    161 LDPRIFIKTAGLWSTNP 177
Cdd:PRK07666 223 LNKRTFIKSAGLWSTNP 239
 
Name Accession Description Interval E-value
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-177 1.74e-126

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 355.15  E-value: 1.74e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK07666  63 ADVSDYEEVTAAIEQLKNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINIS 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQPEDLAEYMVAQLK 160
Cdd:PRK07666 143 STAGQKGAAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDGNPDKVMQPEDLAEFIVAQLK 222
                        170
                 ....*....|....*..
gi 809662    161 LDPRIFIKTAGLWSTNP 177
Cdd:PRK07666 223 LNKRTFIKSAGLWSTNP 239
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
1-167 5.76e-62

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: 191.55  E-value: 5.76e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:COG4221  58 LDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNIS 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSieLNLTDGNPEKV---------MQPEDL 151
Cdd:COG4221 138 SIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFL--DSVFDGDAEAAaavyeglepLTPEDV 215
                       170
                ....*....|....*.
gi 809662   152 AEYMVAQLKLDPRIFI 167
Cdd:COG4221 216 AEAVLFALTQPAHVNV 231
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
1-140 7.40e-60

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 184.74  E-value: 7.40e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662       1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:pfam00106  56 GDVTDRAQVKALVEQAVERLGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNIS 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDG 140
Cdd:pfam00106 136 SVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
1-159 2.04e-55

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: 174.78  E-value: 2.04e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05233  53 ADVSDEEDVEALVEEALEEFGRLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNIS 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPE--------KVMQPEDLA 152
Cdd:cd05233 133 SVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKElaaaiplgRLGTPEEVA 212

                ....*..
gi 809662   153 EyMVAQL 159
Cdd:cd05233 213 E-AVVFL 218
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
1-96 3.15e-05

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 42.47  E-value: 3.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662        1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERkagdIINIS 80
Cdd:smart00822  60 CDVADRDALAAVLAAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDF----FVLFS 135
                           90
                   ....*....|....*.
gi 809662       81 STAGQRGAAVTSAYSA 96
Cdd:smart00822 136 SIAGVLGSPGQANYAA 151
 
Name Accession Description Interval E-value
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-177 1.74e-126

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 355.15  E-value: 1.74e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK07666  63 ADVSDYEEVTAAIEQLKNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINIS 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQPEDLAEYMVAQLK 160
Cdd:PRK07666 143 STAGQKGAAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDGNPDKVMQPEDLAEFIVAQLK 222
                        170
                 ....*....|....*..
gi 809662    161 LDPRIFIKTAGLWSTNP 177
Cdd:PRK07666 223 LNKRTFIKSAGLWSTNP 239
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
1-167 5.76e-62

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: 191.55  E-value: 5.76e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:COG4221  58 LDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNIS 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSieLNLTDGNPEKV---------MQPEDL 151
Cdd:COG4221 138 SIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFL--DSVFDGDAEAAaavyeglepLTPEDV 215
                       170
                ....*....|....*.
gi 809662   152 AEYMVAQLKLDPRIFI 167
Cdd:COG4221 216 AEAVLFALTQPAHVNV 231
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-164 1.43e-60

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 188.54  E-value: 1.43e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:COG0300  61 LDVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVS 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPekVMQPEDLAEYMVAQLK 160
Cdd:COG0300 141 SVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRP--LLSPEEVARAILRALE 218

                ....
gi 809662   161 LDPR 164
Cdd:COG0300 219 RGRA 222
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
1-140 7.40e-60

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 184.74  E-value: 7.40e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662       1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:pfam00106  56 GDVTDRAQVKALVEQAVERLGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNIS 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDG 140
Cdd:pfam00106 136 SVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
1-159 2.04e-55

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: 174.78  E-value: 2.04e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05233  53 ADVSDEEDVEALVEEALEEFGRLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNIS 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPE--------KVMQPEDLA 152
Cdd:cd05233 133 SVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKElaaaiplgRLGTPEEVA 212

                ....*..
gi 809662   153 EyMVAQL 159
Cdd:cd05233 213 E-AVVFL 218
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
1-159 3.90e-54

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: 171.89  E-value: 3.90e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:COG1028  62 ADVTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNIS 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVM---------QPEDL 151
Cdd:COG1028 142 SIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAariplgrlgTPEEV 221

                ....*...
gi 809662   152 AEyMVAQL 159
Cdd:COG1028 222 AA-AVLFL 228
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
1-159 1.79e-47

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 154.97  E-value: 1.79e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK05557  62 GDVSDAESVERAVDEAKAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINIS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielnlTDGNPEKVM-------------Q 147
Cdd:PRK05557 142 SVVGLMGNPGQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDM------TDALPEDVKeailaqiplgrlgQ 215
                        170
                 ....*....|..
gi 809662    148 PEDLAEyMVAQL 159
Cdd:PRK05557 216 PEEIAS-AVAFL 226
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-131 3.71e-47

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 153.84  E-value: 3.71e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK05565  62 ADVSSEEDVENLVEQIVEKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNIS 141
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK05565 142 SIWGLIGASCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEM 192
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-153 6.09e-47

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 153.39  E-value: 6.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK05653  61 FDVSDEAAVRALIEAAVEAFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNIS 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielnlTDGNPEKVM-------------Q 147
Cdd:PRK05653 141 SVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDM------TEGLPEEVKaeilkeiplgrlgQ 214

                 ....*.
gi 809662    148 PEDLAE 153
Cdd:PRK05653 215 PEEVAN 220
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
2-132 1.57e-46

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: 152.38  E-value: 1.57e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:cd05374  54 DVTDEESIKAAVKEVIERFGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSS 133
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 809662    82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:cd05374 134 VAGLVPTPFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFA 184
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
1-160 2.29e-46

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: 151.64  E-value: 2.29e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd08939  61 ADLSDYEEVEQAFAQAVEKGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVS 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTD-------GNPEKVMQPEDLAE 153
Cdd:cd08939 141 SQAALVGIYGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENKTKpeetkaiEGSSGPITPEEAAR 220

                ....*..
gi 809662   154 YMVAQLK 160
Cdd:cd08939 221 IIVKGLD 227
PRK07326 PRK07326
SDR family oxidoreductase;
1-165 2.94e-45

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 149.01  E-value: 2.94e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKaGDIINIS 80
Cdd:PRK07326  61 ADVRDEADVQRAVDAIVAAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINIS 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSielnltdGNP--EKV---MQPEDLAEYM 155
Cdd:PRK07326 140 SLAGTNFFAGGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFN-------GHTpsEKDawkIQPEDIAQLV 212
                        170
                 ....*....|
gi 809662    156 VAQLKLDPRI 165
Cdd:PRK07326 213 LDLLKMPPRT 222
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-159 4.09e-45

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 148.86  E-value: 4.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK12825  63 ADVTDKAALEAAVAAAVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNIS 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM---SIELNLTDGNPE----KVMQPEDLAE 153
Cdd:PRK12825 143 SVAGLPGWPGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMkeaTIEEAREAKDAEtplgRSGTPEDIAR 222

                 ....*.
gi 809662    154 yMVAQL 159
Cdd:PRK12825 223 -AVAFL 227
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
1-147 3.24e-44

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: 146.15  E-value: 3.24e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05333  56 ADVSDREAVEALVEKVEAEFGPVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINIS 135
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielnlTDGNPEKVMQ 147
Cdd:cd05333 136 SVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDM------TDALPEKVKE 196
PRK12826 PRK12826
SDR family oxidoreductase;
1-156 6.56e-40

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 135.43  E-value: 6.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK12826  62 VDVRDRAALKAAVAAGVEDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGA-AVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELnLTDGNPE---------KVMQPED 150
Cdd:PRK12826 142 SVAGPRVGyPGLAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNL-GDAQWAEaiaaaiplgRLGEPED 220

                 ....*.
gi 809662    151 LAEYMV 156
Cdd:PRK12826 221 IAAAVL 226
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
2-167 2.68e-39

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: 133.52  E-value: 2.68e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:cd05339  56 DVSKREEVYEAAKKIKKEVGDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIAS 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVR---KHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQPEDLAEYMVAQ 158
Cdd:cd05339 136 VAGLISPAGLADYCASKAAAVGFHESLRLELKaygKPGIKTTLVCPYFINTGMFQGVKTPRPLLAPILEPEYVAEKIVRA 215

                ....*....
gi 809662   159 LKLDPRIFI 167
Cdd:cd05339 216 ILTNQQMLY 224
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
1-132 9.22e-39

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: 132.48  E-value: 9.22e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05347  61 CDVSDEEAIKAAVEAIEEDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINIC 140
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:cd05347 141 SLLSELGGPPVPAYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMT 192
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
1-132 1.46e-38

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: 131.40  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662       1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS--KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMieRKAGDIIN 78
Cdd:pfam13561  50 CDVTDEEQVEALVAAAVEKFGRLDILVNNAGFApkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVN 127
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 809662      79 ISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:pfam13561 128 LSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLAA 181
FabG-like PRK07231
SDR family oxidoreductase;
1-153 4.60e-38

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 130.72  E-value: 4.60e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS-KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINI 79
Cdd:PRK07231  60 ADVSDEADVEAAVAAALERFGSVDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNV 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIEL--NLTDGNPEKVMQ---------P 148
Cdd:PRK07231 140 ASTAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFmgEPTPENRAKFLAtiplgrlgtP 219

                 ....*
gi 809662    149 EDLAE 153
Cdd:PRK07231 220 EDIAN 224
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
1-164 1.16e-37

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: 129.16  E-value: 1.16e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEW-ENIIQVNLMGVYHVTRAVLPeMIERKAGDIINI 79
Cdd:cd08929  53 GDVRDEADVRRAVDAMEEAFGGLDALVNNAGVGVMKPVEELTPEEWrLVLDTNLTGAFYCIHKAAPA-LLRRGGGTIVNV 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSielnltdGNPEK---VMQPEDLAEYMV 156
Cdd:cd08929 132 GSLAGKNAFKGGAAYNASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFA-------GSPEGqawKLAPEDVAQAVL 204

                ....*...
gi 809662   157 AQLKLDPR 164
Cdd:cd08929 205 FALEMPAR 212
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
1-131 1.91e-37

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: 129.20  E-value: 1.91e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd08934  59 LDVTDEQQVDAAVERTVEALGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNIS 138
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:cd08934 139 SVAGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTEL 189
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
1-156 1.13e-36

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: 127.32  E-value: 1.13e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05332  60 LDMSDLEDAEQVVEEALKLFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVS 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKV--------MQPEDLA 152
Cdd:cd05332 140 SIAGKIGVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNALSGDGSMSAKmddttangMSPEECA 219

                ....
gi 809662   153 EYMV 156
Cdd:cd05332 220 LEIL 223
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
2-166 1.93e-36

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 125.94  E-value: 1.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:cd08932  53 DARDPEDARALVDALRDRFGRIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNS 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNP-EKVMQPEDLAEYMVAQLK 160
Cdd:cd08932 133 LSGKRVLAGNAGYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAFPpEEMIQPKDIANLVRMVIE 212

                ....*.
gi 809662   161 LDPRIF 166
Cdd:cd08932 213 LPENIT 218
PRK07825 PRK07825
short chain dehydrogenase; Provisional
2-173 3.28e-36

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 126.59  E-value: 3.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK07825  58 DVTDPASFAAFLDAVEADLGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVAS 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEkvMQPEDLAEYMVAQL-K 160
Cdd:PRK07825 138 LAGKIPVPGMATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGGAKGFKN--VEPEDVAAAIVGTVaK 215
                        170
                 ....*....|....
gi 809662    161 LDPRIFI-KTAGLW 173
Cdd:PRK07825 216 PRPEVRVpRALGPL 229
PRK07454 PRK07454
SDR family oxidoreductase;
2-127 4.10e-36

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 125.46  E-value: 4.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK07454  63 DLSNPEAIAPGIAELLEQFGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSS 142
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTV 127
Cdd:PRK07454 143 IAARNAFPQWGAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAV 188
PRK12829 PRK12829
short chain dehydrogenase; Provisional
1-131 4.14e-36

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 125.94  E-value: 4.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISK-FGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGD-IIN 78
Cdd:PRK12829  65 ADVADPAQVERVFDTAVERFGGLDVLVNNAGIAGpTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGvIIA 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 809662     79 ISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK12829 145 LSSVAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPR 197
PRK06181 PRK06181
SDR family oxidoreductase;
1-156 9.15e-36

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 125.09  E-value: 9.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEW-ENIIQVNLMGVYHVTRAVLPEMIERKaGDIINI 79
Cdd:PRK06181  57 TDVSDAEACERLIEAAVARFGGIDILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAALPHLKASR-GQIVVV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNP--------EKVMQPEDL 151
Cdd:PRK06181 136 SSLAGLTGVPTRSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATDIRKRALDGDGKPlgkspmqeSKIMSAEEC 215

                 ....*
gi 809662    152 AEYMV 156
Cdd:PRK06181 216 AEAIL 220
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
1-147 1.12e-35

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 124.91  E-value: 1.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK08226  61 ADVRDPASVAAAIKRAKEKEGRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMS 140
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGA-AVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM--SIELNLTDGNPEKVMQ 147
Cdd:PRK08226 141 SVTGDMVAdPGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMaeSIARQSNPEDPESVLT 210
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-131 8.39e-35

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 122.18  E-value: 8.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK12824  59 LDVTDTEECAEALAEIEEEEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINIS 138
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK12824 139 SVNGLKGQFGQTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPM 189
PRK12827 PRK12827
short chain dehydrogenase; Provisional
1-162 1.02e-34

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 122.14  E-value: 1.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIE-RKAGDIINI 79
Cdd:PRK12827  66 FDVRDFAATRAALDAGVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNI 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDG--NP---EKVMQPEDLAEy 154
Cdd:PRK12827 146 ASVAGVRGNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPTEHllNPvpvQRLGEPDEVAA- 224

                 ....*...
gi 809662    155 MVAQLKLD 162
Cdd:PRK12827 225 LVAFLVSD 232
PRK06179 PRK06179
short chain dehydrogenase; Provisional
2-125 1.18e-34

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 122.32  E-value: 1.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK06179  53 DVTDDASVQAAVDEVIARAGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISS 132
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPS 125
Cdd:PRK06179 133 VLGFLPAPYMALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPA 176
PRK06841 PRK06841
short chain dehydrogenase; Provisional
2-127 2.68e-34

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 121.30  E-value: 2.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK06841  69 DVSDSQSVEAAVAAVISAFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLAS 148
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTV 127
Cdd:PRK06841 149 QAGVVALERHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVV 194
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
1-132 8.14e-34

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: 119.74  E-value: 8.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05352  65 CDVSSQESVEKTFKQIQKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITA 144
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 809662    81 STAGQRG--AAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:cd05352 145 SMSGTIVnrPQPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLT 198
PRK06180 PRK06180
short chain dehydrogenase; Provisional
2-125 9.02e-34

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 120.41  E-value: 9.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK06180  58 DVTDFDAIDAVVADAEATFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITS 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPS 125
Cdd:PRK06180 138 MGGLITMPGIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPG 181
PRK07109 PRK07109
short chain dehydrogenase; Provisional
1-120 1.42e-33

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 121.18  E-value: 1.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK07109  64 ADVADAEAVQAAADRAEEELGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVG 143
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVS 120
Cdd:PRK07109 144 SALAYRSIPLQSAYCAAKHAIRGFTDSLRCELLHDGSPVS 183
PRK07063 PRK07063
SDR family oxidoreductase;
1-124 2.04e-33

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 119.00  E-value: 2.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK07063  65 ADVTDAASVAAAVAAAEEAFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIA 144
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK07063 145 STHAFKIIPGCFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAP 188
PRK12939 PRK12939
short chain dehydrogenase; Provisional
1-152 2.11e-33

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 118.54  E-value: 2.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK12939  63 ADLADPASVQRFFDAAAAALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM-----SIELN--LTDGNP-EKVMQPEDLA 152
Cdd:PRK12939 143 SDTALWGAPKLGAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEAtayvpADERHayYLKGRAlERLQVPDDVA 222
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
2-152 2.32e-33

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 119.01  E-value: 2.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK07097  67 DVTDEDGVQAMVSQIEKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICS 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIEL----NLTDGNP-----------EKVM 146
Cdd:PRK07097 147 MMSELGRETVSAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQTAPLrelqADGSRHPfdqfiiaktpaARWG 226

                 ....*.
gi 809662    147 QPEDLA 152
Cdd:PRK07097 227 DPEDLA 232
PRK05855 PRK05855
SDR family oxidoreductase;
2-127 3.49e-33

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 123.55  E-value: 3.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER-KAGDIINIS 80
Cdd:PRK05855 372 DVSDADAMEAFAEWVRAEHGVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVA 451
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTV 127
Cdd:PRK05855 452 SAAAYAPSRSLPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFV 498
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
1-147 5.59e-33

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: 117.57  E-value: 5.59e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQvkeqLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05368  53 LDVTDKEQVAALAKE----EGRIDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMS 128
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 809662    81 STAGQ-RGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQ 147
Cdd:cd05368 129 SVASSiKGVPNRFVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALK 196
PRK12828 PRK12828
short chain dehydrogenase; Provisional
1-152 6.58e-33

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 117.20  E-value: 6.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK12828  61 IDLVDPQAARRAVDEVNRQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIG 140
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsIELNLTDGNPEKVMQPEDLA 152
Cdd:PRK12828 141 AGAALKAGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPP-NRADMPDADFSRWVTPEQIA 211
PRK07832 PRK07832
SDR family oxidoreductase;
2-127 2.00e-32

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 116.68  E-value: 2.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIE-RKAGDIINIS 80
Cdd:PRK07832  58 DISDYDAVAAFAADIHAAHGSMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAaGRGGHLVNVS 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTV 127
Cdd:PRK07832 138 SAAGLVALPWHAAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAV 184
PRK05650 PRK05650
SDR family oxidoreductase;
2-125 2.69e-32

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 116.29  E-value: 2.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVnQAVAQV-KEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK05650  57 DVRDYSQL-TALAQAcEEKWGGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIA 135
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPS 125
Cdd:PRK05650 136 SMAGLMQGPAMSSYNVAKAGVVALSETLLVELADDEIGVHVVCPS 180
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
2-124 2.99e-32

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 116.26  E-value: 2.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISK---------FGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERK 72
Cdd:PRK06171  57 DVSSAEEVNHTVAEIIEKFGRIDGLVNNAGINIprllvdekdPAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQH 136
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 809662     73 AGDIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK06171 137 DGVIVNMSSEAGLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAP 188
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
1-127 3.03e-32

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 115.75  E-value: 3.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK12429  60 MDVTDEEAINAGIDYAVETFGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMA 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTV 127
Cdd:PRK12429 140 SVHGLVGSAGKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYV 186
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
1-153 3.50e-32

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: 115.62  E-value: 3.50e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd08940  60 ADLSKPAAIEDMVAYAQRQFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIA 139
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM---SIE-LNLTDGNPEKVMQPEDLAE 153
Cdd:cd08940 140 SVHGLVASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLvekQISaLAQKNGVPQEQAARELLLE 216
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
1-156 4.91e-32

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: 114.79  E-value: 4.91e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05360  56 ADVADAAQVERAADTAVERFGRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVG 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRK--HNIRVSALTPSTV--------ASDMSIELNLtdgnPEKVMQPED 150
Cdd:cd05360 136 SLLGYRSAPLQAAYSASKHAVRGFTESLRAELAHdgAPISVTLVQPTAMntpffghaRSYMGKKPKP----PPPIYQPER 211

                ....*.
gi 809662   151 LAEYMV 156
Cdd:cd05360 212 VAEAIV 217
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-131 5.79e-32

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 115.12  E-value: 5.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER-KAGDIINI 79
Cdd:PRK07067  59 LDVTRQDSIDRIVAAAVERFGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINM 138
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK07067 139 ASQAGRRGEALVSHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPM 190
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
2-169 7.60e-32

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: 114.68  E-value: 7.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISK-FGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05346  58 DVSDRESIEAALENLPEEFRDIDILVNNAGLALgLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLG 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSieLNLTDGNPEKV---------MQPEDL 151
Cdd:cd05346 138 SIAGRYPYAGGNVYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFS--LVRFHGDKEKAdkvyegvepLTPEDI 215
                       170
                ....*....|....*...
gi 809662   152 AEYMVAQLKLDPRIFIKT 169
Cdd:cd05346 216 AETILWVASRPAHVNIND 233
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
1-159 1.03e-31

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 114.33  E-value: 1.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK12935  63 ADVSKVEDANRLVEEAVNHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISIS 142
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELnltdgnpekvmqPEDLAEYMVAQL 159
Cdd:PRK12935 143 SIIGQAGGFGQTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEV------------PEEVRQKIVAKI 209
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
1-132 2.64e-31

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: 113.08  E-value: 2.64e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLgDIDILINNAGISKF--GGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIIN 78
Cdd:cd05356  58 ADFSAGDDIYERIEKELEGL-DIGILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVN 136
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 809662    79 ISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:cd05356 137 ISSFAGLIPTPLLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKMS 190
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
2-172 4.84e-31

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: 112.48  E-value: 4.84e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:cd05341  59 DVTDEDGWTAVVDTAREAFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSS 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKH--NIRVSALTPSTVASDMSIELNLTDGNPE--------KVMQPEDL 151
Cdd:cd05341 139 IEGLVGDPALAAYNASKGAVRGLTKSAALECATQgyGIRVNSVHPGYIYTPMTDELLIAQGEMGnypntpmgRAGEPDEI 218
                       170       180
                ....*....|....*....|.
gi 809662   152 AeYMVAQLKLDPRIFIKTAGL 172
Cdd:cd05341 219 A-YAVVYLASDESSFVTGSEL 238
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
2-154 5.82e-31

(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: 112.42  E-value: 5.82e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAqvkEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:cd05353  71 SVEDGEKIVKTAI---DAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSS 147
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 809662    82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPsTVASDMSielnltdgnpEKVMQPEDLAEY 154
Cdd:cd05353 148 AAGLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAP-AAGSRMT----------ETVMPEDLFDAL 209
PRK08267 PRK08267
SDR family oxidoreductase;
2-153 1.01e-30

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 111.95  E-value: 1.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQ-VKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK08267  56 DVTDRAAWDAALADfAAATGGRLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTS 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielnlTDGNPEKVM-----------QPE 149
Cdd:PRK08267 136 SASAIYGQPGLAVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAM------LDGTSNEVDagstkrlgvrlTPE 209

                 ....
gi 809662    150 DLAE 153
Cdd:PRK08267 210 DVAE 213
PRK08263 PRK08263
short chain dehydrogenase; Provisional
2-132 1.12e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 112.44  E-value: 1.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK08263  57 DVTDRAAVFAAVETAVEHFGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISS 136
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:PRK08263 137 IGGISAFPMSGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWA 187
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
2-160 1.13e-30

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: 111.27  E-value: 1.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:cd05350  55 DVTDEERNQLVIAELEAELGGLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISS 134
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 809662    82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSielNLTDGNPeKVMQPEDLAEYMVAQLK 160
Cdd:cd05350 135 VAALRGLPGAAAYSASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPLT---ANMFTMP-FLMSVEQAAKRIYKAIK 209
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
1-127 1.14e-30

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 111.91  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMI-ERKAGDIINI 79
Cdd:PRK13394  63 MDVTNEDAVNAGIDKVAERFGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYM 142
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTV 127
Cdd:PRK13394 143 GSVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFV 190
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
2-133 1.17e-30

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: 111.78  E-value: 1.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGIS--KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINI 79
Cdd:cd05326  59 DVTVEADVRAAVDTAVARFGRLDIMFNNAGVLgaPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSV 138
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 809662    80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSI 133
Cdd:cd05326 139 ASVAGVVGGLGPHAYTASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLT 192
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
2-132 1.25e-30

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 111.77  E-value: 1.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK08085  66 NVTHKQEVEAAIEHIEKDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICS 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:PRK08085 146 MQSELGRDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMT 196
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
1-146 1.40e-30

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 111.16  E-value: 1.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK12936  59 ANLSDRDEVKALGQKAEADLEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINIT 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNltDGNPEKVM 146
Cdd:PRK12936 139 SVVGVTGNPGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLN--DKQKEAIM 202
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
1-154 1.85e-30

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: 111.32  E-value: 1.85e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIE-RKAGDIINI 79
Cdd:cd05358  60 ADVSKEEDVVALFQSAIKEFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKsKIKGKIINM 139
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 809662    80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNltdGNPEKVMQPEDLAEY 154
Cdd:cd05358 140 SSVHEKIPWPGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAW---DDPEQRADLLSLIPM 211
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
1-132 2.06e-30

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: 111.09  E-value: 2.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPE--MIERKAGDIIN 78
Cdd:cd08945  59 CDVRSVPEIEALVAAAVARYGPIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIIN 138
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 809662    79 ISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:cd08945 139 IASTGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMA 192
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
1-153 3.23e-30

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 110.36  E-value: 3.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK08220  55 LDVSDAAAVAQVCQRLLAETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAgqrgAAV----TSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM--------SIELNLTDGNPE----- 143
Cdd:PRK08220 135 SNA----AHVprigMAAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMqrtlwvdeDGEQQVIAGFPEqfklg 210
                        170
                 ....*....|....
gi 809662    144 ----KVMQPEDLAE 153
Cdd:PRK08220 211 iplgKIARPQEIAN 224
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
1-130 3.63e-30

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: 110.17  E-value: 3.63e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS-KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINI 79
Cdd:cd05345  58 ADVTKRADVEAMVEAALSKFGRLDILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINI 137
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 809662    80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPstVASD 130
Cdd:cd05345 138 ASTAGLRPRPGLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCP--VAGE 186
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
1-131 4.81e-30

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: 110.16  E-value: 4.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERK-AGDIINI 79
Cdd:cd05366  59 ADVTDKDDVEALIDQAVEKFGSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINA 138
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 809662    80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:cd05366 139 SSIAGVQGFPNLGAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM 190
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
2-131 8.73e-30

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 109.33  E-value: 8.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK12938  61 NVGDWDSTKAAFDKVKAEVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISS 140
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK12938 141 VNGQKGQFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDM 190
PRK06138 PRK06138
SDR family oxidoreductase;
1-156 1.63e-29

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 108.70  E-value: 1.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK06138  60 GDVGSAEAVEALVDFVAARWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTA 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVM-------------Q 147
Cdd:PRK06138 140 SQLALAGGRGRAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPEALRealrarhpmnrfgT 219

                 ....*....
gi 809662    148 PEDLAEYMV 156
Cdd:PRK06138 220 AEEVAQAAL 228
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
2-153 2.38e-29

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: 107.54  E-value: 2.38e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGD-IDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd08931  55 DVTDRAAWAAALADFAAATGGrLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTA 134
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsIELNLTDGNPEK----VMQPEDLAE 153
Cdd:cd08931 135 SSSAIYGQPDLAVYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPI-LTKGETGAAPKKglgrVLPVSDVAK 210
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
2-167 3.20e-29

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: 107.98  E-value: 3.20e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA--GDIINI 79
Cdd:cd05343  64 DLSNEEQILSMFSAIRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIINI 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    80 SSTAGQR--GAAVTSAYSASKFAVLGLTESLMQEVR--KHNIRVSALTPSTVASDMSIELNltDGNPEK---------VM 146
Cdd:cd05343 144 NSMSGHRvpPVSVFHFYAATKHAVTALTEGLRQELReaKTHIRATSISPGLVETEFAFKLH--DNDPEKaaatyesipCL 221
                       170       180
                ....*....|....*....|.
gi 809662   147 QPEDLAEYMVAQLKLDPRIFI 167
Cdd:cd05343 222 KPEDVANAVLYVLSTPPHVQI 242
PRK06398 PRK06398
aldose dehydrogenase; Validated
2-167 3.50e-29

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 108.00  E-value: 3.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK06398  52 DVSNKEQVIKGIDYVISKYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIAS 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     82 ---TAGQRGAAvtsAYSASKFAVLGLTESLMQEVRKhNIRVSALTPST-------------VASD-MSIELNLTDGNPEK 144
Cdd:PRK06398 132 vqsFAVTRNAA---AYVTSKHAVLGLTRSIAVDYAP-TIRCVAVCPGSirtpllewaaeleVGKDpEHVERKIREWGEMH 207
                        170       180
                 ....*....|....*....|....*..
gi 809662    145 VMQ----PEDLAeYMVAQLKLDPRIFI 167
Cdd:PRK06398 208 PMKrvgkPEEVA-YVVAFLASDLASFI 233
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
1-152 5.25e-29

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: 107.17  E-value: 5.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05331  47 LDVADAAAVREVCSRLLAEHGPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVA 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM--------SIELNLTDGNPE--------- 143
Cdd:cd05331 127 SNAAHVPRISMAAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMqrtlwhdeDGAAQVIAGVPEqfrlgiplg 206

                ....*....
gi 809662   144 KVMQPEDLA 152
Cdd:cd05331 207 KIAQPADIA 215
PRK06914 PRK06914
SDR family oxidoreductase;
2-124 5.60e-29

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 107.80  E-value: 5.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVnQAVAQVKEQLGDIDILINNAGISkFGGFL-DLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK06914  62 DVTDQNSI-HNFQLVLKEIGRIDLLVNNAGYA-NGGFVeEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINIS 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK06914 140 SISGRVGFPGLSPYVSSKYALEGFSESLRLELKPFGIDVALIEP 183
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
1-130 6.51e-29

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: 106.97  E-value: 6.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05344  57 ADLTDPEDIDRLVEKAGDAFGRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNIS 136
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASD 130
Cdd:cd05344 137 SLTVKEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
1-131 1.16e-28

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: 106.42  E-value: 1.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGI-SKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINI 79
Cdd:cd08944  56 VDVTDEQQVAALFERAVEEFGGLDLLVNNAGAmHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNL 135
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 809662    80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:cd08944 136 SSIAGQSGDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPL 187
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-129 1.26e-28

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 106.36  E-value: 1.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK06935  70 VDLTKPESAEKVVKEALEEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIA 149
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVAS 129
Cdd:PRK06935 150 SMLSFQGGKFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
PRK07774 PRK07774
SDR family oxidoreductase;
1-164 1.72e-28

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 105.98  E-value: 1.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGI---SKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDII 77
Cdd:PRK07774  62 VDVSDPDSAKAMADATVSAFGGIDYLVNNAAIyggMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIV 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     78 NISSTAgqrgAAVTSA-YSASKFAVLGLTESLMQEVRKHNIRVSALTPStvasdmsielnLTDGNPEKVMQPEDLAEYMV 156
Cdd:PRK07774 142 NQSSTA----AWLYSNfYGLAKVGLNGLTQQLARELGGMNIRVNAIAPG-----------PIDTEATRTVTPKEFVADMV 206

                 ....*...
gi 809662    157 AQLKLDPR 164
Cdd:PRK07774 207 KGIPLSRM 214
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
1-166 2.52e-28

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 105.55  E-value: 2.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05338  71 VDVRDEDQVRALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNIS 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPST-VASDMSIELnLTDGNPEKVMQPEDLAEYMVAQL 159
Cdd:cd05338 151 PPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTaIETPAATEL-SGGSDPARARSPEILSDAVLAIL 229

                ....*..
gi 809662   160 KLDPRIF 166
Cdd:cd05338 230 SRPAAER 236
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
1-157 3.04e-28

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: 105.08  E-value: 3.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS--KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGD--- 75
Cdd:cd05323  56 CDVTSWEQLAAAFKKAIEKFGRVDILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKGGKggv 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    76 IINISSTAGQRGAAVTSAYSASKFAVLGLTESL-MQEVRKHNIRVSALTPSTVASDM--SIELNLTD-GNPEKVMQPEDL 151
Cdd:cd05323 136 IVNIGSVAGLYPAPQFPVYSASKHGVVGFTRSLaDLLEYKTGVRVNAICPGFTNTPLlpDLVAKEAEmLPSAPTQSPEVV 215

                ....*.
gi 809662   152 AEYMVA 157
Cdd:cd05323 216 AKAIVY 221
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-133 1.09e-27

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 104.10  E-value: 1.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK06463  58 CDVGNRDQVKKSKEVVEKEFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIA 137
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 809662     81 STAGQRGAAV-TSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSI 133
Cdd:PRK06463 138 SNAGIGTAAEgTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTL 191
PRK06172 PRK06172
SDR family oxidoreductase;
2-131 1.63e-27

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 103.68  E-value: 1.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFL-DLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK06172  64 DVTRDAEVKALVEQTIAAYGRLDYAFNNAGIEIEQGRLaEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTA 143
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK06172 144 SVAGLGAAPKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM 194
PRK06484 PRK06484
short chain dehydrogenase; Validated
2-135 3.13e-27

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 106.47  E-value: 3.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGIS--KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGD-IIN 78
Cdd:PRK06484  59 DVSDEAQIREGFEQLHREFGRIDVLVNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVN 138
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 809662     79 ISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIEL 135
Cdd:PRK06484 139 VASGAGLVALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAEL 195
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
1-153 4.66e-27

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: 102.28  E-value: 4.66e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGiskfGGFL----DLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA-GD 75
Cdd:cd05369  60 CDVRDPEAVEAAVDETLKEFGKIDILINNAA----GNFLapaeSLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHgGS 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    76 IINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP---------STVASDMSIELNLTDGNPEKVM 146
Cdd:cd05369 136 ILNISATYAYTGSPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPgpipttegmERLAPSGKSEKKMIERVPLGRL 215

                ....*...
gi 809662   147 -QPEDLAE 153
Cdd:cd05369 216 gTPEEIAN 223
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
2-134 5.07e-27

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: 102.74  E-value: 5.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDI--LINNAGISKFGGFLDLSA-DEWENIIQVNLMGVYHVTRAVLPeMIERKAGDIIN 78
Cdd:cd09805  56 DVTKPEQIKRAAQWVKEHVGEKGLwgLVNNAGILGFGGDEELLPmDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVN 134
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 809662    79 ISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPS---TVASDMSIE 134
Cdd:cd09805 135 VSSMGGRVPFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGnfkTGITGNSEL 193
PRK06182 PRK06182
short chain dehydrogenase; Validated
2-130 5.47e-27

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 102.73  E-value: 5.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK06182  54 DVTDEASIKAAVDTIIAEEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISS 133
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASD 130
Cdd:PRK06182 134 MGGKIYTPLGAWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTE 182
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
1-170 5.62e-27

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: 102.21  E-value: 5.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS-KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINI 79
Cdd:cd05330  61 ADVSDEAQVEAYVDATVEQFGRIDGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNT 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsIELNLTDGNPE---------------- 143
Cdd:cd05330 141 ASVGGIRGVGNQSGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPM-VEGSLKQLGPEnpeeageefvsvnpmk 219
                       170       180
                ....*....|....*....|....*..
gi 809662   144 KVMQPEDLAeYMVAQLKLDPRIFIKTA 170
Cdd:cd05330 220 RFGEPEEVA-AVVAFLLSDDAGYVNAA 245
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
2-174 7.83e-27

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: 101.16  E-value: 7.83e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGIS-KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05324  58 DVTDDASIEAAADFVEEKYGGLDILVNNAGIAfKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVS 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRgaavTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielnltdGNPEKVMQPEDLAEYMVaQLK 160
Cdd:cd05324 138 SGLGSL----TSAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDM--------GGGKAPKTPEEGAETPV-YLA 204
                       170
                ....*....|....
gi 809662   161 LDPRIFIKTAGLWS 174
Cdd:cd05324 205 LLPPDGEPTGKFFS 218
PRK05872 PRK05872
short chain dehydrogenase; Provisional
1-131 9.03e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 102.36  E-value: 9.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKaGDIINIS 80
Cdd:PRK05872  64 ADVTDLAAMQAAAEEAVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVS 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK05872 143 SLAAFAAAPGMAAYCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDL 193
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
1-147 9.20e-27

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: 101.72  E-value: 9.20e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKaGDIINIS 80
Cdd:cd05364  62 ADLTEEEGQDRIISTTLAKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVS 140
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQ 147
Cdd:cd05364 141 SVAGGRSFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMPEEQYIKFLS 207
PRK07775 PRK07775
SDR family oxidoreductase;
2-158 9.48e-27

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 102.14  E-value: 9.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK07775  67 DVTDPDSVKSFVAQAEEALGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGS 146
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELnltdgnPEKVMQP--EDLAEYMVAQ 158
Cdd:PRK07775 147 DVALRQRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWSL------PAEVIGPmlEDWAKWGQAR 219
PRK06057 PRK06057
short chain dehydrogenase; Provisional
1-144 1.29e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 101.35  E-value: 1.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS--KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIIN 78
Cdd:PRK06057  58 TDVTDEDAVNALFDTAAETYGSVDIAFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIIN 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 809662     79 ISSTAGQRGAAvTS--AYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDgnPEK 144
Cdd:PRK06057 138 TASFVAVMGSA-TSqiSYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKD--PER 202
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
1-132 1.39e-26

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 101.18  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPE-MIERKAGDIINI 79
Cdd:PRK08213  68 ADVADEADIERLAEETLERFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINV 147
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 809662     80 SSTAGQRGAAV----TSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:PRK08213 148 ASVAGLGGNPPevmdTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMT 204
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
1-124 1.66e-26

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 100.88  E-value: 1.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERK-AGDIINI 79
Cdd:PRK12384  60 ADATSEQSVLALSRGVDEIFGRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQI 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK12384 140 NSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLML 184
PRK08219 PRK08219
SDR family oxidoreductase;
1-153 1.96e-26

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 100.01  E-value: 1.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADqvnqAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMieRKA-GDIINI 79
Cdd:PRK08219  54 VDLTDPE----AIAAAVEQLGRLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPAL--RAAhGHVVFI 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHnIRVSALTPSTVASDMSIELNLTDG---NPEKVMQPEDLAE 153
Cdd:PRK08219 128 NSGAGLRANPGWGSYAASKFALRALADALREEEPGN-VRVTSVHPGRTDTDMQRGLVAQEGgeyDPERYLRPETVAK 203
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
1-132 4.88e-26

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: 99.35  E-value: 4.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05359  55 ADVSQPQDVEEMFAAVKERFGRLDVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAIS 134
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:cd05359 135 SLGSIRALPNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDAL 186
PRK08264 PRK08264
SDR family oxidoreductase;
2-160 5.22e-26

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 99.19  E-value: 5.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVaqvkEQLGDIDILINNAGISKFGGFLDLSA-DEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK08264  57 DVTDPASVAAAA----EAASDVTILVNNAGIFRTGSLLLEGDeDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielnlTDGNPEKVMQPEDLAEYMVAQLK 160
Cdd:PRK08264 133 SVLSWVNFPNLGTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDM------AAGLDAPKASPADVARQILDALE 206
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
9-131 5.29e-26

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 99.27  E-value: 5.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      9 VNQAVAQVKEQLGDIDILINNAGI-SKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISSTAGQRG 87
Cdd:PRK06550  54 LSDDLEPLFDWVPSVDILCNTAGIlDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVA 133
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 809662     88 AAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK06550 134 GGGGAAYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPM 177
PRK06523 PRK06523
short chain dehydrogenase; Provisional
1-135 8.08e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 99.21  E-value: 8.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISK--FGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIIN 78
Cdd:PRK06523  56 ADLTTAEGCAAVARAVLERLGGVDILVHVLGGSSapAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIH 135
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 809662     79 ISSTAGQRGA-AVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIEL 135
Cdd:PRK06523 136 VTSIQRRLPLpESTTAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVAL 193
PRK12937 PRK12937
short chain dehydrogenase; Provisional
1-159 1.06e-25

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 98.66  E-value: 1.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMieRKAGDIINIS 80
Cdd:PRK12937  62 ADVADAAAVTRLFDAAETAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLS 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIE-------LNLTDGNP-EKVMQPEDLA 152
Cdd:PRK12937 140 TSVIALPLPGYGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATELFFNgksaeqiDQLAGLAPlERLGTPEEIA 219

                 ....*..
gi 809662    153 EyMVAQL 159
Cdd:PRK12937 220 A-AVAFL 225
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-152 1.47e-25

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 98.49  E-value: 1.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLD---------LSADEWENIIQVNLMGVYHVTRAVLPEMIE- 70
Cdd:PRK08217  61 ANVTDEEDVEATFAQIAEDFGQLNGLINNAGILRDGLLVKakdgkvtskMSLEQFQSVIDVNLTGVFLCGREAAAKMIEs 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     71 RKAGDIINISSTA-----GQrgaavtSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELN------LTD 139
Cdd:PRK08217 141 GSKGVIINISSIAragnmGQ------TNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKpealerLEK 214
                        170
                 ....*....|....
gi 809662    140 GNPEKVM-QPEDLA 152
Cdd:PRK08217 215 MIPVGRLgEPEEIA 228
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
1-153 4.93e-25

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: 96.96  E-value: 4.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMieRKAGDIINIS 80
Cdd:cd05362  60 ADVSDPSQVARLFDAAEKAFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINIS 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIElNLTDGNPEK---------VMQPEDL 151
Cdd:cd05362 138 SSLTAAYTPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYA-GKTEEAVEGyakmsplgrLGEPEDI 216

                ..
gi 809662   152 AE 153
Cdd:cd05362 217 AP 218
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
1-164 9.32e-25

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 96.00  E-value: 9.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDlSADEWENI---IQVNLMGVYHVTRAVLPEMIERKAGDII 77
Cdd:COG3967  57 LDVADPASIAALAEQVTAEFPDLNVLINNAGIMRAEDLLD-EAEDLADAereITTNLLGPIRLTAAFLPHLKAQPEAAIV 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    78 NISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELnltdGNPEKVMQPEDLAEYMVA 157
Cdd:COG3967 136 NVSSGLAFVPLAVTPTYSATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQ----GGDPRAMPLDEFADEVMA 211

                ....*..
gi 809662   158 QLKLDPR 164
Cdd:COG3967 212 GLETGKY 218
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
2-127 1.03e-24

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: 96.38  E-value: 1.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEqlGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:cd09806  61 DVCDSKSVAAAVERVTE--RHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSS 138
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 809662    82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTV 127
Cdd:cd09806 139 VGGLQGLPFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIECGPV 184
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
1-153 1.46e-24

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 95.53  E-value: 1.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05373  56 TDARDEDEVIALFDLIEEEIGPLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTG 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSAltpstVASDMSIELNLTDGNPEK---------VMQPEDL 151
Cdd:cd05373 136 ATASLRGRAGFAAFAGAKFALRALAQSMARELGPKGIHVAH-----VIIDGGIDTDFIRERFPKrderkeedgILDPDAI 210

                ..
gi 809662   152 AE 153
Cdd:cd05373 211 AE 212
PRK06701 PRK06701
short chain dehydrogenase; Provisional
1-152 1.57e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 96.64  E-value: 1.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKF-GGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMierKAGD-IIN 78
Cdd:PRK06701 103 GDVSDEAFCKDAVEETVRELGRLDILVNNAAFQYPqQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL---KQGSaIIN 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     79 ISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASdmsiELNLTDGNPEKV--------M---- 146
Cdd:PRK06701 180 TGSITGYEGNETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWT----PLIPSDFDEEKVsqfgsntpMqrpg 255

                 ....*.
gi 809662    147 QPEDLA 152
Cdd:PRK06701 256 QPEELA 261
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
1-131 2.59e-24

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 95.38  E-value: 2.59e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER-KAGDIINI 79
Cdd:cd05363  56 LDVTDQASIDRCVAALVDRWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINM 135
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 809662    80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:cd05363 136 ASQAGRRGEALVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEH 187
PRK08589 PRK08589
SDR family oxidoreductase;
2-127 5.35e-24

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 94.84  E-value: 5.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFL-DLSADEWENIIQVNLMGVYHVTRAVLPEMIErKAGDIINIS 80
Cdd:PRK08589  62 DISDEQQVKDFASEIKEQFGRVDVLFNNAGVDNAAGRIhEYPVDVFDKIMAVDMRGTFLMTKMLLPLMME-QGGSIINTS 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTV 127
Cdd:PRK08589 141 SFSGQAADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTI 187
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-152 5.95e-24

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 94.20  E-value: 5.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER-KAGDIINI 79
Cdd:PRK12481  62 ADLIQQKDIDSIVSQAVEVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQgNGGKIINI 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQ---------PED 150
Cdd:PRK12481 142 ASMLSFQGGIRVPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRADTARNEAILEripasrwgtPDD 221

                 ..
gi 809662    151 LA 152
Cdd:PRK12481 222 LA 223
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
2-159 6.49e-24

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 94.05  E-value: 6.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISkfggfLDL------SADEWENIIQVNLMGVYHVTRAVLPEMIERKAGD 75
Cdd:PRK10538  54 DVRNRAAIEEMLASLPAEWRNIDVLVNNAGLA-----LGLepahkaSVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     76 IINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVAsdmSIELNLT--DGNPEKV-------- 145
Cdd:PRK10538 129 IINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVG---GTEFSNVrfKGDDGKAektyqntv 205
                        170
                 ....*....|....*..
gi 809662    146 -MQPEDLAE--YMVAQL 159
Cdd:PRK10538 206 aLTPEDVSEavWWVATL 222
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
2-131 7.79e-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: 93.69  E-value: 7.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVkeqlGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA-GDIINIS 80
Cdd:cd05351  60 DLSDWDATEEALGSV----GPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVS 135
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:cd05351 136 SQASQRALTNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDM 186
PRK07074 PRK07074
SDR family oxidoreductase;
2-127 1.36e-23

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 93.30  E-value: 1.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK07074  57 DLTDAASLAAALANAAAERGPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGS 136
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 809662     82 TagqRGAAVTS--AYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTV 127
Cdd:PRK07074 137 V---NGMAALGhpAYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPGTV 181
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
1-145 1.37e-23

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: 93.12  E-value: 1.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS------KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA- 73
Cdd:cd05371  54 VDVTSEKDVKAALALAKAKFGRLDIVVNCAGIAvaaktyNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPd 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    74 -----GDIINISSTA---GQRGAAvtsAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielnlTDGNPEKV 145
Cdd:cd05371 134 qggerGVIINTASVAafeGQIGQA---AYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPL------LAGLPEKV 204
PRK07831 PRK07831
SDR family oxidoreductase;
2-125 1.49e-23

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 93.17  E-value: 1.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERK-AGDIINIS 80
Cdd:PRK07831  77 DVTSEAQVDALIDAAVERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGhGGVIVNNA 156
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPS 125
Cdd:PRK07831 157 SVLGWRAQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPS 201
PRK07024 PRK07024
SDR family oxidoreductase;
1-157 1.73e-23

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 93.07  E-value: 1.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKfgGFL-----DLSAdeWENIIQVNLMGVYHVTRAVLPEMIERKAGD 75
Cdd:PRK07024  57 ADVRDADALAAAAADFIAAHGLPDVVIANAGISV--GTLteereDLAV--FREVMDTNYFGMVATFQPFIAPMRAARRGT 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     76 IINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielnlTDGNPEK---VMQPEDLA 152
Cdd:PRK07024 133 LVGIASVAGVRGLPGAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPM------TAHNPYPmpfLMDADRFA 206

                 ....*
gi 809662    153 EYMVA 157
Cdd:PRK07024 207 ARAAR 211
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
1-131 1.74e-23

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 92.87  E-value: 1.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERK-AGDIINI 79
Cdd:PRK08643  58 ADVSDRDQVFAAVRQVVDTFGDLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhGGKIINA 137
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK08643 138 TSQAGVVGNPELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPM 189
PRK06139 PRK06139
SDR family oxidoreductase;
2-164 2.87e-23

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 93.63  E-value: 2.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK06139  64 DVTDADQVKALATQAASFGGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMIS 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKH-NIRVSALTPSTVASDmsielNLTDGN---------PEKVMQPEDL 151
Cdd:PRK06139 144 LGGFAAQPYAAAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDTP-----GFRHGAnytgrrltpPPPVYDPRRV 218
                        170
                 ....*....|...
gi 809662    152 AEYMVAqLKLDPR 164
Cdd:PRK06139 219 AKAVVR-LADRPR 230
PRK06198 PRK06198
short chain dehydrogenase; Provisional
1-130 2.93e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 92.38  E-value: 2.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA-GDIINI 79
Cdd:PRK06198  63 ADLSDVEDCRRVVAAADEAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNI 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASD 130
Cdd:PRK06198 143 GSMSAHGGQPFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE 193
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
1-156 3.02e-23

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: 92.14  E-value: 3.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS-KFGGFLDLSAD--EWENII-QVN--LMGVYHVTRAVLPEMIERKAG 74
Cdd:cd05349  54 ADVRDRDQVQAMIEEAKNHFGPVDTIVNNALIDfPFDPDQRKTFDtiDWEDYQqQLEgaVKGALNLLQAVLPDFKERGSG 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    75 DIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP--------STVASDMSIELnLTDGNP-EKV 145
Cdd:cd05349 134 RVINIGTNLFQNPVVPYHDYTTAKAALLGFTRNMAKELGPYGITVNMVSGgllkvtdaSAATPKEVFDA-IAQTTPlGKV 212
                       170
                ....*....|.
gi 809662   146 MQPEDLAEYMV 156
Cdd:cd05349 213 TTPQDIADAVL 223
PRK06949 PRK06949
SDR family oxidoreductase;
2-151 3.10e-23

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 92.52  E-value: 3.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER--------KA 73
Cdd:PRK06949  66 DVTDYQSIKAAVAHAETEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARakgagntkPG 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     74 GDIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGN-------PEK-V 145
Cdd:PRK06949 146 GRIINIASVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQGqklvsmlPRKrV 225

                 ....*.
gi 809662    146 MQPEDL 151
Cdd:PRK06949 226 GKPEDL 231
PRK12743 PRK12743
SDR family oxidoreductase;
2-149 4.43e-23

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 92.02  E-value: 4.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER-KAGDIINIS 80
Cdd:PRK12743  60 DLSDLPEGAQALDKLIQRLGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINIT 139
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSielNLTDGNPEKVMQPE 149
Cdd:PRK12743 140 SVHEHTPLPGASAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMN---GMDDSDVKPDSRPG 205
PRK07856 PRK07856
SDR family oxidoreductase;
1-132 4.65e-23

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 91.92  E-value: 4.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA-GDIINI 79
Cdd:PRK07856  54 ADVRDPDQVAALVDAIVERHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNI 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQE--VRkhnIRVSALTPSTVASDMS 132
Cdd:PRK07856 134 GSVSGRRPSPGTAAYGAAKAGLLNLTRSLAVEwaPK---VRVNAVVVGLVRTEQS 185
PLN02253 PLN02253
xanthoxin dehydrogenase
2-133 1.16e-22

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 91.42  E-value: 1.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGIS--KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINI 79
Cdd:PLN02253  74 DVTVEDDVSRAVDFTVDKFGTLDIMVNNAGLTgpPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSL 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSI 133
Cdd:PLN02253 154 CSVASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALAL 207
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
1-164 1.20e-22

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: 90.06  E-value: 1.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDL--SADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIIN 78
Cdd:cd05370  57 LDVGDAESVEALAEALLSEYPNLDILINNAGIQRPIDLRDPasDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVN 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    79 ISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQPEDLAEYMVAQ 158
Cdd:cd05370 137 VSSGLAFVPMAANPVYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKMPLDEFVDEVVAG 216

                ....*.
gi 809662   159 LKLDPR 164
Cdd:cd05370 217 LERGRE 222
PRK07060 PRK07060
short chain dehydrogenase; Provisional
2-135 1.38e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 90.54  E-value: 1.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQvkeqLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIE-RKAGDIINIS 80
Cdd:PRK07060  61 DVGDDAAIRAALAA----AGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAaGRGGSIVNVS 136
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIEL 135
Cdd:PRK07060 137 SQAALVGLPDHLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEA 191
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
1-124 1.67e-22

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 90.73  E-value: 1.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAG---------------ISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVL 65
Cdd:PRK08277  66 ADVLDKESLEQARQQILEDFGPCDILINGAGgnhpkattdnefhelIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFA 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 809662     66 PEMIERKAGDIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK08277 146 KDMVGRKGGNIINISSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAP 204
PRK06194 PRK06194
hypothetical protein; Provisional
2-127 1.86e-22

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 90.85  E-value: 1.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKfGGFL-DLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA------G 74
Cdd:PRK06194  63 DVSDAAQVEALADAALERFGAVHLLFNNAGVGA-GGLVwENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEkdpayeG 141
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 809662     75 DIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVR--KHNIRVSALTPSTV 127
Cdd:PRK06194 142 HIVNTASMAGLLAPPAMGIYNVSKHAVVSLTETLYQDLSlvTDQVGASVLCPYFV 196
PRK09072 PRK09072
SDR family oxidoreductase;
1-160 1.88e-22

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 90.39  E-value: 1.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVnQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK09072  60 ADLTSEAGR-EAVLARAREMGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVG 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS----IELNLTDGNpeKVMQPEDLAEYMV 156
Cdd:PRK09072 139 STFGSIGYPGYASYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAMNseavQALNRALGN--AMDDPEDVAAAVL 216

                 ....
gi 809662    157 AQLK 160
Cdd:PRK09072 217 QAIE 220
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
2-124 2.49e-22

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 89.83  E-value: 2.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK07523  67 DVTDHDAVRAAIDAFEAEIGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIAS 146
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK07523 147 VQSALARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAP 189
PRK08628 PRK08628
SDR family oxidoreductase;
1-128 2.91e-22

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 89.63  E-value: 2.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGfLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKaGDIINIS 80
Cdd:PRK08628  62 VDLTDDAQCRDAVEQTVAKFGRIDGLVNNAGVNDGVG-LEAGREAFVASLERNLIHYYVMAHYCLPHLKASR-GAIVNIS 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVA 128
Cdd:PRK08628 140 SKTALTGQGGTSGYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVM 187
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
1-164 3.27e-22

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


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 89.28  E-value: 3.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVkdADQVNQAVAQVKEQLGD--IDILINNAGI-SKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDII 77
Cdd:cd05325  54 LDV--TDEIAESAEAVAERLGDagLDVLINNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKII 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    78 NISSTAG---QRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIElnltDGNPEKVMQPEDLAEY 154
Cdd:cd05325 132 NISSRVGsigDNTSGGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGP----FAKNKGPITPEESVAG 207
                       170
                ....*....|.
gi 809662   155 MVAQL-KLDPR 164
Cdd:cd05325 208 LLKVIdNLNEE 218
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
3-152 4.00e-22

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: 89.52  E-value: 4.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     3 VKDADQVNQAVAQVKEQLGDIDILINNAGISKF-GGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:cd08936  68 VGKAEDRERLVATAVNLHGGVDILVSNAAVNPFfGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSS 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVM---------QPEDLA 152
Cdd:cd08936 148 VAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEESMKetlrirrlgQPEDCA 227
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
2-167 6.19e-22

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: 88.79  E-value: 6.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKaGDIINISS 81
Cdd:cd09761  55 DVADETLVKFVVYAMLEKLGRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIAS 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKhNIRVSALTPSTVASDMSIELNLTDGNPE--------KVMQPEDLAe 153
Cdd:cd09761 134 TRAFQSEPDSEAYAASKGGLVALTHALAMSLGP-DIRVNCISPGWINTTEQQEFTAAPLTQEdhaqhpagRVGTPKDIA- 211
                       170
                ....*....|....
gi 809662   154 YMVAQLKLDPRIFI 167
Cdd:cd09761 212 NLVLFLCQQDAGFI 225
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
1-131 9.82e-22

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: 88.29  E-value: 9.82e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERK-AGDIINI 79
Cdd:cd05322  59 ADATNEQSVIALSKGVDEIFKRVDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQI 138
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 809662    80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPST-VASDM 131
Cdd:cd05322 139 NSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLGNlLKSPM 191
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
6-153 1.13e-21

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 88.02  E-value: 1.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     6 ADQVNQAVAQVKEQLGDIDILINNAGIskFGGFLDLS---ADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISST 82
Cdd:cd05340  68 SENCQQLAQRIAVNYPRLDGVLHNAGL--LGDVCPLSeqnPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSS 145
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 809662    83 AGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDgNPEKVMQPEDLAE 153
Cdd:cd05340 146 VGRQGRANWGAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTE-DPQKLKTPADIMP 215
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
2-124 1.43e-21

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: 88.12  E-value: 1.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFG-GFLDLSADEWENIIQVNLMGVYHVTRAVLPEMieRKAGDIINIS 80
Cdd:cd05355  85 DLGDESFCRDLVKEVVKEFGKLDILVNNAAYQHPQeSIEDITTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTT 162
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:cd05355 163 SVTAYKGSPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAP 206
PRK07478 PRK07478
short chain dehydrogenase; Provisional
2-153 1.48e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 87.68  E-value: 1.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFL-DLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK07478  63 DVRDEAYAKALVALAVERFGGLDIAFNNAGTLGEMGPVaEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTS 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 S----TAGQRGAAvtsAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSielNLTDGNPE------------K 144
Cdd:PRK07478 143 TfvghTAGFPGMA---AYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMG---RAMGDTPEalafvaglhalkR 216

                 ....*....
gi 809662    145 VMQPEDLAE 153
Cdd:PRK07478 217 MAQPEEIAQ 225
PRK09242 PRK09242
SDR family oxidoreductase;
1-167 1.93e-21

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 87.50  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK09242  67 ADVSDDEDRRAILDWVEDHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIG 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPstvasdMSIELNLTDG---NPEK------------V 145
Cdd:PRK09242 147 SVSGLTHVRSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAP------WYIRTPLTSGplsDPDYyeqviertpmrrV 220
                        170       180
                 ....*....|....*....|..
gi 809662    146 MQPEDLAEyMVAQLKLDPRIFI 167
Cdd:PRK09242 221 GEPEEVAA-AVAFLCMPAASYI 241
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-152 2.57e-21

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 87.24  E-value: 2.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER-KAGDIINI 79
Cdd:PRK08993  64 ADLRKIDGIPALLERAVAEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINI 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQ---------PED 150
Cdd:PRK08993 144 ASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEILDripagrwglPSD 223

                 ..
gi 809662    151 LA 152
Cdd:PRK08993 224 LM 225
PRK06484 PRK06484
short chain dehydrogenase; Validated
1-124 3.22e-21

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.52  E-value: 3.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISK-FGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMieRKAGDIINI 79
Cdd:PRK06484 322 ADITDEAAVESAFAQIQARWGRLDVLVNNAGIAEvFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNL 399
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK06484 400 GSIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAP 444
PRK07069 PRK07069
short chain dehydrogenase; Validated
2-119 3.25e-21

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 87.07  E-value: 3.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK07069  59 DVTDEAQWQALLAQAADAMGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISS 138
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRV 119
Cdd:PRK07069 139 VAAFKAEPDYTAYNASKAAVASLTKSIALDCARRGLDV 176
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
1-167 3.64e-21

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: 86.73  E-value: 3.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADV---KDADQVNQAVAQVKEqlGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDII 77
Cdd:cd05329  62 CDVssrSERQELMDTVASHFG--GKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIV 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    78 NISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVM---------QP 148
Cdd:cd05329 140 FISSVAGVIAVPSGAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIertplkrfgEP 219
                       170
                ....*....|....*....
gi 809662   149 EDLAEyMVAQLKLDPRIFI 167
Cdd:cd05329 220 EEVAA-LVAFLCMPAASYI 237
PRK07677 PRK07677
short chain dehydrogenase; Provisional
2-124 4.25e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 86.66  E-value: 4.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGiskfGGFL----DLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA-GDI 76
Cdd:PRK07677  58 DVRNPEDVQKMVEQIDEKFGRIDALINNAA----GNFIcpaeDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIkGNI 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 809662     77 INISST-AGQRGAAVtsAYSAS-KFAVLGLTESLMQEV-RKHNIRVSALTP 124
Cdd:PRK07677 134 INMVATyAWDAGPGV--IHSAAaKAGVLAMTRTLAVEWgRKYGIRVNAIAP 182
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
1-147 4.61e-21

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 86.31  E-value: 4.61e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKeqlgDIDILINNAGISKFGGFL---DLSADEWEniIQVNLMGVYHVTRAVLPEMIERKAGDII 77
Cdd:cd05354  57 LDVTDPESIKAAAAQAK----DVDVVINNAGVLKPATLLeegALEALKQE--MDVNVFGLLRLAQAFAPVLKANGGGAIV 130
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    78 NISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQ 147
Cdd:cd05354 131 NLNSVASLKNFPAMGTYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAGGPKESPETVAE 200
PRK05866 PRK05866
SDR family oxidoreductase;
1-177 5.41e-21

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 87.10  E-value: 5.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDlSADEW---ENIIQVNLMGVYHVTRAVLPEMIERKAGDII 77
Cdd:PRK05866  96 CDLSDLDAVDALVADVEKRIGGVDILINNAGRSIRRPLAE-SLDRWhdvERTMVLNYYAPLRLIRGLAPGMLERGDGHII 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     78 NISSTAGQRGAA-VTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPekVMQPEDLAEYMV 156
Cdd:PRK05866 175 NVATWGVLSEASpLFSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIAPTKAYDGLP--ALTADEAAEWMV 252
                        170       180
                 ....*....|....*....|....*.
gi 809662    157 AQ-----LKLDPRIFIKTAGLWSTNP 177
Cdd:PRK05866 253 TAartrpVRIAPRVAVAARALDSVAP 278
PRK06114 PRK06114
SDR family oxidoreductase;
1-131 5.66e-21

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 86.37  E-value: 5.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK06114  65 ADVTSKADLRAAVARTEAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIA 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 809662     81 STAG---QRGaAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK06114 145 SMSGiivNRG-LLQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPM 197
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
24-153 1.09e-20

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: 84.10  E-value: 1.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    24 DILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISSTAGQRGAAVTSAYSASKFAVLG 103
Cdd:cd02266  33 DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDG 112
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662   104 LTESLMQEVRKHNIRVSALTPSTVASDMSIELNltdGNPEKV----------MQPEDLAE 153
Cdd:cd02266 113 LAQQWASEGWGNGLPATAVACGTWAGSGMAKGP---VAPEEIlgnrrhgvrtMPPEEVAR 169
PRK05876 PRK05876
short chain dehydrogenase; Provisional
2-145 1.75e-20

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 85.39  E-value: 1.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER-KAGDIINIS 80
Cdd:PRK05876  63 DVRHREEVTHLADEAFRLLGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQgTGGHVVFTA 142
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPstvasdMSIELNLTdGNPEKV 145
Cdd:PRK05876 143 SFAGLVPNAGLGAYGVAKYGVVGLAETLAREVTADGIGVSVLCP------MVVETNLV-ANSERI 200
PRK05693 PRK05693
SDR family oxidoreductase;
2-129 2.51e-20

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 84.84  E-value: 2.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPeMIERKAGDIINISS 81
Cdd:PRK05693  52 DVNDGAALARLAEELEAEHGGLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFP-LLRRSRGLVVNIGS 130
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVAS 129
Cdd:PRK05693 131 VSGVLVTPFAGAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIAS 178
PRK06482 PRK06482
SDR family oxidoreductase;
2-124 3.25e-20

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 84.78  E-value: 3.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK06482  56 DVTDSAAVRAVVDRAFAALGRIDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSS 135
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK06482 136 EGGQIAYPGFSLYHATKWGIEGFVEAVAQEVAPFGIEFTIVEP 178
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
1-152 6.44e-20

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: 83.54  E-value: 6.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS---KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDII 77
Cdd:cd08930  59 LDITSKESIKELIESYLEKFGRIDILINNAYPSpkvWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSII 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    78 NISSTAG------------QRGAAVTsaYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIEL--NLTDGNPE 143
Cdd:cd08930 139 NIASIYGviapdfriyentQMYSPVE--YSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNNQPSEFleKYTKKCPL 216
                       170
                ....*....|
gi 809662   144 KVM-QPEDLA 152
Cdd:cd08930 217 KRMlNPEDLR 226
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-162 6.51e-20

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 83.62  E-value: 6.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMieRKAGDIINIS 80
Cdd:PRK06077  63 ADVSTREGCETLAKATIDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVrKHNIRVSALTPSTVASDMSIEL----NLTDGN-------PEKVMQPE 149
Cdd:PRK06077 141 SVAGIRPAYGLSIYGAMKAAVINLTKYLALEL-APKIRVNAIAPGFVKTKLGESLfkvlGMSEKEfaekftlMGKILDPE 219
                        170
                 ....*....|...
gi 809662    150 DLAEYMVAQLKLD 162
Cdd:PRK06077 220 EVAEFVAAILKIE 232
PRK07890 PRK07890
short chain dehydrogenase; Provisional
1-125 1.77e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 82.31  E-value: 1.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNA-GISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKaGDIINI 79
Cdd:PRK07890  61 TDITDEDQCANLVALALERFGRVDALVNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMI 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPS 125
Cdd:PRK07890 140 NSMVLRHSQPKYGAYKMAKGALLAASQSLATELGPQGIRVNSVAPG 185
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
1-155 2.21e-19

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 84.51  E-value: 2.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAG-DIINI 79
Cdd:PRK08324 477 CDVTDEAAVQAAFEEAALAFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGgSIVFI 556
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     80 SS---TAGQRGAAvtsAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIelnLTDGNPEKVMQ-----PEDL 151
Cdd:PRK08324 557 ASknaVNPGPNFG---AYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAVVRGSGI---WTGEWIEARAAayglsEEEL 630

                 ....*
gi 809662    152 -AEYM 155
Cdd:PRK08324 631 eEFYR 635
PRK08278 PRK08278
SDR family oxidoreductase;
2-166 2.74e-19

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 82.26  E-value: 2.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK08278  70 DVRDEDQVAAAVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSP 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     82 --TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIElNLTDGnpEKVMQ----PEDLAEYM 155
Cdd:PRK08278 150 plNLDPKWFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPRTTIATAAVR-NLLGG--DEAMRrsrtPEIMADAA 226
                        170
                 ....*....|.
gi 809662    156 VAQLKLDPRIF 166
Cdd:PRK08278 227 YEILSRPAREF 237
PRK06125 PRK06125
short chain dehydrogenase; Provisional
12-130 2.93e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 82.01  E-value: 2.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     12 AVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISSTAGQRGAAVT 91
Cdd:PRK06125  71 AREQLAAEAGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPDADY 150
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 809662     92 SAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASD 130
Cdd:PRK06125 151 ICGSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATD 189
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
1-124 6.50e-19

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: 81.35  E-value: 6.50e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAG--------------ISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLP 66
Cdd:cd08935  61 ADVLDRASLERAREEIVAQFGTVDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGK 140
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 809662    67 EMIERKAGDIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:cd08935 141 DMLEQKGGSIINISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAP 198
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
1-124 7.60e-19

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: 80.65  E-value: 7.60e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAG---ISKFggFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDII 77
Cdd:cd08937  59 ADLETYAGAQGVVRAAVERFGRVDVLINNVGgtiWAKP--YEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIV 136
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 809662    78 NISSTAGQRGAAVtsAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:cd08937 137 NVSSIATRGIYRI--PYSAAKGGVNALTASLAFEHARDGIRVNAVAP 181
PRK07201 PRK07201
SDR family oxidoreductase;
1-100 8.30e-19

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 82.69  E-value: 8.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGfLDLSAD---EWENIIQVNLMGVYHVTRAVLPEMIERKAGDII 77
Cdd:PRK07201 427 CDLTDSAAVDHTVKDILAEHGHVDYLVNNAGRSIRRS-VENSTDrfhDYERTMAVNYFGAVRLILGLLPHMRERRFGHVV 505
                         90       100
                 ....*....|....*....|...
gi 809662     78 NISSTAGQRGAAVTSAYSASKFA 100
Cdd:PRK07201 506 NVSSIGVQTNAPRFSAYVASKAA 528
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
2-153 9.23e-19

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: 80.66  E-value: 9.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLD-LSADEWENIIQVNLMGVYHVTRAVLPEMIERKaGDIINIS 80
Cdd:cd08933  67 DVTKEEDIKTLISVTVERFGRIDCLVNNAGWHPPHQTTDeTSAQEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLS 145
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQPEDLAE 153
Cdd:cd08933 146 SLVGSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATIKEGELAQ 218
PRK05993 PRK05993
SDR family oxidoreductase;
2-129 1.47e-18

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 80.46  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGD-IDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK05993  55 DYAEPESIAALVAQVLELSGGrLDALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCS 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 809662     81 STAG-----QRGaavtsAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVAS 129
Cdd:PRK05993 135 SILGlvpmkYRG-----AYNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIET 183
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-153 1.77e-18

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 79.75  E-value: 1.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLG-DIDILINNAGIS-KFGG-----FLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA 73
Cdd:PRK08642  59 ADVTDREQVQAMFATATEHFGkPITTVVNNALADfSFDGdarkkADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGF 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     74 GDIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALT--------PSTVASDMSIELnLTDGNP-EK 144
Cdd:PRK08642 139 GRIINIGTNLFQNPVVPYHDYTTAKAALLGLTRNLAAELGPYGITVNMVSggllrttdASAATPDEVFDL-IAATTPlRK 217

                 ....*....
gi 809662    145 VMQPEDLAE 153
Cdd:PRK08642 218 VTTPQEFAD 226
PRK06124 PRK06124
SDR family oxidoreductase;
2-130 2.61e-18

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 79.37  E-value: 2.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK06124  68 DIADEEAVAAAFARIDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITS 147
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASD 130
Cdd:PRK06124 148 IAGQVARAGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE 196
PRK09291 PRK09291
SDR family oxidoreductase;
22-124 2.70e-18

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 79.27  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     22 DIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISSTAGQRGAAVTSAYSASKFAV 101
Cdd:PRK09291  73 DVDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHAL 152
                         90       100
                 ....*....|....*....|...
gi 809662    102 LGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK09291 153 EAIAEAMHAELKPFGIQVATVNP 175
PRK07035 PRK07035
SDR family oxidoreductase;
3-124 2.74e-18

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 79.29  E-value: 2.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      3 VKDADQVNQAVAQVKEQLGDIDILINNAGISK-FGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK07035  66 IGEMEQIDALFAHIRERHGRLDILVNNAAANPyFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVAS 145
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK07035 146 VNGVSPGDFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLP 188
PRK05867 PRK05867
SDR family oxidoreductase;
2-131 2.78e-18

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 79.31  E-value: 2.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER-KAGDIINIS 80
Cdd:PRK05867  66 DVSQHQQVTSMLDQVTAELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTA 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 809662     81 STAGQ--RGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK05867 146 SMSGHiiNVPQQVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
2-156 4.18e-18

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: 78.38  E-value: 4.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGF-LDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05365  56 NVTSEQDLEAVVKATVSQFGGITILVNNAGGGGPKPFdMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNIS 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASD--------MSIELNLTDGNPEKVMQPEDLA 152
Cdd:cd05365 136 SMSSENKNVRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDalasvltpEIERAMLKHTPLGRLGEPEDIA 215

                ....
gi 809662   153 EYMV 156
Cdd:cd05365 216 NAAL 219
PRK08265 PRK08265
short chain dehydrogenase; Provisional
1-132 5.97e-18

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 78.51  E-value: 5.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFlDLSADEWENIIQVNLMGVYHVTRAVLPEMIeRKAGDIINIS 80
Cdd:PRK08265  59 TDITDDAAIERAVATVVARFGRVDILVNLACTYLDDGL-ASSRADWLAALDVNLVSAAMLAQAAHPHLA-RGGGAIVNFT 136
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP----STVASDMS 132
Cdd:PRK08265 137 SISAKFAQTGRWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPgwtwSRVMDELS 192
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
1-153 6.63e-18

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 78.23  E-value: 6.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER-KAGDIINI 79
Cdd:PRK08936  64 GDVTVESDVVNLIQTAVKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINM 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVAsdmsielnlTDGNPEKVMQPEDLAE 153
Cdd:PRK08936 144 SSVHEQIPWPLFVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAIN---------TPINAEKFADPKQRAD 208
PRK07062 PRK07062
SDR family oxidoreductase;
2-122 6.63e-18

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 78.16  E-value: 6.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK07062  67 DVLDEADVAAFAAAVEARFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNS 146
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSAL 122
Cdd:PRK07062 147 LLALQPEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSI 187
PRK07577 PRK07577
SDR family oxidoreductase;
1-131 1.22e-17

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 77.07  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQlGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK07577  48 CDLADIEQTAATLAQINEI-HPVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNIC 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 809662     81 STAGQrGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK07577 127 SRAIF-GALDRTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
11-124 1.22e-17

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 77.22  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     11 QAVAQVKEQLGDIDILINNAGI-SKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISSTAGQRGAA 89
Cdd:PRK08945  81 QLADTIEEQFGRLDGVLHNAGLlGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRA 160
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 809662     90 VTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK08945 161 NWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINP 195
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
2-166 2.15e-17

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 76.72  E-value: 2.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:cd09762  67 DIRDEDQVRAAVEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSP 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    82 TAGQRGA--AVTSAYSASKFA----VLGLTEslmqEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQPEDLAEYM 155
Cdd:cd09762 147 PLNLNPKwfKNHTAYTMAKYGmsmcVLGMAE----EFKPGGIAVNALWPRTAIATAAMNMLGGVDVAACCRKPEIMADAA 222
                       170
                ....*....|.
gi 809662   156 VAQLKLDPRIF 166
Cdd:cd09762 223 YAILTKPSSEF 233
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
1-131 2.95e-17

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: 76.37  E-value: 2.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMieRKAGD----- 75
Cdd:cd08942  61 ADLSSEEGIEALVARVAERSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLL--RAAATaenpa 138
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 809662    76 -IINISSTAGQRGAAVTS-AYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:cd08942 139 rVINIGSIAGIVVSGLENySYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKM 196
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
2-169 3.64e-17

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: 76.33  E-value: 3.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQV-KEQLGDIDILINNA--GISKFG-----GFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA 73
Cdd:cd09763  61 DHSDDDEVEALFERVaREQQGRLDILVNNAyaAVQLILvgvakPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGK 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    74 GDIINISSTAGQRGaAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASD-----MSIELNLTDGNPEKVMQP 148
Cdd:cd09763 141 GLIVIISSTGGLEY-LFNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTElvlemPEDDEGSWHAKERDAFLN 219
                       170       180
                ....*....|....*....|....
gi 809662   149 EDLAEYM---VAQLKLDPRIFIKT 169
Cdd:cd09763 220 GETTEYSgrcVVALAADPDLMELS 243
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
2-152 5.82e-17

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 75.65  E-value: 5.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGiskfGGF---LDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIIN 78
Cdd:PRK06113  68 DITSEQELSALADFALSKLGKVDILVNNAG----GGGpkpFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILT 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     79 ISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM-------SIELNLTDGNPEKVM-QPED 150
Cdd:PRK06113 144 ITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDAlksvitpEIEQKMLQHTPIRRLgQPQD 223

                 ..
gi 809662    151 LA 152
Cdd:PRK06113 224 IA 225
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
1-124 6.06e-17

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 75.75  E-value: 6.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGiskfgG------FLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAG 74
Cdd:PRK12823  63 ADLETYAGAQAAMAAAVEAFGRIDVLINNVG-----GtiwakpFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGG 137
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 809662     75 DIINISSTAgQRGAAVTsAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK12823 138 AIVNVSSIA-TRGINRV-PYSAAKGGVNALTASLAFEYAEHGIRVNAVAP 185
PRK07791 PRK07791
short chain dehydrogenase; Provisional
1-125 7.10e-17

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 75.86  E-value: 7.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTR-AVLPEMIERKAGD---- 75
Cdd:PRK07791  71 DDIADWDGAANLVDAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRhAAAYWRAESKAGRavda 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 809662     76 -IINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPS 125
Cdd:PRK07791 151 rIINTSSGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA 201
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
1-131 1.80e-16

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: 74.57  E-value: 1.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGI--SKFGgfldLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIIN 78
Cdd:cd05327  59 LDLSSLASVRQFAEEFLARFPRLDILINNAGImaPPRR----LTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVN 134
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 809662    79 ISSTAGQRGA--------------AVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:cd05327 135 VSSIAHRAGPidfndldlennkeySPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTEL 201
PRK06500 PRK06500
SDR family oxidoreductase;
1-146 2.37e-16

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 73.84  E-value: 2.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPeMIERKAGDIINIS 80
Cdd:PRK06500  59 ADAGDVAAQKALAQALAEAFGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLP-LLANPASIVLNGS 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 809662     81 STAgQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVM 146
Cdd:PRK06500 138 INA-HIGMPNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATLDAVA 202
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
2-129 5.72e-16

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: 72.81  E-value: 5.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDII--NI 79
Cdd:cd08943  57 DVTSEAQVQSAFEQAVLEFGGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIvfNA 136
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 809662    80 S--STAGQRGAAvtsAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVAS 129
Cdd:cd08943 137 SknAVAPGPNAA---AYSAAKAAEAHLARCLALEGGEDGIRVNTVNPDAVFR 185
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
1-127 7.31e-16

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: 72.31  E-value: 7.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:cd05357  57 ADLSDFAACADLVAAAFRAFGRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINII 136
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKhNIRVSALTPSTV 127
Cdd:cd05357 137 DAMTDRPLTGYFAYCMSKAALEGLTRSAALELAP-NIRVNGIAPGLI 182
PRK09730 PRK09730
SDR family oxidoreductase;
1-156 9.84e-16

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 72.19  E-value: 9.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLD-LSADEWENIIQVNLMGVYHVTRAVLPEMIER---KAGDI 76
Cdd:PRK09730  58 ADISDENQVVAMFTAIDQHDEPLAALVNNAGILFTQCTVEnLTAERINRVLSTNVTGYFLCCREAVKRMALKhggSGGAI 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     77 INISSTAGQRGAAVTSA-YSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielNLTDGNPEKV--------MQ 147
Cdd:PRK09730 138 VNVSSAASRLGAPGEYVdYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEM----HASGGEPGRVdrvksnipMQ 213
                        170
                 ....*....|...
gi 809662    148 ----PEDLAEYMV 156
Cdd:PRK09730 214 rggqPEEVAQAIV 226
PRK07814 PRK07814
SDR family oxidoreductase;
1-152 1.13e-15

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 72.12  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERK-AGDIINI 79
Cdd:PRK07814  66 ADLAHPEATAGLAGQAVEAFGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINI 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHnIRVSALTPSTVasdMSIELNLTDGNPE------------KVMQ 147
Cdd:PRK07814 146 SSTMGRLAGRGFAAYGTAKAALAHYTRLAALDLCPR-IRVNAIAPGSI---LTSALEVVAANDElrapmekatplrRLGD 221

                 ....*
gi 809662    148 PEDLA 152
Cdd:PRK07814 222 PEDIA 226
PLN02780 PLN02780
ketoreductase/ oxidoreductase
9-132 2.08e-15

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 72.21  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      9 VNQAVAQVKEQLG--DIDILINNAGIS----KFggFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISSt 82
Cdd:PLN02780 117 IDEGVKRIKETIEglDVGVLINNVGVSypyaRF--FHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGS- 193
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 809662     83 agqrGAAVT-------SAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:PLN02780 194 ----GAAIVipsdplyAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMA 246
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-131 2.36e-15

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 72.56  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK08261 264 DITAPDAPARIAEHLAERHGGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSS 343
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 809662     82 TAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK08261 344 ISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQM 393
PRK08251 PRK08251
SDR family oxidoreductase;
2-132 4.33e-15

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 70.35  E-value: 4.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISK-----FGGFldlsadeWENI--IQVNLMGVYHVTRAVLPEMIERKAG 74
Cdd:PRK08251  61 DVNDHDQVFEVFAEFRDELGGLDRVIVNAGIGKgarlgTGKF-------WANKatAETNFVAALAQCEAAMEIFREQGSG 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 809662     75 DIINISSTAGQRGA-AVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMS 132
Cdd:PRK08251 134 HLVLISSVSAVRGLpGVKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMN 192
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
2-150 5.28e-15

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: 70.46  E-value: 5.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGI-SKFGGFLDLSADE----WENIIQVNLMGVYHVTRAVLPEMIERKaGDI 76
Cdd:cd05348  58 DVRSLADNERAVARCVERFGKLDCFIGNAGIwDYSTSLVDIPEEKldeaFDELFHINVKGYILGAKAALPALYATE-GSV 136
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 809662    77 INISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHnIRVSALTPSTVASDMSIELNLTDGNPEKVMQPED 150
Cdd:cd05348 137 IFTVSNAGFYPGGGGPLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLRGPASLGQGETSISTPPLD 209
PRK12742 PRK12742
SDR family oxidoreductase;
1-159 5.82e-15

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 69.79  E-value: 5.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVkeqlGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIErkAGDIINIS 80
Cdd:PRK12742  58 TDSADRDAVIDVVRKS----GALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPE--GGRIIIIG 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQR----GAAvtsAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielNLTDGNPEKVM---------- 146
Cdd:PRK12742 132 SVNGDRmpvaGMA---AYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDA----NPANGPMKDMMhsfmaikrhg 204
                        170
                 ....*....|...
gi 809662    147 QPEDLAEyMVAQL 159
Cdd:PRK12742 205 RPEEVAG-MVAWL 216
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-131 1.05e-14

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 69.61  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS--KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA----- 73
Cdd:PRK12745  59 ADVADLSAHEAMLDAAQAAWGRIDCLVNNAGVGvkVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelp 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 809662     74 -GDIINISSTAgqrgAAVTSA----YSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK12745 139 hRSIVFVSSVN----AIMVSPnrgeYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
2-131 1.65e-14

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 69.21  E-value: 1.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFG-GFLDLSADE----WENIIQVNLMGVYHVTRAVLPEMIERKaGDI 76
Cdd:PRK06200  60 DVTSYADNQRAVDQTVDAFGKLDCFVGNAGIWDYNtSLVDIPAETldtaFDEIFNVNVKGYLLGAKAALPALKASG-GSM 138
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 809662     77 INISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHnIRVSALTPSTVASDM 131
Cdd:PRK06200 139 IFTLSNSSFYPGGGGPLYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDL 192
PRK08017 PRK08017
SDR family oxidoreductase;
2-124 3.01e-14

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 68.19  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGD-IDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK08017  53 DLDDPESVERAADEVIALTDNrLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTS 132
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK08017 133 SVMGLISTPGRGAYAASKYALEAWSDALRMELRHSGIKVSLIEP 176
PRK06123 PRK06123
SDR family oxidoreductase;
1-145 3.49e-14

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 67.88  E-value: 3.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLD-LSADEWENIIQVNLMGVYHVTRAVLPEMIER---KAGDI 76
Cdd:PRK06123  59 ADVADEADVLRLFEAVDRELGRLDALVNNAGILEAQMRLEqMDAARLTRIFATNVVGSFLCAREAVKRMSTRhggRGGAI 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     77 INISSTAGQRGAAVTSA-YSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMsielNLTDGNPEKV 145
Cdd:PRK06123 139 VNVSSMAARLGSPGEYIdYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEI----HASGGEPGRV 204
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
1-133 5.54e-14

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: 67.49  E-value: 5.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGIS--KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA----- 73
Cdd:cd05337  58 ADIGELSDHEALLDQAWEDFGRLDCLVNNAGIAvrPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDrfdgp 137
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 809662    74 -GDIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSI 133
Cdd:cd05337 138 hRSIIFVTSINAYLVSPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTA 198
PRK07576 PRK07576
short chain dehydrogenase; Provisional
1-128 5.72e-14

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 67.67  E-value: 5.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGiskfGGFL----DLSADEWENIIQVNLMGVYHVTRAVLPEMiERKAGDI 76
Cdd:PRK07576  65 ADVRDYAAVEAAFAQIADEFGPIDVLVSGAA----GNFPapaaGMSANGFKTVVDIDLLGTFNVLKAAYPLL-RRPGASI 139
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 809662     77 INISstAGQRGAAV--TSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVA 128
Cdd:PRK07576 140 IQIS--APQAFVPMpmQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIA 191
PRK06128 PRK06128
SDR family oxidoreductase;
2-127 8.32e-14

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 67.58  E-value: 8.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKF-GGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMierKAG-DIINI 79
Cdd:PRK06128 114 DLKDEAFCRQLVERAVKELGGLDILVNIAGKQTAvKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL---PPGaSIINT 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTV 127
Cdd:PRK06128 191 GSIQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPV 238
PRK09135 PRK09135
pteridine reductase; Provisional
1-124 1.41e-13

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 66.49  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAgiSKF-----GgflDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKaGD 75
Cdd:PRK09135  64 ADLLDPDALPELVAACVAAFGRLDALVNNA--SSFyptplG---SITEAQWDDLFASNLKAPFFLSQAAAPQLRKQR-GA 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 809662     76 IINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHnIRVSALTP 124
Cdd:PRK09135 138 IVNITDIHAERPLKGYPVYCAAKAALEMLTRSLALELAPE-VRVNAVAP 185
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
1-143 1.61e-13

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: 66.16  E-value: 1.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAG----ISKFGgflDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKA-GD 75
Cdd:cd05367  56 ADLSDAAGVEQLLEAIRKLDGERDLLINNAGslgpVSKIE---FIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKT 132
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 809662    76 IINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKhnIRVSALTPSTVASDMSIELNLTDGNPE 143
Cdd:cd05367 133 VVNVSSGAAVNPFKGWGLYCSSKAARDMFFRVLAAEEPD--VRVLSYAPGVVDTDMQREIRETSADPE 198
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-130 2.98e-13

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 65.51  E-value: 2.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK08063  61 ANVGDVEKIKEMFAQIDEEFGRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLS 140
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASD 130
Cdd:PRK08063 141 SLGSIRYLENYTTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-124 3.42e-13

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 65.96  E-value: 3.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEqLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIER-KAGD----- 75
Cdd:PRK07792  70 DISQRATADELVATAVG-LGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKaKAAGgpvyg 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 809662     76 -IINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK07792 149 rIVNTSSEAGLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK05717 PRK05717
SDR family oxidoreductase;
2-124 6.71e-13

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 64.53  E-value: 6.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGIS--KFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPeMIERKAGDIINI 79
Cdd:PRK05717  64 DVADEAQVAAGVAEVLGQFGRLDALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAP-YLRAHNGAIVNL 142
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKhNIRVSALTP 124
Cdd:PRK05717 143 ASTRARQSEPDTEAYAASKGGLLALTHALAISLGP-EIRVNAVSP 186
PRK08339 PRK08339
short chain dehydrogenase; Provisional
1-154 6.98e-13

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 64.49  E-value: 6.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEqLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIS 80
Cdd:PRK08339  65 ADLTKREDLERTVKELKN-IGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYST 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKVMQPEDLAEY 154
Cdd:PRK08339 144 SVAIKEPIPNIALSNVVRISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDRAKREGKSVEEALQEY 217
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
11-145 1.14e-12

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 63.75  E-value: 1.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    11 QAVAQVKEQLGDIDILINNAGISKFGGFLDLSADE-WENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISSTAGQRGAA 89
Cdd:cd05361  61 ELVDAVLQAGGAIDVLVSNDYIPRPMNPIDGTSEAdIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLA 140
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 809662    90 VTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTDGNPEKV 145
Cdd:cd05361 141 YNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSPTYFPTSDWENNPELR 196
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-124 8.55e-12

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 61.63  E-value: 8.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIs 80
Cdd:PRK12748  74 IDLSQPYAPNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINL- 152
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 809662     81 sTAGQRGAAVTS--AYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK12748 153 -TSGQSLGPMPDelAYAATKGAIEAFTKSLAPELAEKGITVNAVNP 197
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-124 1.08e-11

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 61.34  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTrAVLPEMIERK-AGDIINIS 80
Cdd:PRK12859  76 DLTQNDAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLS-SQFARGFDKKsGGRIINMT 154
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK12859 155 SGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINP 198
PRK06947 PRK06947
SDR family oxidoreductase;
2-147 1.94e-11

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 60.59  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGI-SKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAG---DII 77
Cdd:PRK06947  60 DVANEADVIAMFDAVQSAFGRLDALVNNAGIvAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGrggAIV 139
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 809662     78 NISSTAGQRGAAVTSA-YSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASdmsiELNLTDGNPEKVMQ 147
Cdd:PRK06947 140 NVSSIASRLGSPNEYVdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIET----EIHASGGQPGRAAR 206
PRK12746 PRK12746
SDR family oxidoreductase;
1-135 2.84e-11

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 60.05  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQL------GDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMieRKAG 74
Cdd:PRK12746  63 ADLNSIDGVKKLVEQLKNELqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEG 140
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 809662     75 DIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIEL 135
Cdd:PRK12746 141 RVINISSAEVRLGFTGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKL 201
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
1-145 7.28e-10

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: 55.96  E-value: 7.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQL-GDIDILINNAGISKFGGFldlsadewENIIQVNLMGVYHVTRAVLPEMIERKAGDIINI 79
Cdd:cd05328  38 ADLSTPEGRAAAIADVLARCsGVLDGLVNCAGVGGTTVA--------GLVLKVNYFGLRALMEALLPRLRKGHGPAAVVV 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    80 SSTAG---------------------------QRGAAVTSAYSASKFAVLGLTESLM-QEVRKHNIRVSALTPSTVASDM 131
Cdd:cd05328 110 SSIAGagwaqdklelakalaagtearavalaeHAGQPGYLAYAGSKEALTVWTRRRAaTWLYGAGVRVNTVAPGPVETPI 189
                       170
                ....*....|....
gi 809662   132 SIELNLTDGNPEKV 145
Cdd:cd05328 190 LQAFLQDPRGGESV 203
PRK05875 PRK05875
short chain dehydrogenase; Provisional
1-131 8.23e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 56.35  E-value: 8.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISK-FGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINI 79
Cdd:PRK05875  65 ADVTDEDQVARAVDAATAWHGRLHGVVHCAGGSEtIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGI 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK05875 145 SSIAASNTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDL 196
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
1-164 1.13e-09

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: 55.22  E-value: 1.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDAdqvnQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIInis 80
Cdd:cd11730  49 ADVAAE----LEVWALAQELGPLDLLVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFL--- 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662    81 staGQRGAAVT----SAYSASKFAVLGLTESLMQEVRKhnIRVSALTPSTVASDMsieLNLTDGNPEKVMQPEDLAEYMV 156
Cdd:cd11730 122 ---GAYPELVMlpglSAYAAAKAALEAYVEVARKEVRG--LRLTLVRPPAVDTGL---WAPPGRLPKGALSPEDVAAAIL 193

                ....*...
gi 809662   157 AQLKLDPR 164
Cdd:cd11730 194 EAHQGEPQ 201
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
5-153 1.73e-09

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: 54.64  E-value: 1.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     5 DADQVNQAVAQVKEQLGDIDILINNAGISKFGgflDLSADE----WENIIQVNLMGVYHVTRAVLPEMieRKAGDIINIS 80
Cdd:cd05334  51 FTEQAKQVVASVARLSGKVDALICVAGGWAGG---SAKSKSfvknWDLMWKQNLWTSFIASHLATKHL--LSGGLLVLTG 125
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQE--VRKHNIRVSALTPSTVASDMSIElNLTDGNPEKVMQPEDLAE 153
Cdd:cd05334 126 AKAALEPTPGMIGYGAAKAAVHQLTQSLAAEnsGLPAGSTANAILPVTLDTPANRK-AMPDADFSSWTPLEFIAE 199
PRK12747 PRK12747
short chain dehydrogenase; Provisional
24-135 2.45e-09

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 54.70  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     24 DILINNAGISKfGGFLDLSADEW-ENIIQVNLMGVYHVTRAVLPEMieRKAGDIINISSTAGQRGAAVTSAYSASKFAVL 102
Cdd:PRK12747  90 DILINNAGIGP-GAFIEETTEQFfDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFIAYSMTKGAIN 166
                         90       100       110
                 ....*....|....*....|....*....|...
gi 809662    103 GLTESLMQEVRKHNIRVSALTPSTVASDMSIEL 135
Cdd:PRK12747 167 TMTFTLAKQLGARGITVNAILPGFIKTDMNAEL 199
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
1-127 3.24e-09

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 54.24  E-value: 3.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQlgdIDILINNAGISKFGGFLDlsadewenIIQVNLMGVYHVTRAVLPEMieRKAGDIINIS 80
Cdd:PRK12428  30 ADLGDPASIDAAVAALPGR---IDALFNIAGVPGTAPVEL--------VARVNFLGLRHLTEALLPRM--APGGAIVNVA 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 809662     81 STAG---------------------------QRGAAVTSAYSASKFAVLGLTeslMQEV----RKHNIRVSALTPSTV 127
Cdd:PRK12428  97 SLAGaewpqrlelhkalaatasfdegaawlaAHPVALATGYQLSKEALILWT---MRQAqpwfGARGIRVNCVAPGPV 171
PRK07985 PRK07985
SDR family oxidoreductase;
2-158 4.48e-09

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 54.23  E-value: 4.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGI-SKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMieRKAGDIINIS 80
Cdd:PRK07985 108 DLSDEKFARSLVHEAHKALGGLDIMALVAGKqVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLL--PKGASIITTS 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIelnlTDGNPEKVM-------------Q 147
Cdd:PRK07985 186 SIQAYQPSPHLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQI----SGGQTQDKIpqfgqqtpmkragQ 261
                        170
                 ....*....|....
gi 809662    148 PEDLAE---YMVAQ 158
Cdd:PRK07985 262 PAELAPvyvYLASQ 275
PRK09186 PRK09186
flagellin modification protein A; Provisional
2-124 8.00e-09

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 53.07  E-value: 8.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNA-GISKFGG--FLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIIN 78
Cdd:PRK09186  63 DITDQESLEEFLSKSAEKYGKIDGAVNCAyPRNKDYGkkFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVN 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 809662     79 ISSTAG--------QRGAAVTSA--YSASKFAVLGLTESLMQEVRKHNIRVSALTP 124
Cdd:PRK09186 143 ISSIYGvvapkfeiYEGTSMTSPveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSP 198
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
1-131 4.50e-08

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: 50.66  E-value: 4.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADqvnqAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERkaGDIINIS 80
Cdd:cd11731  37 VDITDEA----SIKALFEKVGHFDAIVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLNDG--GSITLTS 110
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 809662    81 STAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKhNIRVSALTPSTVASDM 131
Cdd:cd11731 111 GILAQRPIPGGAAAATVNGALEGFVRAAAIELPR-GIRINAVSPGVVEESL 160
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
1-96 8.45e-08

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: 50.83  E-value: 8.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERkagdIINIS 80
Cdd:cd08953 267 ADVTDAAAVRRLLEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDF----FVLFS 342
                        90
                ....*....|....*.
gi 809662    81 STAGQRGAAVTSAYSA 96
Cdd:cd08953 343 SVSAFFGGAGQADYAA 358
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-152 5.53e-07

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 47.83  E-value: 5.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSadEWENIIQVNLMGVYHVTRAVLPEMieRKAGDIINISS 81
Cdd:PRK05786  61 DVSSTESARNVIEKAAKVLNAIDGLVVTVGGYVEDTVEEFS--GLEEMLTNHIKIPLYAVNASLRFL--KEGSSIVLVSS 136
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 809662     82 TAGQRGAAVTS-AYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIELNLTD----GNPEkvMQPEDLA 152
Cdd:PRK05786 137 MSGIYKASPDQlSYAVAKAGLAKAVEILASELLGRGIRVNGIAPTTISGDFEPERNWKKlrklGDDM--APPEDFA 210
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
2-131 6.25e-07

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: 47.85  E-value: 6.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFldLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:cd09807  60 DLASLKSIRAFAAEFLAEEDRLDVLINNAGVMRCPYS--KTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSS 137
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 809662    82 TAGQRGAAVTS------------AYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:cd09807 138 LAHKAGKINFDdlnseksyntgfAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
PRK08303 PRK08303
short chain dehydrogenase; Provisional
5-134 1.29e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 46.92  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      5 DADQVNQAVAQVKEQLGDIDILINNAgiskFGG--FLDLSADEWE----NIIQVNLMGV-YHV--TRAVLPEMIERKAGD 75
Cdd:PRK08303  78 VPEQVRALVERIDREQGRLDILVNDI----WGGekLFEWGKPVWEhsldKGLRMLRLAIdTHLitSHFALPLLIRRPGGL 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 809662     76 IINISSTAGQRGAA---VTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIE 134
Cdd:PRK08303 154 VVEITDGTAEYNAThyrLSVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPGWLRSEMMLD 215
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
1-127 1.38e-06

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 46.90  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAqvkeqlgDIDILINNAGISkfggflDLSADEWENIIQVNLMGVYHVTRAVLPEMIERkagdIINIS 80
Cdd:COG0451  50 GDLRDPEALAAALA-------GVDAVVHLAAPA------GVGEEDPDETLEVNVEGTLNLLEAARAAGVKR----FVYAS 112
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 809662    81 STA--GQRGAAVT--------SAYSASKFAVlgltESLMQEV-RKHNIRVSALTPSTV 127
Cdd:COG0451 113 SSSvyGDGEGPIDedtplrpvSPYGASKLAA----ELLARAYaRRYGLPVTILRPGNV 166
PRK08703 PRK08703
SDR family oxidoreductase;
7-129 7.05e-06

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 44.54  E-value: 7.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      7 DQVNQAVAQVKEQL-GDIDILINNAG-ISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISSTAG 84
Cdd:PRK08703  71 KEFEQFAATIAEATqGKLDGIVHCAGyFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHG 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 809662     85 QRGAAVTSAYSASKFAVLGLTESLMQEVRKH-NIRVSALTPSTVAS 129
Cdd:PRK08703 151 ETPKAYWGGFGASKAALNYLCKVAADEWERFgNLRANVLVPGPINS 196
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
1-132 1.45e-05

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 44.02  E-value: 1.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     1 ADVKDADQVNQAVAQVKEqLGDIDILINNAGISKfGGFLDLSADEWENIIQVNLMGVYhvtraVLPEMIeRKAGDIINIS 80
Cdd:cd08951  60 GDLSSLAETRKLADQVNA-IGRFDAVIHNAGILS-GPNRKTPDTGIPAMVAVNVLAPY-----VLTALI-RRPKRLIYLS 131
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 809662    81 ST-------------AGQRGAAVTSAYSASKFAVLGLTESLmqEVRKHNIRVSALTPSTVASDMS 132
Cdd:cd08951 132 SGmhrggnaslddidWFNRGENDSPAYSDSKLHVLTLAAAV--ARRWKDVSSNAVHPGWVPTKMG 194
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
1-131 2.11e-05

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 43.52  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDI-LINNAG----ISKFGgflDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKaGD 75
Cdd:PRK06924  58 QDVHELETNFNEILSSIQEDNVSSIhLINNAGmvapIKPIE---KAESEELITNVHLNLLAPMILTSTFMKHTKDWK-VD 133
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     76 --IINISSTAGQRGAAVTSAYSASKFAVLGLTES--LMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK06924 134 krVINISSGAAKNPYFGWSAYCSSKAGLDMFTQTvaTEQEEEEYPVKIVAFSPGVMDTNM 193
PRK09134 PRK09134
SDR family oxidoreductase;
1-124 3.02e-05

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 42.99  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINIs 80
Cdd:PRK09134  66 ADLADEAEVRALVARASAALGPITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNM- 144
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 809662     81 stAGQRGAAVTS---AYSASKFAVLGLTESLMQEVRKhNIRVSALTP 124
Cdd:PRK09134 145 --IDQRVWNLNPdflSYTLSKAALWTATRTLAQALAP-RIRVNAIGP 188
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
1-96 3.15e-05

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 42.47  E-value: 3.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662        1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERkagdIINIS 80
Cdd:smart00822  60 CDVADRDALAAVLAAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDF----FVLFS 135
                           90
                   ....*....|....*.
gi 809662       81 STAGQRGAAVTSAYSA 96
Cdd:smart00822 136 SIAGVLGSPGQANYAA 151
PRK07023 PRK07023
SDR family oxidoreductase;
2-139 4.52e-05

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 42.31  E-value: 4.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDID----ILINNAGISKFGGFLD-LSADEWENIIQVNLMGVYHVTRAVL---PEMIERKa 73
Cdd:PRK07023  53 DLSDAAAAAAWLAGDLLAAFVDGasrvLLINNAGTVEPIGPLAtLDAAAIARAVGLNVAAPLMLTAALAqaaSDAAERR- 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 809662     74 gdIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHnIRVSALTPSTVASDMSIELNLTD 139
Cdd:PRK07023 132 --ILHISSGAARNAYAGWSVYCATKAALDHHARAVALDANRA-LRIVSLAPGVVDTGMQATIRATD 194
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
1-96 6.57e-05

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 41.39  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662       1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERkagdIINIS 80
Cdd:pfam08659  60 CDVSDPDAVAALLAEIKAEGPPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDF----FVLFS 135
                          90
                  ....*....|....*.
gi 809662      81 STAGQRGAAVTSAYSA 96
Cdd:pfam08659 136 SIAGLLGSPGQANYAA 151
PRK07102 PRK07102
SDR family oxidoreductase;
42-153 8.75e-05

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 41.45  E-value: 8.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     42 SADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSA 121
Cdd:PRK07102  96 DPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTAFLSGLRNRLFKSGVHVLT 175
                         90       100       110
                 ....*....|....*....|....*....|...
gi 809662    122 LTPSTVASDMSIELNLtdgnPEK-VMQPEDLAE 153
Cdd:PRK07102 176 VKPGFVRTPMTAGLKL----PGPlTAQPEEVAK 204
PRK08177 PRK08177
SDR family oxidoreductase;
2-131 1.93e-04

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 40.40  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLgdIDILINNAGISkfgGFLDLSADEweniIQVNLMGVYHVTRAVLP--------EMIERKA 73
Cdd:PRK08177  53 DMNDPASLDQLLQRLQGQR--FDLLFVNAGIS---GPAHQSAAD----ATAAEIGQLFLTNAIAPirlarrllGQVRPGQ 123
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 809662     74 GDIINISSTAG--QRGAAVTSA-YSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDM 131
Cdd:PRK08177 124 GVLAFMSSQLGsvELPDGGEMPlYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
9-135 2.55e-04

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 40.08  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      9 VNQAVAQvkeqlGDIDILINNAGIskfggfLDLSADEWEN------IIQVNLMGVYHVTRAVLPEMIERKAGDIINISST 82
Cdd:PRK07904  79 IDAAFAG-----GDVDVAIVAFGL------LGDAEELWQNqrkavqIAEINYTAAVSVGVLLGEKMRAQGFGQIIAMSSV 147
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 809662     83 AGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDMSIEL 135
Cdd:PRK07904 148 AGERVRRSNFVYGSTKAGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMSAHA 200
PRK06101 PRK06101
SDR family oxidoreductase;
2-141 4.99e-04

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 39.47  E-value: 4.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQlgdIDILINNAGISKF--GGFLDlsADEWENIIQVNLMGVYHVTRAVLPEMieRKAGDIINI 79
Cdd:PRK06101  54 DVTDHPGTKAALSQLPFI---PELWIFNAGDCEYmdDGKVD--ATLMARVFNVNVLGVANCIEGIQPHL--SCGHRVVIV 126
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 809662     80 SSTAGQRGAAVTSAYSASKFAVLGLTESLMQEVRKHNIRVSALTPSTVASDmsielnLTDGN 141
Cdd:PRK06101 127 GSIASELALPRAEAYGASKAAVAYFARTLQLDLRPKGIEVVTVFPGFVATP------LTDKN 182
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
2-129 1.49e-03

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 37.77  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINN---AGISKFGG-FLDLSADEWENIIQVNLMGVYHVTRAVLPEMIErkAGDII 77
Cdd:PRK07370  67 DVQDDAQIEETFETIKQKWGKLDILVHClafAGKEELIGdFSATSREGFARALEISAYSLAPLCKAAKPLMSE--GGSIV 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 809662     78 NISSTAGQRgaaVTSAYSASKFAVLGLTES---LMQEVRKHNIRVSALTPS---TVAS 129
Cdd:PRK07370 145 TLTYLGGVR---AIPNYNVMGVAKAALEASvryLAAELGPKNIRVNAISAGpirTLAS 199
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
2-81 2.53e-03

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: 37.19  E-value: 2.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662     2 DVKDADQVNQAVAQVKEQLGDIDILINNAG--ISKfggfLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINI 79
Cdd:cd09808  60 DMSDPKQVWEFVEEFKEEGKKLHVLINNAGcmVNK----RELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITV 135

                ..
gi 809662    80 SS 81
Cdd:cd09808 136 SS 137
PRK06196 PRK06196
oxidoreductase; Provisional
2-90 3.35e-03

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 36.97  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      2 DVKDADQVNQAVAQVKEQLGDIDILINNAGIskFGGFLDLSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGDIINISS 81
Cdd:PRK06196  79 DLADLESVRAFAERFLDSGRRIDILINNAGV--MACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSS 156

                 ....*....
gi 809662     82 tAGQRGAAV 90
Cdd:PRK06196 157 -AGHRRSPI 164
PRK06940 PRK06940
short chain dehydrogenase; Provisional
1-93 5.66e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 36.15  E-value: 5.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVnQAVAQVKEQLGDIDILINNAGISKfggfldlSADEWENIIQVNLMGVYHVTRAVLPEMIERKAGdiINIS 80
Cdd:PRK06940  56 VDVSSRESV-KALAATAQTLGPVTGLVHTAGVSP-------SQASPEAILKVDLYGTALVLEEFGKVIAPGGAG--VVIA 125
                         90
                 ....*....|...
gi 809662     81 STAGQRGAAVTSA 93
Cdd:PRK06940 126 SQSGHRLPALTAE 138
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
1-125 6.53e-03

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 36.06  E-value: 6.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 809662      1 ADVKDADQVNQAVAQVKEQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMGVYHVTRAvLPEMIER---KAGDII 77
Cdd:PRK06483  53 ADFSTNAGIMAFIDELKQHTDGLRAIIHNASDWLAEKPGAPLADVLARMMQIHVNAPYLLNLA-LEDLLRGhghAASDII 131
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 809662     78 NISSTAGQRGAAVTSAYSASKFAVLGLTESLmqeVRKH--NIRVSALTPS 125
Cdd:PRK06483 132 HITDYVVEKGSDKHIAYAASKAALDNMTLSF---AAKLapEVKVNSIAPA 178
PRK07578 PRK07578
short chain dehydrogenase; Provisional
18-56 8.03e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 35.56  E-value: 8.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 809662     18 EQLGDIDILINNAGISKFGGFLDLSADEWENIIQVNLMG 56
Cdd:PRK07578  51 EKVGKVDAVVSAAGKVHFAPLAEMTDEDFNVGLQSKLMG 89
 
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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