NCBI Conserved Domain Search

Conserved domains on [gi|809662|emb|CAA29533|]

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unnamed protein product, partial [Bacillus subtilis]

Protein Classification

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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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

(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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

(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

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

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

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

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

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

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

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

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

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

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

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

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

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