NCBI Conserved Domain Search

Conserved domains on [gi|498358419|ref|WP_010672575|]

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MULTISPECIES: SDR family oxidoreductase [Aeromonas]

Protein Classification

SDR family oxidoreductase( domain architecture ID 11468002)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue

CATH: 3.40.50.720

EC: 1.-.-.-

Gene Ontology: GO:0016491

PubMed: 19011750|19011748|12604210|19027726|20423462

SCOP: 4000029

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

YdfG

COG4221

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...

27-237

2.06e-70

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: 215.43 E-value: 2.06e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQALNL---PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLN 103
Cdd:COG4221   29 GARVVLAARRAERLEALAAelgGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMID 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 104 INVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:COG4221  109 VNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEF 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498358419 184 LSHTTDERIKAGYHDWKDqmGGVIAPEVIADAVLYAWHQPANVCVREIVLAATR 237
Cdd:COG4221  189 LDSVFDGDAEAAAAVYEG--LEPLTPEDVAEAVLFALTQPAHVNVNELVLRPTA 240

Name

Accession

Description

Interval

E-value

YdfG

COG4221

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...

27-237

2.06e-70

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: 215.43 E-value: 2.06e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQALNL---PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLN 103
Cdd:COG4221   29 GARVVLAARRAERLEALAAelgGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMID 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 104 INVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:COG4221  109 VNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEF 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498358419 184 LSHTTDERIKAGYHDWKDqmGGVIAPEVIADAVLYAWHQPANVCVREIVLAATR 237
Cdd:COG4221  189 LDSVFDGDAEAAAAVYEG--LEPLTPEDVAEAVLFALTQPAHVNVNELVLRPTA 240

CAD_SDR_c

cd08934

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...

27-238

2.76e-51

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: 166.94 E-value: 2.76e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQALNLPDT------LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQ 100
Cdd:cd08934   27 GAAVAIAARRVDRLEALADELEaeggkaLVLELDVTDEQQVDAAVERTVEALGRLDILVNNAGIMLLGPVEDADTTDWTR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 101 MLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVE 180
Cdd:cd08934  107 MIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVD 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 181 TELLSHTTDERIKAGYHDWKDQMGGVIApEVIADAVLYAWHQPANVCVREIVLAATRQ 238
Cdd:cd08934  187 TELRDHITHTITKEAYEERISTIRKLQA-EDIAAAVRYAVTAPHHVTVNEILIRPTDQ 243

adh_short

pfam00106

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

27-184

2.54e-41

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

Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 139.67 E-value: 2.54e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   27 GHPLLLLARRVEPMQAL------NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQ 100
Cdd:pfam00106  24 GAKVVLVDRSEEKLEAVakelgaLGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAGITGLGPFSELSDEDWER 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  101 MLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVE 180
Cdd:pfam00106 104 VIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVD 183


                  ....
gi 498358419  181 TELL 184
Cdd:pfam00106 184 TDMT 187

PRK07825

short chain dehydrogenase; Provisional

52-216

4.16e-40

short chain dehydrogenase; Provisional

Pssm-ID: 181136 [Multi-domain] Cd Length: 273 Bit Score: 138.92 E-value: 4.16e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  52 GVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINI 131
Cdd:PRK07825  56 PLDVTDPASFAAFLDAVEADLGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNV 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 132 SSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDerikagyhdwkdqMGGV--IAP 209
Cdd:PRK07825 136 ASLAGKIPVPGMATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGG-------------AKGFknVEP 202


                 ....*..
gi 498358419 210 EVIADAV 216
Cdd:PRK07825 203 EDVAAAI 209

23BDH

TIGR02415

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...

51-218

5.49e-25

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

Pssm-ID: 131468 [Multi-domain] Cd Length: 254 Bit Score: 99.06 E-value: 5.49e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRS-GTII 129
Cdd:TIGR02415  54 YKLDVSDKDQVFSAIDQAAEKFGGFDVMVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKII 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  130 NISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL-------LSHTTDERIKAGYHDWKDQ 202
Cdd:TIGR02415 134 NAASIAGHEGNPILSAYSSTKFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPMweeideeTSEIAGKPIGEGFEEFSSE 213

                         170
                  ....*....|....*...
gi 498358419  203 --MGGVIAPEVIADAVLY 218
Cdd:TIGR02415 214 iaLGRPSEPEDVAGLVSF 231

Name

Accession

Description

Interval

E-value

YdfG

COG4221

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...

27-237

2.06e-70

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: 215.43 E-value: 2.06e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQALNL---PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLN 103
Cdd:COG4221   29 GARVVLAARRAERLEALAAelgGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMID 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 104 INVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:COG4221  109 VNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEF 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498358419 184 LSHTTDERIKAGYHDWKDqmGGVIAPEVIADAVLYAWHQPANVCVREIVLAATR 237
Cdd:COG4221  189 LDSVFDGDAEAAAAVYEG--LEPLTPEDVAEAVLFALTQPAHVNVNELVLRPTA 240

CAD_SDR_c

cd08934

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...

27-238

2.76e-51

Pssm-ID: 187639 [Multi-domain] Cd Length: 243 Bit Score: 166.94 E-value: 2.76e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQALNLPDT------LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQ 100
Cdd:cd08934   27 GAAVAIAARRVDRLEALADELEaeggkaLVLELDVTDEQQVDAAVERTVEALGRLDILVNNAGIMLLGPVEDADTTDWTR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 101 MLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVE 180
Cdd:cd08934  107 MIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPGTVD 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 181 TELLSHTTDERIKAGYHDWKDQMGGVIApEVIADAVLYAWHQPANVCVREIVLAATRQ 238
Cdd:cd08934  187 TELRDHITHTITKEAYEERISTIRKLQA-EDIAAAVRYAVTAPHHVTVNEILIRPTDQ 243

YqjQ

COG0300

Short-chain dehydrogenase [General function prediction only];

27-228

9.35e-51

Short-chain dehydrogenase [General function prediction only];

Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 165.81 E-value: 9.35e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQAL------NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQ 100
Cdd:COG0300   29 GARVVLVARDAERLEALaaelraAGARVEVVALDVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRR 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 101 MLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVE 180
Cdd:COG0300  109 VFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVD 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 498358419 181 TELLSHTTDERIKAgyhdwkdqmggVIAPEVIADAVLYAWHQPANVCV 228
Cdd:COG0300  189 TPFTARAGAPAGRP-----------LLSPEEVARAILRALERGRAEVY 225

SDR_c5

cd05346

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...

27-238

4.93e-48

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: 158.60 E-value: 4.93e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQAL------NLPDT-LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVML----LGQADVQDp 95
Cdd:cd05346   24 GAKLILTGRRAERLQELadelgaKFPVKvLPLQLDVSDRESIEAALENLPEEFRDIDILVNNAGLALgldpAQEADLED- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  96 aeWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIA 175
Cdd:cd05346  103 --WETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQFSLNLRKDLIGTGIRVTNIE 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 176 PGAVETELLS---HTTDERIKAGYHdwkdqmgGVIA--PEVIADAVLYAWHQPANVCVREIVLAATRQ 238
Cdd:cd05346  181 PGLVETEFSLvrfHGDKEKADKVYE-------GVEPltPEDIAETILWVASRPAHVNINDIEIMPVNQ 241

SDR_c

cd05233

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...

27-219

4.63e-47

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: 155.90 E-value: 4.63e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQAL-----NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQM 101
Cdd:cd05233   22 GAKVVLADRNEEALAELaaieaLGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNNAGIARPGPLEELTDEDWDRV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 102 LNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:cd05233  102 LDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDT 181

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 498358419 182 ELLSHTTDERIKAGYHDWKDqMGGVIAPEVIADAVLYA 219
Cdd:cd05233  182 PMLAKLGPEEAEKELAAAIP-LGRLGTPEEVAEAVVFL 218

17beta-HSD-like_SDR_c

cd05374

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...

34-219

3.92e-45

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: 151.23 E-value: 3.92e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  34 ARRVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGV 113
Cdd:cd05374   34 PDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVT 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 114 HAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD---- 189
Cdd:cd05374  114 RAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGsale 193

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 498358419 190 ERIKAGYH-------DWKDQMGGVIA-PEVIADAVLYA 219
Cdd:cd05374  194 DPEISPYAperkeikENAAGVGSNPGdPEKVADVIVKA 231

adh_short

pfam00106

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

27-184

2.54e-41

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

Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 139.67 E-value: 2.54e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   27 GHPLLLLARRVEPMQAL------NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQ 100
Cdd:pfam00106  24 GAKVVLVDRSEEKLEAVakelgaLGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAGITGLGPFSELSDEDWER 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  101 MLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVE 180
Cdd:pfam00106 104 VIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVD 183


                  ....
gi 498358419  181 TELL 184
Cdd:pfam00106 184 TDMT 187

FabG

COG1028

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...

46-218

3.06e-41

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

Pssm-ID: 440651 [Multi-domain] Cd Length: 249 Bit Score: 141.08 E-value: 3.06e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  46 PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRS 125
Cdd:COG1028   55 GRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 126 GTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELL-SHTTDERIKAGYHDwKDQMG 204
Cdd:COG1028  135 GRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTrALLGAEEVREALAA-RIPLG 213

                        170
                 ....*....|....
gi 498358419 205 GVIAPEVIADAVLY 218
Cdd:COG1028  214 RLGTPEEVAAAVLF 227

PRK07825

short chain dehydrogenase; Provisional

52-216

4.16e-40

short chain dehydrogenase; Provisional

Pssm-ID: 181136 [Multi-domain] Cd Length: 273 Bit Score: 138.92 E-value: 4.16e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  52 GVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINI 131
Cdd:PRK07825  56 PLDVTDPASFAAFLDAVEADLGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNV 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 132 SSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDerikagyhdwkdqMGGV--IAP 209
Cdd:PRK07825 136 ASLAGKIPVPGMATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGG-------------AKGFknVEP 202


                 ....*..
gi 498358419 210 EVIADAV 216
Cdd:PRK07825 203 EDVAAAI 209

PRK07454

SDR family oxidoreductase;

30-233

1.79e-36

SDR family oxidoreductase;

Pssm-ID: 180984 [Multi-domain] Cd Length: 241 Bit Score: 128.54 E-value: 1.79e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  30 LLLLARRVEPMQAL--NLPDT----LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLN 103
Cdd:PRK07454  33 LALVARSQDALEALaaELRSTgvkaAAYSIDLSNPEAIAPGIAELLEQFGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQ 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 104 INVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK07454 113 LNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 498358419 184 LSHTTderIKAGYHdwKDQMggvIAPEVIADAVLYAWHQPANVCVREIVL 233
Cdd:PRK07454 193 WDTET---VQADFD--RSAM---LSPEQVAQTILHLAQLPPSAVIEDLTL 234

PRK06180

short chain dehydrogenase; Provisional

27-182

9.87e-36

short chain dehydrogenase; Provisional

Pssm-ID: 180446 [Multi-domain] Cd Length: 277 Bit Score: 127.72 E-value: 9.87e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARR---VEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLN 103
Cdd:PRK06180  28 GHRVVGTVRSeaaRADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFE 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358419 104 INVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK06180 108 VNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPGSFRTD 186

PRK07326

SDR family oxidoreductase;

54-237

9.91e-36

SDR family oxidoreductase;

Pssm-ID: 235990 [Multi-domain] Cd Length: 237 Bit Score: 126.66 E-value: 9.91e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKaRRSGTIINISS 133
Cdd:PRK07326  62 DVRDEADVQRAVDAIVAAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALK-RGGGYIINISS 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 134 IAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKagyhdWKdqmggvIAPEVIA 213
Cdd:PRK07326 141 LAGTNFFAGGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPSEKDA-----WK------IQPEDIA 209

                        170       180
                 ....*....|....*....|....
gi 498358419 214 DAVLYAWHQPANVCVREIVLAATR 237
Cdd:PRK07326 210 QLVLDLLKMPPRTLPSKIEVRPSR 233

fabG

PRK05653

3-oxoacyl-ACP reductase FabG;

49-218

1.58e-34

3-oxoacyl-ACP reductase FabG;

Pssm-ID: 235546 [Multi-domain] Cd Length: 246 Bit Score: 123.73 E-value: 1.58e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:PRK05653  57 RVLVFDVSDEAAVRALIEAAVEAFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRI 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 129 INISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELlshtTDERIKAGYHDWKDQ--MGGV 206
Cdd:PRK05653 137 VNISSVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDM----TEGLPEEVKAEILKEipLGRL 212

                        170
                 ....*....|..
gi 498358419 207 IAPEVIADAVLY 218
Cdd:PRK05653 213 GQPEEVANAVAF 224

SDR_c4

cd08929

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...

27-237

3.22e-32

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: 117.22 E-value: 3.22e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLAR---RVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLN 103
Cdd:cd08929   24 GYRVGICARdeaRLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNAGVGVMKPVEELTPEEWRLVLD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 104 INVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:cd08929  104 TNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGF 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498358419 184 LSHTTDErikagyhDWKdqmggvIAPEVIADAVLYAWHQPANVCVREIVLAATR 237
Cdd:cd08929  184 AGSPEGQ-------AWK------LAPEDVAQAVLFALEMPARALVSRIELRPTR 224

fabG

PRK05557

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

47-218

1.51e-31

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

Pssm-ID: 235500 [Multi-domain] Cd Length: 248 Bit Score: 116.06 E-value: 1.51e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSG 126
Cdd:PRK05557  56 KALAVQGDVSDAESVERAVDEAKAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 127 TIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERikagyhdwKDQMGGV 206
Cdd:PRK05557 136 RIINISSVVGLMGNPGQANYAASKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDV--------KEAILAQ 207

                        170
                 ....*....|....*...
gi 498358419 207 IA------PEVIADAVLY 218
Cdd:PRK05557 208 IPlgrlgqPEEIASAVAF 225

fabG

PRK07666

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

53-236

6.53e-31

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

Pssm-ID: 236074 [Multi-domain] Cd Length: 239 Bit Score: 114.02 E-value: 6.53e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:PRK07666  63 ADVSDYEEVTAAIEQLKNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINIS 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELlshTTDERIKAGYHDwkdqmgGVIAPEVI 212
Cdd:PRK07666 143 STAGQKGAAVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDM---AVDLGLTDGNPD------KVMQPEDL 213

                        170       180
                 ....*....|....*....|....
gi 498358419 213 ADAVLYAWHQPANVCVREIVLAAT 236
Cdd:PRK07666 214 AEFIVAQLKLNKRTFIKSAGLWST 237

fabG

PRK05565

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

47-218

1.71e-30

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

Pssm-ID: 235506 [Multi-domain] Cd Length: 247 Bit Score: 113.40 E-value: 1.71e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSG 126
Cdd:PRK05565  56 DAIAVKADVSSEEDVENLVEQIVEKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 127 TIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAgyhdWKDQ--MG 204
Cdd:PRK05565 136 VIVNISSIWGLIGASCEVLYSASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEG----LAEEipLG 211

                        170
                 ....*....|....
gi 498358419 205 GVIAPEVIADAVLY 218
Cdd:PRK05565 212 RLGKPEEIAKVVLF 225

fabG

PRK12825

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

49-218

4.56e-29

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

Pssm-ID: 237218 [Multi-domain] Cd Length: 249 Bit Score: 109.57 E-value: 4.56e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:PRK12825  59 QAVQADVTDKAALEAAVAAAVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRI 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 129 INISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAgYHDWKdQMGGVIA 208
Cdd:PRK12825 139 VNISSVAGLPGWPGRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREA-KDAET-PLGRSGT 216

                        170
                 ....*....|
gi 498358419 209 PEVIADAVLY 218
Cdd:PRK12825 217 PEDIARAVAF 226

SDR_c3

cd05360

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...

54-225

9.08e-29

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: 108.24 E-value: 9.08e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS 133
Cdd:cd05360   57 DVADAAQVERAADTAVERFGRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGS 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 134 IAGRKTFPNHAAYCATKFAVHALTENIREEVADVG--VRMVTIAPGAVETELLSHTtderikAGYHDWKDQ-MGGVIAPE 210
Cdd:cd05360  137 LLGYRSAPLQAAYSASKHAVRGFTESLRAELAHDGapISVTLVQPTAMNTPFFGHA------RSYMGKKPKpPPPIYQPE 210

                        170
                 ....*....|....*
gi 498358419 211 VIADAVLYAWHQPAN 225
Cdd:cd05360  211 RVAEAIVRAAEHPRR 225

PRK07024

SDR family oxidoreductase;

27-186

1.24e-28

SDR family oxidoreductase;

Pssm-ID: 235910 [Multi-domain] Cd Length: 257 Bit Score: 108.48 E-value: 1.24e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQAL-----NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGV---MLLGQADvqDPAEW 98
Cdd:PRK07024  26 GATLGLVARRTDALQAFaarlpKAARVSVYAADVRDADALAAAAADFIAAHGLPDVVIANAGIsvgTLTEERE--DLAVF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  99 QQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGA 178
Cdd:PRK07024 104 REVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGY 183


                 ....*...
gi 498358419 179 VETELLSH 186
Cdd:PRK07024 184 IRTPMTAH 191

PRK06182

short chain dehydrogenase; Validated

34-219

2.50e-28

short chain dehydrogenase; Validated

Pssm-ID: 180448 [Multi-domain] Cd Length: 273 Bit Score: 108.12 E-value: 2.50e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  34 ARRVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGV 113
Cdd:PRK06182  34 ARRVDKMEDLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLT 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 114 HAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD---E 190
Cdd:PRK06182 114 QLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEWGDIAADhllK 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 498358419 191 RIKAG-YHDWKDQMGGVIA----------PEVIADAVLYA 219
Cdd:PRK06182 194 TSGNGaYAEQAQAVAASMRstygsgrlsdPSVIADAISKA 233

PRK06179

short chain dehydrogenase; Provisional

53-219

3.29e-28

short chain dehydrogenase; Provisional

Pssm-ID: 235725 [Multi-domain] Cd Length: 270 Bit Score: 107.68 E-value: 3.29e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:PRK06179  52 LDVTDDASVQAAVDEVIARAGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINIS 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHT--TDERIKAgYHD--------WKDQ 202
Cdd:PRK06179 132 SVLGFLPAPYMALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDANApePDSPLAE-YDReravvskaVAKA 210

                        170
                 ....*....|....*..
gi 498358419 203 MGGVIAPEVIADAVLYA 219
Cdd:PRK06179 211 VKKADAPEVVADTVVKA 227

SDR_c6

cd05350

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...

27-183

4.65e-28

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: 106.65 E-value: 4.65e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQAL-NLPDTLCIGV-----DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQ 100
Cdd:cd05350   22 GYNVALAARRTDRLDELkAELLNPNPSVeveilDVTDEERNQLVIAELEAELGGLDLVIINAGVGKGTSLGDLSFKAFRE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 101 MLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVE 180
Cdd:cd05350  102 TIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAESLRYDVKKRGIRVTVINPGFID 181


                 ...
gi 498358419 181 TEL 183
Cdd:cd05350  182 TPL 184

PRK09072

SDR family oxidoreductase;

30-219

9.77e-28

SDR family oxidoreductase;

Pssm-ID: 236372 [Multi-domain] Cd Length: 263 Bit Score: 106.56 E-value: 9.77e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  30 LLLLARRVEPMQAL----NLPDTLC-IGVDVTDTAAMKAAVAQAEaQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNI 104
Cdd:PRK09072  32 LLLVGRNAEKLEALaarlPYPGRHRwVVADLTSEAGREAVLARAR-EMGGINVLINNAGVNHFALLEDQDPEAIERLLAL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 105 NVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELL 184
Cdd:PRK09072 111 NLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAMN 190

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 498358419 185 SHTTDErikagyhdWKDQMG-GVIAPEVIADAVLYA 219
Cdd:PRK09072 191 SEAVQA--------LNRALGnAMDDPEDVAAAVLQA 218

HetN_like_SDR_c

cd08932

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...

27-225

1.16e-27

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: 105.14 E-value: 1.16e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQALNL--PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNI 104
Cdd:cd08932   24 GYRVSLGLRNPEDLAALSAsgGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHNAGIGRPTTLREGSDAELEAHFSI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 105 NVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELL 184
Cdd:cd08932  104 NVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPMA 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 498358419 185 SHTTDerikagyhDWKDQMGGVIAPEVIADAVLYAWHQPAN 225
Cdd:cd08932  184 QGLTL--------VGAFPPEEMIQPKDIANLVRMVIELPEN 216

adh_short_C2

pfam13561

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

33-218

1.54e-27

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: 105.21 E-value: 1.54e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   33 LARRVEPMQALnLPDTLcIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADV--QDPAEWQQMLNINVMGVL 110
Cdd:pfam13561  32 LAKRVEELAEE-LGAAV-LPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFAPKLKGPFldTSREDFDRALDVNLYSLF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  111 NGVHAVLAGMKarRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDE 190
Cdd:pfam13561 110 LLAKAALPLMK--EGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLAASGIPGF 187

                         170       180       190
                  ....*....|....*....|....*....|
gi 498358419  191 RikAGYHDWKDQ--MGGVIAPEVIADAVLY 218
Cdd:pfam13561 188 D--ELLAAAEARapLGRLGTPEEVANAAAF 215

meso-BDH-like_SDR_c

cd05366

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...

51-195

1.56e-27

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: 105.92 E-value: 1.56e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGM-KARRSGTII 129
Cdd:cd05366   57 VGADVTDKDDVEALIDQAVEKFGSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFkKLGHGGKII 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498358419 130 NISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAG 195
Cdd:cd05366  137 NASSIAGVQGFPNLGAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGEIA 202

Mgc4172-like_SDR_c

cd05343

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...

2-236

5.29e-27

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: 104.13 E-value: 5.29e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   2 SKSLVVITGASAGIGAAIARAFSAAGHPLLLLARRVEPMQAL-------NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGP 74
Cdd:cd05343    5 RGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALaaecqsaGYPTLFPYQCDLSNEEQILSMFSAIRTQHQG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  75 VGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARR--SGTIINISSIAGRKTFPNHAA--YCATK 150
Cdd:cd05343   85 VDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSMSGHRVPPVSVFhfYAATK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 151 FAVHALTENIREEV--ADVGVRMVTIAPGAVETELLSHTTD---ERIKAGYHDWKdqmggVIAPEVIADAVLYAWHQPAN 225
Cdd:cd05343  165 HAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDndpEKAAATYESIP-----CLKPEDVANAVLYVLSTPPH 239

                        250
                 ....*....|.
gi 498358419 226 VCVREIVLAAT 236
Cdd:cd05343  240 VQIHDILLRPT 250

3beta-17beta-HSD_like_SDR_c

cd05341

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...

54-218

5.96e-27

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: 104.00 E-value: 5.96e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS 133
Cdd:cd05341   59 DVTDEDGWTAVVDTAREAFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSS 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 134 IAGRKTFPNHAAYCATKFAVHALTENIREEVA--DVGVRMVTIAPGAVETELLSHTTDEriKAGYHDWKDQ-MGGVIAPE 210
Cdd:cd05341  139 IEGLVGDPALAAYNASKGAVRGLTKSAALECAtqGYGIRVNSVHPGYIYTPMTDELLIA--QGEMGNYPNTpMGRAGEPD 216


                 ....*...
gi 498358419 211 VIADAVLY 218
Cdd:cd05341  217 EIAYAVVY 224

PRK07109

short chain dehydrogenase; Provisional

53-223

1.76e-26

short chain dehydrogenase; Provisional

Pssm-ID: 235935 [Multi-domain] Cd Length: 334 Bit Score: 104.62 E-value: 1.76e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:PRK07109  64 ADVADAEAVQAAADRAEEELGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVG 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEV--ADVGVRMVTIAPGAVETELLSHTtderikAGYHDWKDQ-MGGVIAP 209
Cdd:PRK07109 144 SALAYRSIPLQSAYCAAKHAIRGFTDSLRCELlhDGSPVSVTMVQPPAVNTPQFDWA------RSRLPVEPQpVPPIYQP 217

                        170
                 ....*....|....
gi 498358419 210 EVIADAVLYAWHQP 223
Cdd:PRK07109 218 EVVADAILYAAEHP 231

KDSR-like_SDR_c

cd08939

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...

49-182

7.54e-26

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: 100.79 E-value: 7.54e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:cd08939   57 SYISADLSDYEEVEQAFAQAVEKGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHI 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498358419 129 INISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:cd08939  137 VFVSSQAALVGIYGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTP 190

PRK08263

short chain dehydrogenase; Provisional

34-217

1.07e-25

short chain dehydrogenase; Provisional

Pssm-ID: 181334 [Multi-domain] Cd Length: 275 Bit Score: 101.27 E-value: 1.07e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  34 ARRVEPMQALN--LPDTLC-IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVL 110
Cdd:PRK08263  34 ARDTATLADLAekYGDRLLpLALDVTDRAAVFAAVETAVEHFGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGAL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 111 NGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL--LSHTT 188
Cdd:PRK08263 114 WVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWagTSAKR 193

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 498358419 189 DERIKAgYHDWKDQMG-------GVIAPEVIADAVL 217
Cdd:PRK08263 194 ATPLDA-YDTLREELAeqwsersVDGDPEAAAEALL 228

11beta-HSD1_like_SDR_c

cd05332

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...

27-240

1.92e-25

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: 100.35 E-value: 1.92e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQA-----LNLPDTLCIGV--DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQ 99
Cdd:cd05332   27 GARLVLSARREERLEEvksecLELGAPSPHVVplDMSDLEDAEQVVEEALKLFGGLDILINNAGISMRSLFHDTSIDVDR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 100 QMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAV 179
Cdd:cd05332  107 KIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLI 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 180 ETELLSHTTDERIKAGYHDWKDQMGGViapeviadavlyawhqPANVCVREIVLAATRQQP 240
Cdd:cd05332  187 DTNIAMNALSGDGSMSAKMDDTTANGM----------------SPEECALEILKAIALRKR 231

PRK07775

SDR family oxidoreductase;

27-223

3.17e-25

SDR family oxidoreductase;

Pssm-ID: 181113 [Multi-domain] Cd Length: 274 Bit Score: 100.21 E-value: 3.17e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQAL------NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQ 100
Cdd:PRK07775  34 GFPVALGARRVEKCEELvdkiraDGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLVSGAGDTYFGKLHEISTEQFES 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 101 MLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVE 180
Cdd:PRK07775 114 QVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTL 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 498358419 181 TELLSHTTDERIKAGYHDWKD----QMGGVIAPEVIADAVLYAWHQP 223
Cdd:PRK07775 194 TGMGWSLPAEVIGPMLEDWAKwgqaRHDYFLRASDLARAITFVAETP 240

PRK08220

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

50-218

5.07e-25

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

Pssm-ID: 236190 [Multi-domain] Cd Length: 252 Bit Score: 98.80 E-value: 5.07e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  50 CIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTII 129
Cdd:PRK08220  52 TFVLDVSDAAAVAQVCQRLLAETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIV 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 130 NISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSH--TTDERIKAGYHDWKDQ--MG- 204
Cdd:PRK08220 132 TVGSNAAHVPRIGMAAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTlwVDEDGEQQVIAGFPEQfkLGi 211

                        170
                 ....*....|....*..
gi 498358419 205 --GVIA-PEVIADAVLY 218
Cdd:PRK08220 212 plGKIArPQEIANAVLF 228

PRK12824

3-oxoacyl-ACP reductase;

54-218

5.22e-25

3-oxoacyl-ACP reductase;

Pssm-ID: 183773 [Multi-domain] Cd Length: 245 Bit Score: 98.68 E-value: 5.22e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS 133
Cdd:PRK12824  60 DVTDTEECAEALAEIEEEEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 134 IAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDErIKAGYhdwKDQ--MGGVIAPEV 211
Cdd:PRK12824 140 VNGLKGQFGQTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQMGPE-VLQSI---VNQipMKRLGTPEE 215


                 ....*..
gi 498358419 212 IADAVLY 218
Cdd:PRK12824 216 IAAAVAF 222

23BDH

TIGR02415

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...

51-218

5.49e-25

Pssm-ID: 131468 [Multi-domain] Cd Length: 254 Bit Score: 99.06 E-value: 5.49e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRS-GTII 129
Cdd:TIGR02415  54 YKLDVSDKDQVFSAIDQAAEKFGGFDVMVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKII 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  130 NISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL-------LSHTTDERIKAGYHDWKDQ 202
Cdd:TIGR02415 134 NAASIAGHEGNPILSAYSSTKFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPMweeideeTSEIAGKPIGEGFEEFSSE 213

                         170
                  ....*....|....*...
gi 498358419  203 --MGGVIAPEVIADAVLY 218
Cdd:TIGR02415 214 iaLGRPSEPEDVAGLVSF 231

PRK06914

SDR family oxidoreductase;

42-181

7.70e-25

SDR family oxidoreductase;

Pssm-ID: 180744 [Multi-domain] Cd Length: 280 Bit Score: 98.94 E-value: 7.70e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  42 ALNLPDTLCI-GVDVTDTAAMKAAVAQaEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGM 120
Cdd:PRK06914  49 QLNLQQNIKVqQLDVTDQNSIHNFQLV-LKEIGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYM 127

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 121 KARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK06914 128 RKQKSGKIINISSISGRVGFPGLSPYVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNT 188

BKR_SDR_c

cd05333

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...

47-218

1.41e-24

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: 97.62 E-value: 1.41e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGV----MLLGQadvqDPAEWQQMLNINVMGVLNGVHAVLAGMKA 122
Cdd:cd05333   50 NAAALEADVSDREAVEALVEKVEAEFGPVDILVNNAGItrdnLLMRM----SEEDWDAVINVNLTGVFNVTQAVIRAMIK 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 123 RRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAgyhdWKDQ 202
Cdd:cd05333  126 RRSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEK----ILKQ 201

                        170
                 ....*....|....*...
gi 498358419 203 --MGGVIAPEVIADAVLY 218
Cdd:cd05333  202 ipLGRLGTPEEVANAVAF 219

PRK12826

SDR family oxidoreductase;

53-218

2.14e-24

SDR family oxidoreductase;

Pssm-ID: 183775 [Multi-domain] Cd Length: 251 Bit Score: 97.29 E-value: 2.14e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:PRK12826  62 VDVRDRAALKAAVAAGVEDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTS 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 133 SIAGRKT-FPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAGYHdwKDQ-MGGVIAPE 210
Cdd:PRK12826 142 SVAGPRVgYPGLAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEAIA--AAIpLGRLGEPE 219


                 ....*...
gi 498358419 211 VIADAVLY 218
Cdd:PRK12826 220 DIAAAVLF 227

DH-DHB-DH_SDR_c

cd05331

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...

54-218

3.30e-24

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: 96.77 E-value: 3.30e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS 133
Cdd:cd05331   48 DVADAAAVREVCSRLLAEHGPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVAS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 134 IAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELL------SHTTDERIKAGYHDWKdqMG--- 204
Cdd:cd05331  128 NAAHVPRISMAAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQrtlwhdEDGAAQVIAGVPEQFR--LGipl 205

                        170
                 ....*....|....*
gi 498358419 205 GVIA-PEVIADAVLY 218
Cdd:cd05331  206 GKIAqPADIANAVLF 220

FabG-like

PRK07231

SDR family oxidoreductase;

51-218

5.25e-24

SDR family oxidoreductase;

Pssm-ID: 235975 [Multi-domain] Cd Length: 251 Bit Score: 96.05 E-value: 5.25e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQ--ADVqDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:PRK07231  58 VAADVSDEADVEAAVAAALERFGSVDILVNNAGTTHRNGplLDV-DEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAI 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 129 INISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSH----TTDER---IKAGYhdwkd 201
Cdd:PRK07231 137 VNVASTAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAfmgePTPENrakFLATI----- 211

                        170
                 ....*....|....*..
gi 498358419 202 QMGGVIAPEVIADAVLY 218
Cdd:PRK07231 212 PLGRLGTPEDIANAALF 228

SDR_c9

cd08931

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...

53-223

1.63e-23

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: 94.44 E-value: 1.63e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVaqaeAQFGP-----VGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGT 127
Cdd:cd08931   54 LDVTDRAAWAAAL----ADFAAatggrLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGAR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 128 IINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERikagyhDWKDQMGGVI 207
Cdd:cd08931  130 VINTASSSAIYGQPDLAVYSATKFAVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGA------APKKGLGRVL 203

                        170
                 ....*....|....*.
gi 498358419 208 APEVIADAVLYAWHQP 223
Cdd:cd08931  204 PVSDVAKVVWAAAHGV 219

PRK08267

SDR family oxidoreductase;

78-226

2.36e-23

SDR family oxidoreductase;

Pssm-ID: 236210 [Multi-domain] Cd Length: 260 Bit Score: 94.62 E-value: 2.36e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALT 157
Cdd:PRK08267  81 LFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLT 160

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 158 ENIREEVADVGVRMVTIAPGAVETELLSHTTDErIKAGyhdwKDQMGGV-IAPEVIADAVLYAWHQPANV 226
Cdd:PRK08267 161 EALDLEWRRHGIRVADVMPLFVDTAMLDGTSNE-VDAG----STKRLGVrLTPEDVAEAVWAAVQHPTRL 225

17beta-HSD1_like_SDR_c

cd05356

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...

74-183

2.58e-23

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: 94.21 E-value: 2.58e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  74 PVGCLVNNAGVML-LGQADVQ-DPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKF 151
Cdd:cd05356   78 DIGILVNNVGISHsIPEYFLEtPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKA 157

                         90       100       110
                 ....*....|....*....|....*....|..
gi 498358419 152 AVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:cd05356  158 FLDFFSRALYEEYKSQGIDVQSLLPYLVATKM 189

PRK07832

SDR family oxidoreductase;

53-219

2.64e-23

SDR family oxidoreductase;

Pssm-ID: 181139 [Multi-domain] Cd Length: 272 Bit Score: 94.72 E-value: 2.64e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGM-KARRSGTIINI 131
Cdd:PRK07832  57 LDISDYDAVAAFAADIHAAHGSMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMvAAGRGGHLVNV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 132 SSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLS-------HTTDERIKAgyhdWKDQMG 204
Cdd:PRK07832 137 SSAAGLVALPWHAAYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNtveiagvDREDPRVQK----WVDRFR 212

                        170
                 ....*....|....*.
gi 498358419 205 GV-IAPEVIADAVLYA 219
Cdd:PRK07832 213 GHaVTPEKAAEKILAG 228

Ga5DH-like_SDR_c

cd05347

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...

53-187

3.31e-23

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: 93.96 E-value: 3.31e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:cd05347   61 CDVSDEEAIKAAVEAIEEDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINIC 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHT 187
Cdd:cd05347  141 SLLSELGGPPVPAYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAV 195

PRK12829

short chain dehydrogenase; Provisional

45-218

3.81e-23

short chain dehydrogenase; Provisional

Pssm-ID: 183778 [Multi-domain] Cd Length: 264 Bit Score: 94.35 E-value: 3.81e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  45 LPDTLCIGV--DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLL--GQADVqDPAEWQQMLNINVMGVLNGVHAVLAGM 120
Cdd:PRK12829  55 LPGAKVTATvaDVADPAQVERVFDTAVERFGGLDVLVNNAGIAGPtgGIDEI-TPEQWEQTLAVNLNGQFYFARAAVPLL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 121 KARRSG-TIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKA---GY 196
Cdd:PRK12829 134 KASGHGgVIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQlgiGL 213

                        170       180
                 ....*....|....*....|....*...
gi 498358419 197 HDWKDQ------MGGVIAPEVIADAVLY 218
Cdd:PRK12829 214 DEMEQEylekisLGRMVEPEDIAATALF 241

PRK06841

short chain dehydrogenase; Provisional

41-218

4.09e-23

short chain dehydrogenase; Provisional

Pssm-ID: 180723 [Multi-domain] Cd Length: 255 Bit Score: 93.95 E-value: 4.09e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  41 QALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGM 120
Cdd:PRK06841  56 AQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHM 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 121 KARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELlshttderikaGYHDWK 200
Cdd:PRK06841 136 IAAGGGKIVNLASQAGVVALERHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTEL-----------GKKAWA 204

                        170       180
                 ....*....|....*....|....*...
gi 498358419 201 DQMG---------GVIA-PEVIADAVLY 218
Cdd:PRK06841 205 GEKGerakklipaGRFAyPEEIAAAALF 232

fabG

PRK06463

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

51-218

6.24e-23

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

Pssm-ID: 180576 [Multi-domain] Cd Length: 255 Bit Score: 93.69 E-value: 6.24e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIIN 130
Cdd:PRK06463  56 IKCDVGNRDQVKKSKEVVEKEFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVN 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 131 ISSIAGRKTFP-NHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL-LSHTTDERIKAGYHDWKDQ----MG 204
Cdd:PRK06463 136 IASNAGIGTAAeGTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMtLSGKSQEEAEKLRELFRNKtvlkTT 215

                        170
                 ....*....|....
gi 498358419 205 GViaPEVIADAVLY 218
Cdd:PRK06463 216 GK--PEDIANIVLF 227

PRK12828

short chain dehydrogenase; Provisional

52-182

8.14e-23

short chain dehydrogenase; Provisional

Pssm-ID: 237220 [Multi-domain] Cd Length: 239 Bit Score: 92.94 E-value: 8.14e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  52 GVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINI 131
Cdd:PRK12828  60 GIDLVDPQAARRAVDEVNRQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNI 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 498358419 132 SSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK12828 140 GAGAALKAGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTP 190

PRK06181

SDR family oxidoreductase;

30-219

1.85e-22

SDR family oxidoreductase;

Pssm-ID: 235726 [Multi-domain] Cd Length: 263 Bit Score: 92.35 E-value: 1.85e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  30 LLLLARRVEPMQALNL------PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGV-MLLGQADVQDPAEWQQML 102
Cdd:PRK06181  28 LVLAARNETRLASLAQeladhgGEALVVPTDVSDAEACERLIEAAVARFGGIDILVNNAGItMWSRFDELTDLSVFERVM 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 103 NINVMGVLNGVHAVLAGMKARRsGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK06181 108 RVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGYAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATD 186

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 498358419 183 LLSHTTDERIKAgYHDWKDQMGGVIAPEVIADAVLYA 219
Cdd:PRK06181 187 IRKRALDGDGKP-LGKSPMQESKIMSAEECAEAILPA 222

GlcDH_SDR_c

cd05358

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...

49-220

2.80e-22

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: 91.68 E-value: 2.80e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVmllgQADV----QDPAEWQQMLNINVMGV-LNGVHAVLAGMKAR 123
Cdd:cd05358   56 IAVQADVSKEEDVVALFQSAIKEFGTLDILVNNAGL----QGDAssheMTLEDWNKVIDVNLTGQfLCAREAIKRFRKSK 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 124 RSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAGYHDWKDQM 203
Cdd:cd05358  132 IKGKIINMSSVHEKIPWPGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSLIPM 211

                        170
                 ....*....|....*..
gi 498358419 204 GGVIAPEVIADAVlyAW 220
Cdd:cd05358  212 GRIGEPEEIAAAA--AW 226

SDR_c11

cd05364

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...

49-218

4.38e-22

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: 91.32 E-value: 4.38e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRsGTI 128
Cdd:cd05364   58 LLVVADLTEEEGQDRIISTTLAKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEI 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 129 INISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHT--TDERIKAGYHDWKD--QMG 204
Cdd:cd05364  137 VNVSSVAGGRSFPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMgmPEEQYIKFLSRAKEthPLG 216

                        170
                 ....*....|....
gi 498358419 205 GVIAPEVIADAVLY 218
Cdd:cd05364  217 RPGTVDEVAEAIAF 230

SDR_c12

cd08944

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...

49-218

7.68e-22

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: 90.24 E-value: 7.68e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAE-WQQMLNINVMGVLNGVHAVLAGMKARRSGT 127
Cdd:cd08944   52 LALRVDVTDEQQVAALFERAVEEFGGLDLLVNNAGAMHLTPAIIDTDLAvWDQTMAINLRGTFLCCRHAAPRMIARGGGS 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 128 IINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKA----GYHDWKDQM 203
Cdd:cd08944  132 IVNLSSIAGQSGDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEGAlgpgGFHLLIHQL 211

                        170
                 ....*....|....*.
gi 498358419 204 GG-VIAPEVIADAVLY 218
Cdd:cd08944  212 QGrLGRPEDVAAAVVF 227

PRK07063

SDR family oxidoreductase;

47-183

1.08e-21

SDR family oxidoreductase;

Pssm-ID: 235924 [Multi-domain] Cd Length: 260 Bit Score: 90.11 E-value: 1.08e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSG 126
Cdd:PRK07063  59 RVLAVPADVTDAASVAAAVAAAEEAFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRG 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498358419 127 TIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK07063 139 SIVNIASTHAFKIIPGCFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQL 195

PRK12937

short chain dehydrogenase; Provisional

54-218

1.10e-21

short chain dehydrogenase; Provisional

Pssm-ID: 171821 [Multi-domain] Cd Length: 245 Bit Score: 89.80 E-value: 1.10e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMkaRRSGTIINISS 133
Cdd:PRK12937  63 DVADAAAVTRLFDAAETAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLST 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 134 IAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDErikagyhDWKDQMGGVIA----- 208
Cdd:PRK12937 141 SVIALPLPGYGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATELFFNGKSA-------EQIDQLAGLAPlerlg 213

                        170
                 ....*....|.
gi 498358419 209 -PEVIADAVLY 218
Cdd:PRK12937 214 tPEEIAAAVAF 224

PRK08219

SDR family oxidoreductase;

28-233

1.32e-21

SDR family oxidoreductase;

Pssm-ID: 181298 [Multi-domain] Cd Length: 227 Bit Score: 89.22 E-value: 1.32e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  28 HPLLLLARRVEPMQAL--NLPDTLCIGVDVTDTAAMKAAVaqaeAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNIN 105
Cdd:PRK08219  27 HTLLLGGRPAERLDELaaELPGATPFPVDLTDPEAIAAAV----EQLGRLDVLVHNAGVADLGPVAESTVDEWRATLEVN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 106 VMGVLNGVHAVLAGMKARRsGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVgVRMVTIAPGAVETELLs 185
Cdd:PRK08219 103 VVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAASKFALRALADALREEEPGN-VRVTSVHPGRTDTDMQ- 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498358419 186 httdERIKAgyhdwkdQMGG------VIAPEVIADAVLYAWHQPANVCVREIVL 233
Cdd:PRK08219 180 ----RGLVA-------QEGGeydperYLRPETVAKAVRFAVDAPPDAHITEVVV 222

ADH_SDR_c_like

cd05323

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...

53-219

1.33e-21

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: 89.67 E-value: 1.33e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVM--LLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKAR---RSGT 127
Cdd:cd05323   56 CDVTSWEQLAAAFKKAIEKFGRVDILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNkggKGGV 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 128 IINISSIAGRKTFPNHAAYCATKFAVHALTENIR-EEVADVGVRMVTIAPGAVETELLSHTTDERIKAGyhdwkdQMGGV 206
Cdd:cd05323  136 IVNIGSVAGLYPAPQFPVYSASKHGVVGFTRSLAdLLEYKTGVRVNAICPGFTNTPLLPDLVAKEAEML------PSAPT 209

                        170
                 ....*....|...
gi 498358419 207 IAPEVIADAVLYA 219
Cdd:cd05323  210 QSPEVVAKAIVYL 222

PRK12429

3-hydroxybutyrate dehydrogenase; Provisional

51-194

1.55e-21

3-hydroxybutyrate dehydrogenase; Provisional

Pssm-ID: 237100 [Multi-domain] Cd Length: 258 Bit Score: 89.95 E-value: 1.55e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLgqADVQD--PAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:PRK12429  58 VAMDVTDEEAINAGIDYAVETFGGVDILVNNAGIQHV--APIEDfpTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRI 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498358419 129 INISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKA 194
Cdd:PRK12429 136 INMASVHGLVGSAGKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPLVRKQIPDLAKE 201

PRK05650

SDR family oxidoreductase;

53-216

1.80e-21

SDR family oxidoreductase;

Pssm-ID: 235545 [Multi-domain] Cd Length: 270 Bit Score: 89.71 E-value: 1.80e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:PRK05650  56 CDVRDYSQLTALAQACEEKWGGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIA 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLS--HTTDERIKAgyhdwkdQMGGV---- 206
Cdd:PRK05650 136 SMAGLMQGPAMSSYNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNLLDsfRGPNPAMKA-------QVGKLleks 208

                        170
                 ....*....|.
gi 498358419 207 -IAPEVIADAV 216
Cdd:PRK05650 209 pITAADIADYI 219

PRK08264

SDR family oxidoreductase;

70-219

3.72e-21

SDR family oxidoreductase;

Pssm-ID: 181335 [Multi-domain] Cd Length: 238 Bit Score: 88.41 E-value: 3.72e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  70 AQFGPVGCLVNNAGVMLLGQA-DVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCA 148
Cdd:PRK08264  69 EAASDVTILVNNAGIFRTGSLlLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSA 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 149 TKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHttderikagyhdwkdQMGGVIAPEVIADAVLYA 219
Cdd:PRK08264 149 SKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAAG---------------LDAPKASPADVARQILDA 204

DHRS6_like_SDR_c

cd05368

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...

53-194

3.76e-21

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

Pssm-ID: 187626 [Multi-domain] Cd Length: 241 Bit Score: 88.30 E-value: 3.76e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVaqaeAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:cd05368   53 LDVTDKEQVAALA----KEEGRIDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMS 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358419 133 SIAGR-KTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLshttDERIKA 194
Cdd:cd05368  129 SVASSiKGVPNRFVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSL----EERIQA 187

THN_reductase-like_SDR_c

cd05362

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...

49-216

3.91e-21

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

Pssm-ID: 187620 [Multi-domain] Cd Length: 243 Bit Score: 88.49 E-value: 3.91e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMkaRRSGTI 128
Cdd:cd05362   56 IAVQADVSDPSQVARLFDAAEKAFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 129 INISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAGYHDWkdQMGGVIA 208
Cdd:cd05362  134 INISSSLTAAYTPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYAKM--SPLGRLG 211


                 ....*....
gi 498358419 209 -PEVIADAV 216
Cdd:cd05362  212 ePEDIAPVV 220

SDR_c7

cd05354

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...

75-219

4.99e-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: 87.85 E-value: 4.99e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  75 VGCLVNNAGVM----LLGQADVQDPaewQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATK 150
Cdd:cd05354   75 VDVVINNAGVLkpatLLEEGALEAL---KQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASK 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358419 151 FAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTtdERIKAgyhdwkdqmggviAPEVIADAVLYA 219
Cdd:cd05354  152 SAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGA--GGPKE-------------SPETVAEAVLKA 205

PRK06171

sorbitol-6-phosphate 2-dehydrogenase; Provisional

53-196

5.39e-21

sorbitol-6-phosphate 2-dehydrogenase; Provisional

Pssm-ID: 180439 [Multi-domain] Cd Length: 266 Bit Score: 88.53 E-value: 5.39e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGV---MLLgqADVQDP--------AEWQQMLNINVMGVLNGVHAVLAGMK 121
Cdd:PRK06171  56 TDVSSAEEVNHTVAEIIEKFGRIDGLVNNAGInipRLL--VDEKDPagkyelneAAFDKMFNINQKGVFLMSQAVARQMV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 122 ARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET---------ELLS---HTTD 189
Cdd:PRK06171 134 KQHDGVIVNMSSEAGLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEAtglrtpeyeEALAytrGITV 213


                 ....*..
gi 498358419 190 ERIKAGY 196
Cdd:PRK06171 214 EQLRAGY 220

HBDH_SDR_c

cd08940

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...

47-218

5.99e-21

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

Pssm-ID: 187644 [Multi-domain] Cd Length: 258 Bit Score: 88.27 E-value: 5.99e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLgqADVQD-PAE-WQQMLNINVMGVLNGVHAVLAGMKARR 124
Cdd:cd08940   54 KVLYHGADLSKPAAIEDMVAYAQRQFGGVDILVNNAGIQHV--APIEDfPTEkWDAIIALNLSAVFHTTRLALPHMKKQG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 125 SGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAGYHDW----- 199
Cdd:cd08940  132 WGRIINIASVHGLVASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQISALAQKNGVPQeqaar 211

                        170       180
                 ....*....|....*....|....
gi 498358419 200 -----KDQMGGVIAPEVIADAVLY 218
Cdd:cd08940  212 ellleKQPSKQFVTPEQLGDTAVF 235

SDR_c2

cd05370

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...

35-185

6.25e-21

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: 87.36 E-value: 6.25e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  35 RRVEPMQAL--NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLgqADVQDPAEW----QQMLNINVMG 108
Cdd:cd05370   37 RREERLAEAkkELPNIHTIVLDVGDAESVEALAEALLSEYPNLDILINNAGIQRP--IDLRDPASDldkaDTEIDTNLIG 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358419 109 VLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLS 185
Cdd:cd05370  115 PIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHE 191

PRK06138

SDR family oxidoreductase;

53-218

1.20e-20

SDR family oxidoreductase;

Pssm-ID: 235712 [Multi-domain] Cd Length: 252 Bit Score: 87.51 E-value: 1.20e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:PRK06138  60 GDVGSAEAVEALVDFVAARWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLS-----HTTDERIKAGYhDWKDQMGGVI 207
Cdd:PRK06138 140 SQLALAGGRGRAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRrifarHADPEALREAL-RARHPMNRFG 218

                        170
                 ....*....|.
gi 498358419 208 APEVIADAVLY 218
Cdd:PRK06138 219 TAEEVAQAALF 229

BKR_3_SDR_c

cd05345

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...

32-218

2.59e-20

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

Pssm-ID: 187603 [Multi-domain] Cd Length: 248 Bit Score: 86.29 E-value: 2.59e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  32 LLARRVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQ--ADVqDPAEWQQMLNINVMGV 109
Cdd:cd05345   37 INADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDILVNNAGITHRNKpmLEV-DEEEFDRVFAVNVKSI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 110 LNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD 189
Cdd:cd05345  116 YLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMG 195

                        170       180       190
                 ....*....|....*....|....*....|.
gi 498358419 190 ERIKAGYHDWKDQ--MGGVIAPEVIADAVLY 218
Cdd:cd05345  196 EDTPENRAKFRATipLGRLSTPDDIANAALY 226

secoisolariciresinol-DH_like_SDR_c

cd05326

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...

70-218

7.19e-20

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: 85.20 E-value: 7.19e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  70 AQFGPVGCLVNNAGVMLLGQADVQD--PAEWQQMLNINVMGVLNGV-HAVLAgMKARRSGTIINISSIAGRKTFPNHAAY 146
Cdd:cd05326   75 ARFGRLDIMFNNAGVLGAPCYSILEtsLEEFERVLDVNVYGAFLGTkHAARV-MIPAKKGSIVSVASVAGVVGGLGPHAY 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358419 147 CATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTT---DERIKAGYHDWKDQMGGVIAPEVIADAVLY 218
Cdd:cd05326  154 TASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFgveDEAIEEAVRGAANLKGTALRPEDIAAAVLY 228

carb_red_PTCR-like_SDR_c

cd05324

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...

53-195

1.71e-19

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: 83.44 E-value: 1.71e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLG-QADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINI 131
Cdd:cd05324   57 LDVTDDASIEAAADFVEEKYGGLDILVNNAGIAFKGfDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNV 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358419 132 SSIAGRKTfpnhAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAG 195
Cdd:cd05324  137 SSGLGSLT----SAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAPKTPEEG 196

PRK06172

SDR family oxidoreductase;

47-218

2.08e-19

SDR family oxidoreductase;

Pssm-ID: 180440 [Multi-domain] Cd Length: 253 Bit Score: 84.03 E-value: 2.08e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVML-LGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRS 125
Cdd:PRK06172  57 EALFVACDVTRDAEVKALVEQTIAAYGRLDYAFNNAGIEIeQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 126 GTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELL--SHTTDERiKAGYHDWKDQM 203
Cdd:PRK06172 137 GAIVNTASVAGLGAAPKMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFrrAYEADPR-KAEFAAAMHPV 215

                        170
                 ....*....|....*
gi 498358419 204 GGVIAPEVIADAVLY 218
Cdd:PRK06172 216 GRIGKVEEVASAVLY 230

PRK05693

SDR family oxidoreductase;

6-190

2.32e-19

SDR family oxidoreductase;

Pssm-ID: 168186 [Multi-domain] Cd Length: 274 Bit Score: 84.46 E-value: 2.32e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   6 VVITGASAGIGAAIARAFSAAGHPLLLLARRVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVM 85
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHGGLDVLINNAGYG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  86 LLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKaRRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVA 165
Cdd:PRK05693  84 AMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLR-RSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDALRLELA 162

                        170       180
                 ....*....|....*....|....*
gi 498358419 166 DVGVRMVTIAPGAVETELLSHTTDE 190
Cdd:PRK05693 163 PFGVQVMEVQPGAIASQFASNASRE 187

PRK06484

short chain dehydrogenase; Validated

33-218

5.91e-19

short chain dehydrogenase; Validated

Pssm-ID: 168574 [Multi-domain] Cd Length: 520 Bit Score: 85.29 E-value: 5.91e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  33 LARRVEPMQALNlPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVM---LLGQADvQDPAEWQQMLNINVMGV 109
Cdd:PRK06484  39 VERARERADSLG-PDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVNNAGVTdptMTATLD-TTLEEFARLQAINLTGA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 110 LNGVHAVLAGMKARRSGT-IINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLShtt 188
Cdd:PRK06484 117 YLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVA--- 193

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 498358419 189 dERIKAGYHD-----WKDQMGGVIAPEVIADAVLY 218
Cdd:PRK06484 194 -ELERAGKLDpsavrSRIPLGRLGRPEEIAEAVFF 227

ChcA_like_SDR_c

cd05359

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...

54-219

6.06e-19

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

Pssm-ID: 187617 [Multi-domain] Cd Length: 242 Bit Score: 82.40 E-value: 6.06e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS 133
Cdd:cd05359   56 DVSQPQDVEEMFAAVKERFGRLDVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 134 IAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD-ERIKAGYHDWKdQMGGVIAPEVI 212
Cdd:cd05359  136 LGSIRALPNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNrEDLLEAAAANT-PAGRVGTPQDV 214


                 ....*..
gi 498358419 213 ADAVLYA 219
Cdd:cd05359  215 ADAVGFL 221

type1_17beta-HSD-like_SDR_c

cd09806

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...

78-182

6.33e-19

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: 82.89 E-value: 6.33e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALT 157
Cdd:cd09806   83 LVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALEGLC 162

                         90       100
                 ....*....|....*....|....*
gi 498358419 158 ENIREEVADVGVRMVTIAPGAVETE 182
Cdd:cd09806  163 ESLAVQLLPFNVHLSLIECGPVHTA 187

DltE

COG3967

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...

51-183

7.12e-19

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: 82.52 E-value: 7.12e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLG--QADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:COG3967   55 IVLDVADPASIAALAEQVTAEFPDLNVLINNAGIMRAEdlLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAI 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 498358419 129 INISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:COG3967  135 VNVSSGLAFVPLAVTPTYSATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDL 189

MDH-like_SDR_c

cd05352

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...

53-218

9.87e-19

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: 81.99 E-value: 9.87e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:cd05352   65 CDVSSQESVEKTFKQIQKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITA 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 133 SIAG-RKTFPNH-AAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHtTDERIKAGYHDwKDQMGGVIAPE 210
Cdd:cd05352  145 SMSGtIVNRPQPqAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDF-VDKELRKKWES-YIPLKRIALPE 222


                 ....*...
gi 498358419 211 VIADAVLY 218
Cdd:cd05352  223 ELVGAYLY 230

BKR_like_SDR_like

cd05344

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...

27-218

1.04e-18

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: 81.94 E-value: 1.04e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQ----ALNLPDTLCIGV--DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQ 100
Cdd:cd05344   25 GARVAICARNRENLEraasELRAGGAGVLAVvaDLTDPEDIDRLVEKAGDAFGRVDILVNNAGGPPPGPFAELTDEDWLE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 101 MLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVE 180
Cdd:cd05344  105 AFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYID 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 498358419 181 TE----LLSHTTdERIKAGYHDWKDQMGGVIA------PEVIADAVLY 218
Cdd:cd05344  185 TErvrrLLEARA-EKEGISVEEAEKEVASQIPlgrvgkPEELAALIAF 231

PRK07074

SDR family oxidoreductase;

51-182

1.35e-18

SDR family oxidoreductase;

Pssm-ID: 180823 [Multi-domain] Cd Length: 257 Bit Score: 81.74 E-value: 1.35e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIIN 130
Cdd:PRK07074  54 VACDLTDAASLAAALANAAAERGPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVN 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498358419 131 ISSIAGRKTFpNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK07074 134 IGSVNGMAAL-GHPAYSAAKAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQ 184

type2_17beta_HSD-like_SDR_c

cd09805

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...

78-193

2.12e-18

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: 81.56 E-value: 2.12e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMLLGQadvqdPAEW------QQMLNINVMGVLNGVHAVLAGMkaRRS-GTIINISSIAGRKTFPNHAAYCATK 150
Cdd:cd09805   82 LVNNAGILGFGG-----DEELlpmddyRKCMEVNLFGTVEVTKAFLPLL--RRAkGRVVNVSSMGGRVPFPAGGAYCASK 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 498358419 151 FAVHALTENIREEVADVGVRMVTIAPGAVETElLSHTTDERIK 193
Cdd:cd09805  155 AAVEAFSDSLRRELQPWGVKVSIIEPGNFKTG-ITGNSELWEK 196

HSD10-like_SDR_c

cd05371

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...

53-190

2.74e-18

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: 80.80 E-value: 2.74e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQAD------VQDPAEWQQMLNINVMGVLNGVHAVLAGMKAR--- 123
Cdd:cd05371   54 VDVTSEKDVKAALALAKAKFGRLDIVVNCAGIAVAAKTYnkkgqqPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNepd 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 124 ---RSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDE 190
Cdd:cd05371  134 qggERGVIINTASVAAFEGQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEK 203

PRK10538

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...

27-226

3.42e-18

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

Pssm-ID: 182531 [Multi-domain] Cd Length: 248 Bit Score: 80.57 E-value: 3.42e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQALN--LPDTLCIG-VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVML-LGQADVQDPAEWQQML 102
Cdd:PRK10538  24 GHKVIATGRRQERLQELKdeLGDNLYIAqLDVRNRAAIEEMLASLPAEWRNIDVLVNNAGLALgLEPAHKASVEDWETMI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 103 NINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK10538 104 DTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGT 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 498358419 183 LLSHT----TDERIKAGYHDwkdqmGGVIAPEVIADAVLYAWHQPANV 226
Cdd:PRK10538 184 EFSNVrfkgDDGKAEKTYQN-----TVALTPEDVSEAVWWVATLPAHV 226

PRK07067

L-iditol 2-dehydrogenase;

36-182

3.59e-18

L-iditol 2-dehydrogenase;

Pssm-ID: 235925 [Multi-domain] Cd Length: 257 Bit Score: 80.84 E-value: 3.59e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  36 RVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHA 115
Cdd:PRK07067  42 RARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQA 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 116 VLAGMKAR-RSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK07067 122 VARHMVEQgRGGKIINMASQAGRRGEALVSHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTP 189

PRK13394

3-hydroxybutyrate dehydrogenase; Provisional

54-193

6.35e-18

3-hydroxybutyrate dehydrogenase; Provisional

Pssm-ID: 184025 [Multi-domain] Cd Length: 262 Bit Score: 80.32 E-value: 6.35e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGM-KARRSGTIINIS 132
Cdd:PRK13394  64 DVTNEDAVNAGIDKVAERFGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMG 143

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIK 193
Cdd:PRK13394 144 SVHSHEASPLKSAYVTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIPEQAK 204

PRK08643

(S)-acetoin forming diacetyl reductase;

47-181

9.42e-18

(S)-acetoin forming diacetyl reductase;

Pssm-ID: 181518 [Multi-domain] Cd Length: 256 Bit Score: 79.38 E-value: 9.42e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKAR-RS 125
Cdd:PRK08643  52 KAIAVKADVSDRDQVFAAVRQVVDTFGDLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLgHG 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 498358419 126 GTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK08643 132 GKIINATSQAGVVGNPELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKT 187

BKR_1_SDR_c

cd05337

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...

48-217

1.04e-17

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: 79.43 E-value: 1.04e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  48 TLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAE--WQQMLNINVMGVLNGVHAVLAGM----- 120
Cdd:cd05337   53 AIYFQADIGELSDHEALLDQAWEDFGRLDCLVNNAGIAVRPRGDLLDLTEdsFDRLIAINLRGPFFLTQAVARRMveqpd 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 121 -KARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTT---DERIKAGY 196
Cdd:cd05337  133 rFDGPHRSIIFVTSINAYLVSPNRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKekyDELIAAGL 212

                        170       180
                 ....*....|....*....|.
gi 498358419 197 HDWKdQMGgviAPEVIADAVL 217
Cdd:cd05337  213 VPIR-RWG---QPEDIAKAVR 229

cyclohexanol_reductase_SDR_c

cd05330

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...

48-184

1.27e-17

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: 79.10 E-value: 1.27e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  48 TLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMllG-QADVQD--PAEWQQMLNINVMGVLNGVHAVLAGMKARR 124
Cdd:cd05330   56 VLLIKADVSDEAQVEAYVDATVEQFGRIDGFFNNAGIE--GkQNLTEDfgADEFDKVVSINLRGVFYGLEKVLKVMREQG 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 125 SGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELL 184
Cdd:cd05330  134 SGMIVNTASVGGIRGVGNQSGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMV 193

PRK05872

short chain dehydrogenase; Provisional

51-190

1.79e-17

short chain dehydrogenase; Provisional

Pssm-ID: 235633 [Multi-domain] Cd Length: 296 Bit Score: 79.24 E-value: 1.79e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRsGTIIN 130
Cdd:PRK05872  62 VVADVTDLAAMQAAAEEAVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQ 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 131 ISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRmVTIA-PGAVETELLSHTTDE 190
Cdd:PRK05872 141 VSSLAAFAAAPGMAAYCASKAGVEAFANALRLEVAHHGVT-VGSAyLSWIDTDLVRDADAD 200

PRK12939

short chain dehydrogenase; Provisional

6-219

2.73e-17

short chain dehydrogenase; Provisional

Pssm-ID: 183833 [Multi-domain] Cd Length: 250 Bit Score: 78.09 E-value: 2.73e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   6 VVITGASAGIGAAIARAFSAAGHPLLL----------LARRVEPMQAlnlpDTLCIGVDVTDTAAMKAAVAQAEAQFGPV 75
Cdd:PRK12939  10 ALVTGAARGLGAAFAEALAEAGATVAFndglaaeareLAAALEAAGG----RAHAIAADLADPASVQRFFDAAAAALGGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  76 GCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHA 155
Cdd:PRK12939  86 DGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIG 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358419 156 LTENIREEVADVGVRMVTIAPGAVETEL-LSHTTDERIkAGYHDwKDQMGGVIAPEVIADAVLYA 219
Cdd:PRK12939 166 MTRSLARELGGRGITVNAIAPGLTATEAtAYVPADERH-AYYLK-GRALERLQVPDDVAGAVLFL 228

PRK07060

short chain dehydrogenase; Provisional

51-183

2.75e-17

short chain dehydrogenase; Provisional

Pssm-ID: 180817 [Multi-domain] Cd Length: 245 Bit Score: 78.22 E-value: 2.75e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVaqaeAQFGPVGCLVNNAGVMLLGQA-DVQDpAEWQQMLNINVMGVLNGVHAVLAGM-KARRSGTI 128
Cdd:PRK07060  58 LRLDVGDDAAIRAAL----AAAGAFDGLVNCAGIASLESAlDMTA-EGFDRVMAVNARGAALVARHVARAMiAAGRGGSI 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 498358419 129 INISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK07060 133 VNVSSQAALVGLPDHLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187

PRK07069

short chain dehydrogenase; Validated

54-218

2.84e-17

short chain dehydrogenase; Validated

Pssm-ID: 180822 [Multi-domain] Cd Length: 251 Bit Score: 78.21 E-value: 2.84e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS 133
Cdd:PRK07069  59 DVTDEAQWQALLAQAADAMGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISS 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 134 IAGRKTFPNHAAYCATKFAVHALTENIREEVA--DVGVRMVTIAPGAVET---ELLSHTTDERIKAGYHDWKDQMGGVIA 208
Cdd:PRK07069 139 VAAFKAEPDYTAYNASKAAVASLTKSIALDCArrGLDVRCNSIHPTFIRTgivDPIFQRLGEEEATRKLARGVPLGRLGE 218

                        170
                 ....*....|
gi 498358419 209 PEVIADAVLY 218
Cdd:PRK07069 219 PDDVAHAVLY 228

PRK06484

short chain dehydrogenase; Validated

27-181

2.90e-17

short chain dehydrogenase; Validated

Pssm-ID: 168574 [Multi-domain] Cd Length: 520 Bit Score: 80.28 E-value: 2.90e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQALN--LPDT-LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGV--MLLGQADvQDPAEWQQM 101
Cdd:PRK06484 293 GDRLLIIDRDAEGAKKLAeaLGDEhLSVQADITDEAAVESAFAQIQARWGRLDVLVNNAGIaeVFKPSLE-QSAEDFTRV 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 102 LNINVMGVLNGVHAVLAGMkaRRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK06484 372 YDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449

SPR-like_SDR_c

cd05367

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...

30-213

3.69e-17

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

Pssm-ID: 187625 [Multi-domain] Cd Length: 241 Bit Score: 77.71 E-value: 3.69e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  30 LLLLARRVEPMQALNLPDT-----LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVML-LGQADVQDPAEWQQMLN 103
Cdd:cd05367   28 VVLLARSEEPLQELKEELRpglrvTTVKADLSDAAGVEQLLEAIRKLDGERDLLINNAGSLGpVSKIEFIDLDELQKYFD 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 104 INVMGVLNGVHAVLAGMKARRS-GTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEvaDVGVRMVTIAPGAVET- 181
Cdd:cd05367  108 LNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAARDMFFRVLAAE--EPDVRVLSYAPGVVDTd 185

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 498358419 182 ---ELLSHTTDERIKAGYHDWKDQmGGVIAPEVIA 213
Cdd:cd05367  186 mqrEIRETSADPETRSRFRSLKEK-GELLDPEQSA 219

PRK09291

SDR family oxidoreductase;

78-181

4.07e-17

SDR family oxidoreductase;

Pssm-ID: 181762 [Multi-domain] Cd Length: 257 Bit Score: 77.73 E-value: 4.07e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMLLGqADVQDPAEW-QQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHAL 156
Cdd:PRK09291  77 LLNNAGIGEAG-AVVDIPVELvRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEAI 155

                         90       100
                 ....*....|....*....|....*
gi 498358419 157 TENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK09291 156 AEAMHAELKPFGIQVATVNPGPYLT 180

fabG

PRK08217

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

47-183

4.27e-17

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

Pssm-ID: 181297 [Multi-domain] Cd Length: 253 Bit Score: 77.69 E-value: 4.27e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGV----MLLGQAD--VQDP---AEWQQMLNINVMGV-LNGVHAV 116
Cdd:PRK08217  55 EVRGYAANVTDEEDVEATFAQIAEDFGQLNGLINNAGIlrdgLLVKAKDgkVTSKmslEQFQSVIDVNLTGVfLCGREAA 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358419 117 LAGMKARRSGTIINISSIAgRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK08217 135 AKMIESGSKGVIINISSIA-RAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEM 200

PRK06398

aldose dehydrogenase; Validated

51-218

4.91e-17

aldose dehydrogenase; Validated

Pssm-ID: 235794 [Multi-domain] Cd Length: 258 Bit Score: 77.56 E-value: 4.91e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIIN 130
Cdd:PRK06398  49 FKVDVSNKEQVIKGIDYVISKYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIIN 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 131 ISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVgVRMVTIAPGAVETELLSHTTD-------ERIKAGYHDWKDQ- 202
Cdd:PRK06398 129 IASVQSFAVTRNAAAYVTSKHAVLGLTRSIAVDYAPT-IRCVAVCPGSIRTPLLEWAAElevgkdpEHVERKIREWGEMh 207

                        170
                 ....*....|....*..
gi 498358419 203 -MGGVIAPEVIADAVLY 218
Cdd:PRK06398 208 pMKRVGKPEEVAYVVAF 224

PRK08213

gluconate 5-dehydrogenase; Provisional

27-187

5.59e-17

gluconate 5-dehydrogenase; Provisional

Pssm-ID: 181295 [Multi-domain] Cd Length: 259 Bit Score: 77.29 E-value: 5.59e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVE-------PMQALNLpDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMlLGQADVQDPAE-W 98
Cdd:PRK08213  36 GARVVLSARKAEeleeaaaHLEALGI-DALWIAADVADEADIERLAEETLERFGHVDILVNNAGAT-WGAPAEDHPVEaW 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  99 QQMLNINVMGVLNGVHAVLA-GMKARRSGTIINISSIAGRK----TFPNHAAYCATKFAVHALTENIREEVADVGVRMVT 173
Cdd:PRK08213 114 DKVMNLNVRGLFLLSQAVAKrSMIPRGYGRIINVASVAGLGgnppEVMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNA 193

                        170       180
                 ....*....|....*....|....*.
gi 498358419 174 IAPG------------AVETELLSHT 187
Cdd:PRK08213 194 IAPGffptkmtrgtleRLGEDLLAHT 219

fabG

PRK06550

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

78-181

7.28e-17

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

Pssm-ID: 180617 [Multi-domain] Cd Length: 235 Bit Score: 76.54 E-value: 7.28e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVM-----LLGQADvqdpAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFA 152
Cdd:PRK06550  71 LCNTAGILddykpLLDTSL----EEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHA 146

                         90       100
                 ....*....|....*....|....*....
gi 498358419 153 VHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK06550 147 LAGFTKQLALDYAKDGIQVFGIAPGAVKT 175

PRK06482

SDR family oxidoreductase;

46-198

1.06e-16

SDR family oxidoreductase;

Pssm-ID: 235813 [Multi-domain] Cd Length: 276 Bit Score: 77.08 E-value: 1.06e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  46 PDTLCIGV-DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARR 124
Cdd:PRK06482  47 GDRLWVLQlDVTDSAAVRAVVDRAFAALGRIDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQG 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358419 125 SGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAGYHD 198
Cdd:PRK06482 127 GGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFGAGLDRGAPLDAYDD 200

PRK06523

short chain dehydrogenase; Provisional

72-218

1.85e-16

short chain dehydrogenase; Provisional

Pssm-ID: 180604 [Multi-domain] Cd Length: 260 Bit Score: 76.10 E-value: 1.85e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  72 FGPVGCLVNNAG--VMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNH-AAYCA 148
Cdd:PRK06523  75 LGGVDILVHVLGgsSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPEStTAYAA 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 149 TKFAVHALTENIREEVADVGVRMVTIAPGAVETE----LLSHTTDER---IKAGYHDWKDQMGGV-----IAPEVIADAV 216
Cdd:PRK06523 155 AKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEaavaLAERLAEAAgtdYEGAKQIIMDSLGGIplgrpAEPEEVAELI 234


                 ..
gi 498358419 217 LY 218
Cdd:PRK06523 235 AF 236

PRK07523

gluconate 5-dehydrogenase; Provisional

54-183

2.45e-16

gluconate 5-dehydrogenase; Provisional

Pssm-ID: 236040 [Multi-domain] Cd Length: 255 Bit Score: 75.57 E-value: 2.45e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLlgQADVQD-PAE-WQQMLNINVMGVLNGVHAVLAGMKARRSGTIINI 131
Cdd:PRK07523  67 DVTDHDAVRAAIDAFEAEIGPIDILVNNAGMQF--RTPLEDfPADaFERLLRTNISSVFYVGQAVARHMIARGAGKIINI 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498358419 132 SSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK07523 145 ASVQSALARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPL 196

17beta-HSDXI-like_SDR_c

cd05339

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...

53-188

2.97e-16

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: 75.36 E-value: 2.97e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVM----LLgqaDVQDPaEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:cd05339   55 CDVSKREEVYEAAKKIKKEVGDVTILINNAGVVsgkkLL---ELPDE-EIEKTFEVNTLAHFWTTKAFLPDMLERNHGHI 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358419 129 INISSIAGRKTFPNHAAYCATKFAVHALTENIREEVA---DVGVRMVTIAPGAVETELLSHTT 188
Cdd:cd05339  131 VTIASVAGLISPAGLADYCASKAAAVGFHESLRLELKaygKPGIKTTLVCPYFINTGMFQGVK 193

PKR_SDR_c

cd08945

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...

27-218

3.85e-16

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: 75.27 E-value: 3.85e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQA---------LNLPDTLCigvDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGvmLLGQADVQDPAE 97
Cdd:cd08945   27 GLRVFVCARGEEGLATtvkelreagVEADGRTC---DVRSVPEIEALVAAAVARYGPIDVLVNNAG--RSGGGATAELAD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  98 --WQQMLNINVMGVLNGVHAVLA--GMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVT 173
Cdd:cd08945  102 elWLDVVETNLTGVFRVTKEVLKagGMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNA 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 498358419 174 IAPGAVETELLshttdERIKAGYHD-W-------------KDQMGGVIAPEVIADAVLY 218
Cdd:cd08945  182 VCPGFVETPMA-----ASVREHYADiWevsteeafdritaRVPLGRYVTPEEVAGMVAY 235

DHB_DH-like_SDR_c

cd08937

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...

69-182

5.00e-16

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

Pssm-ID: 187642 [Multi-domain] Cd Length: 256 Bit Score: 74.87 E-value: 5.00e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  69 EAQFGPVGCLVNNAGVMLLGQA-DVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTfpNHAAYC 147
Cdd:cd08937   75 VERFGRVDVLINNVGGTIWAKPyEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGI--YRIPYS 152

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 498358419 148 ATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:cd08937  153 AAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAP 187

PRK07023

SDR family oxidoreductase;

27-181

6.38e-16

SDR family oxidoreductase;

Pssm-ID: 180796 [Multi-domain] Cd Length: 243 Bit Score: 74.28 E-value: 6.38e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQALNLPDTLC-IGVDVTDTAAMKAAVAQAEAQFGPVGC----LVNNAGVML-LGQADVQDPAEWQQ 100
Cdd:PRK07023  25 GIAVLGVARSRHPSLAAAAGERLAeVELDLSDAAAAAAWLAGDLLAAFVDGAsrvlLINNAGTVEpIGPLATLDAAAIAR 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 101 MLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEvADVGVRMVTIAPGAVE 180
Cdd:PRK07023 105 AVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAALDHHARAVALD-ANRALRIVSLAPGVVD 183


                 .
gi 498358419 181 T 181
Cdd:PRK07023 184 T 184

PRK12827

short chain dehydrogenase; Provisional

53-218

6.46e-16

short chain dehydrogenase; Provisional

Pssm-ID: 237219 [Multi-domain] Cd Length: 249 Bit Score: 74.37 E-value: 6.46e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGM-KARRSGTIINI 131
Cdd:PRK12827  66 FDVRDFAATRAALDAGVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMiRARRGGRIVNI 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 132 SSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHttderikAGYHDWKDQ---MGGVIA 208
Cdd:PRK12827 146 ASVAGVRGNRGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADN-------AAPTEHLLNpvpVQRLGE 218

                        170
                 ....*....|
gi 498358419 209 PEVIADAVLY 218
Cdd:PRK12827 219 PDEVAALVAF 228

PRK06125

short chain dehydrogenase; Provisional

30-218

7.13e-16

short chain dehydrogenase; Provisional

Pssm-ID: 235703 [Multi-domain] Cd Length: 259 Bit Score: 74.31 E-value: 7.13e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  30 LLLLARRVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAE---AQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINV 106
Cdd:PRK06125  34 LHLVARDADALEALAADLRAAHGVDVAVHALDLSSPEAREqlaAEAGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 107 MGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSH 186
Cdd:PRK06125 114 FGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPDADYICGSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLT 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 498358419 187 TTDERIKAGYHD---WKDQMGGV-----IAPEVIADAVLY 218
Cdd:PRK06125 194 LLKGRARAELGDesrWQELLAGLplgrpATPEEVADLVAF 233

XR_like_SDR_c

cd05351

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...

73-183

7.58e-16

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: 74.04 E-value: 7.58e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  73 GPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARR-SGTIINISSIAGRKTFPNHAAYCATKF 151
Cdd:cd05351   75 GPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCSTKA 154

                         90       100       110
                 ....*....|....*....|....*....|..
gi 498358419 152 AVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:cd05351  155 ALDMLTKVMALELGPHKIRVNSVNPTVVMTDM 186

carb_red_sniffer_like_SDR_c

cd05325

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...

50-183

8.11e-16

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: 73.87 E-value: 8.11e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  50 CIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQ-DPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:cd05325   51 ILELDVTDEIAESAEAVAERLGDAGLDVLINNAGILHSYGPASEvDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKI 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 129 INISSIAGR---KTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:cd05325  131 INISSRVGSigdNTSGGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDM 188

PRK07774

SDR family oxidoreductase;

49-194

8.71e-16

SDR family oxidoreductase;

Pssm-ID: 236094 [Multi-domain] Cd Length: 250 Bit Score: 74.01 E-value: 8.71e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVM------LLGQADVQDpaeWQQMLNINVMGVLNGVHAVLAGMKA 122
Cdd:PRK07774  58 IAVQVDVSDPDSAKAMADATVSAFGGIDYLVNNAAIYggmkldLLITVPWDY---YKKFMSVNLDGALVCTRAVYKHMAK 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358419 123 RRSGTIINISSIAGrktFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKA 194
Cdd:PRK07774 135 RGGGAIVNQSSTAA---WLYSNFYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKEFVA 203

PRK08226

SDR family oxidoreductase UcpA;

46-183

1.14e-15

SDR family oxidoreductase UcpA;

Pssm-ID: 181305 [Multi-domain] Cd Length: 263 Bit Score: 74.07 E-value: 1.14e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  46 PDTLCIGV--DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQAdVQDPAEWQQM-LNINVMGVLNGVHAVLAGMKA 122
Cdd:PRK08226  52 RGHRCTAVvaDVRDPASVAAAIKRAKEKEGRIDILVNNAGVCRLGSF-LDMSDEDRDFhIDINIKGVWNVTKAVLPEMIA 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358419 123 RRSGTIINISSIAGRKTF-PNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK08226 131 RKDGRIVMMSSVTGDMVAdPGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPM 192

PRK06198

short chain dehydrogenase; Provisional

46-218

1.64e-15

short chain dehydrogenase; Provisional

Pssm-ID: 180462 [Multi-domain] Cd Length: 260 Bit Score: 73.50 E-value: 1.64e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  46 PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRS 125
Cdd:PRK06198  56 AKAVFVQADLSDVEDCRRVVAAADEAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKA 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 126 -GTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEllshtTDERIKAGYH----DWK 200
Cdd:PRK06198 136 eGTIVNIGSMSAHGGQPFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE-----GEDRIQREFHgapdDWL 210

                        170       180
                 ....*....|....*....|....
gi 498358419 201 DQ------MGGVIAPEVIADAVLY 218
Cdd:PRK06198 211 EKaaatqpFGRLLDPDEVARAVAF 234

PRK12938

3-ketoacyl-ACP reductase;

69-220

1.69e-15

3-ketoacyl-ACP reductase;

Pssm-ID: 171822 [Multi-domain] Cd Length: 246 Bit Score: 73.12 E-value: 1.69e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  69 EAQFGPVGCLVNNAGVMllgqADV----QDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHA 144
Cdd:PRK12938  76 KAEVGEIDVLVNNAGIT----RDVvfrkMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQT 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 145 AYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELlshttderIKAGYHDWKDQMGGVI------APEVIADAVly 218
Cdd:PRK12938 152 NYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDM--------VKAIRPDVLEKIVATIpvrrlgSPDEIGSIV-- 221


                 ..
gi 498358419 219 AW 220
Cdd:PRK12938 222 AW 223

PRK07890

short chain dehydrogenase; Provisional

47-177

1.94e-15

short chain dehydrogenase; Provisional

Pssm-ID: 181159 [Multi-domain] Cd Length: 258 Bit Score: 73.07 E-value: 1.94e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVM--LLGQADVqDPAEWQQMLNINVMGVLNGVHAVLAGMKaRR 124
Cdd:PRK07890  55 RALAVPTDITDEDQCANLVALALERFGRVDALVNNAFRVpsMKPLADA-DFAHWRAVIELNVLGTLRLTQAFTPALA-ES 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 498358419 125 SGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPG 177
Cdd:PRK07890 133 GGSIVMINSMVLRHSQPKYGAYKMAKGALLAASQSLATELGPQGIRVNSVAPG 185

PRK06123

SDR family oxidoreductase;

49-218

3.39e-15

SDR family oxidoreductase;

Pssm-ID: 180411 [Multi-domain] Cd Length: 248 Bit Score: 72.50 E-value: 3.39e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGvMLLGQADVQ--DPAEWQQMLNINVMGVLNGVHAVLAGMKAR--- 123
Cdd:PRK06123  55 LAVAADVADEADVLRLFEAVDRELGRLDALVNNAG-ILEAQMRLEqmDAARLTRIFATNVVGSFLCAREAVKRMSTRhgg 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 124 RSGTIINISSIAGRKTFPN-HAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD----ERIKAGYhd 198
Cdd:PRK06123 134 RGGAIVNVSSMAARLGSPGeYIDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEpgrvDRVKAGI-- 211

                        170       180
                 ....*....|....*....|
gi 498358419 199 wKDQMGGviAPEVIADAVLY 218
Cdd:PRK06123 212 -PMGRGG--TAEEVARAILW 228

PRK07577

SDR family oxidoreductase;

27-187

6.58e-15

SDR family oxidoreductase;

Pssm-ID: 181044 [Multi-domain] Cd Length: 234 Bit Score: 71.30 E-value: 6.58e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPmqalNLPDTLcIGVDVTDTAAMKAAVAQAEAQFgPVGCLVNNAGVML---LGQADVQDpaeWQQMLN 103
Cdd:PRK07577  27 GHQVIGIARSAID----DFPGEL-FACDLADIEQTAATLAQINEIH-PVDAIVNNVGIALpqpLGKIDLAA---LQDVYD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 104 INVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTfPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK07577  98 LNVRAAVQVTQAFLEGMKLREQGRIVNICSRAIFGA-LDRTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176


                 ....
gi 498358419 184 LSHT 187
Cdd:PRK07577 177 FRQT 180

PRK12745

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

54-195

8.31e-15

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

Pssm-ID: 237188 [Multi-domain] Cd Length: 256 Bit Score: 71.53 E-value: 8.31e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQD--PAEWQQMLNINVMGVLNGVHAVLAGMKARR------S 125
Cdd:PRK12745  60 DVADLSAHEAMLDAAQAAWGRIDCLVNNAGVGVKVRGDLLDltPESFDRVLAINLRGPFFLTQAVAKRMLAQPepeelpH 139

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358419 126 GTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTT---DERIKAG 195
Cdd:PRK12745 140 RSIVFVSSVNAIMVSPNRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTakyDALIAKG 212

PRK06114

SDR family oxidoreductase;

49-181

9.87e-15

SDR family oxidoreductase;

Pssm-ID: 180408 [Multi-domain] Cd Length: 254 Bit Score: 71.35 E-value: 9.87e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:PRK06114  61 IQIAADVTSKADLRAAVARTEAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSI 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498358419 129 INISSIAG----RKTfpNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK06114 141 VNIASMSGiivnRGL--LQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTAT 195

PRK06949

SDR family oxidoreductase;

27-186

1.23e-14

SDR family oxidoreductase;

Pssm-ID: 180773 [Multi-domain] Cd Length: 258 Bit Score: 70.95 E-value: 1.23e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQALNLP------DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQ 100
Cdd:PRK06949  33 GAKVVLASRRVERLKELRAEieaeggAAHVVSLDVTDYQSIKAAVAHAETEAGTIDILVNNSGVSTTQKLVDVTPADFDF 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 101 MLNINVMGVLNGVHAVLAGMKARRSGT--------IINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMV 172
Cdd:PRK06949 113 VFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVN 192

                        170
                 ....*....|....
gi 498358419 173 TIAPGAVETELLSH 186
Cdd:PRK06949 193 AICPGYIDTEINHH 206

7_alpha_HSDH_SDR_c

cd05365

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...

50-218

1.45e-14

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: 70.68 E-value: 1.45e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  50 CIGV--DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADV-QDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSG 126
Cdd:cd05365   50 AIGLecNVTSEQDLEAVVKATVSQFGGITILVNNAGGGGPKPFDMpMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 127 TIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELL-SHTTDERIKAGYHDwkDQMGG 205
Cdd:cd05365  130 AILNISSMSSENKNVRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALaSVLTPEIERAMLKH--TPLGR 207

                        170
                 ....*....|...
gi 498358419 206 VIAPEVIADAVLY 218
Cdd:cd05365  208 LGEPEDIANAALF 220

PRK12936

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

36-218

2.38e-14

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

Pssm-ID: 171820 [Multi-domain] Cd Length: 245 Bit Score: 69.94 E-value: 2.38e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  36 RVEPMQAL--NLPDTLCI-GVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNG 112
Cdd:PRK12936  39 RVEKLEALaaELGERVKIfPANLSDRDEVKALGQKAEADLEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 113 VHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERi 192
Cdd:PRK12936 119 TRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQ- 197

                        170       180       190
                 ....*....|....*....|....*....|..
gi 498358419 193 kagyhdwKDQMGGVI------APEVIADAVLY 218
Cdd:PRK12936 198 -------KEAIMGAIpmkrmgTGAEVASAVAY 222

fabG

PRK08642

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

48-218

3.02e-14

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

Pssm-ID: 181517 [Multi-domain] Cd Length: 253 Bit Score: 69.73 E-value: 3.02e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  48 TLCIGVDVTDTAAMKAAVAQAEAQFG-PVGCLVNNAGVMLLGQADVQDPAE---W---QQMLNINVMGVLNGVHAVLAGM 120
Cdd:PRK08642  54 AIALQADVTDREQVQAMFATATEHFGkPITTVVNNALADFSFDGDARKKADditWedfQQQLEGSVKGALNTIQAALPGM 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 121 KARRSGTIINISS-IAGRKTFPNHaAYCATKFAVHALTENIREEVADVGVRMVTIAPGAV-ETELLSHTTDE---RIKAG 195
Cdd:PRK08642 134 REQGFGRIINIGTnLFQNPVVPYH-DYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLrTTDASAATPDEvfdLIAAT 212

                        170       180
                 ....*....|....*....|...
gi 498358419 196 yhdwkDQMGGVIAPEVIADAVLY 218
Cdd:PRK08642 213 -----TPLRKVTTPQEFADAVLF 230

SDH_SDR_c

cd05363

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...

46-182

4.24e-14

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: 69.57 E-value: 4.24e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  46 PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKAR-R 124
Cdd:cd05363   49 PAACAISLDVTDQASIDRCVAALVDRWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgR 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 125 SGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:cd05363  129 GGKIINMASQAGRRGEALVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186

PRK08589

SDR family oxidoreductase;

53-218

7.88e-14

SDR family oxidoreductase;

Pssm-ID: 181491 [Multi-domain] Cd Length: 272 Bit Score: 69.04 E-value: 7.88e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAE-WQQMLNINVMGVLNGVHAVLAGMkARRSGTIINI 131
Cdd:PRK08589  61 VDISDEQQVKDFASEIKEQFGRVDVLFNNAGVDNAAGRIHEYPVDvFDKIMAVDMRGTFLMTKMLLPLM-MEQGGSIINT 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 132 SSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL---LSHTTDERIKAGYHD---WKDQMGG 205
Cdd:PRK08589 140 SSFSGQAADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLvdkLTGTSEDEAGKTFREnqkWMTPLGR 219

                        170
                 ....*....|...
gi 498358419 206 VIAPEVIADAVLY 218
Cdd:PRK08589 220 LGKPEEVAKLVVF 232

PRK06194

hypothetical protein; Provisional

33-181

8.05e-14

hypothetical protein; Provisional

Pssm-ID: 180458 [Multi-domain] Cd Length: 287 Bit Score: 69.27 E-value: 8.05e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  33 LARRVEPMQALNLpDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNG 112
Cdd:PRK06194  43 LDRAVAELRAQGA-EVLGVRTDVSDAAQVEALADAALERFGAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHG 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358419 113 VHAVLAGMKAR------RSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVG--VRMVTIAPGAVET 181
Cdd:PRK06194 122 VRAFTPLMLAAaekdpaYEGHIVNTASMAGLLAPPAMGIYNVSKHAVVSLTETLYQDLSLVTdqVGASVLCPYFVPT 198

PRK07097

gluconate 5-dehydrogenase; Provisional

54-181

1.45e-13

gluconate 5-dehydrogenase; Provisional

Pssm-ID: 235933 [Multi-domain] Cd Length: 265 Bit Score: 68.17 E-value: 1.45e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGV-----MLLGQAdvqdpAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:PRK07097  67 DVTDEDGVQAMVSQIEKEVGVIDILVNNAGIikripMLEMSA-----EDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKI 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 498358419 129 INISSIA---GRKTFpnhAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK07097 142 INICSMMselGRETV---SAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIAT 194

PRK06124

SDR family oxidoreductase;

54-182

1.61e-13

SDR family oxidoreductase;

Pssm-ID: 235702 [Multi-domain] Cd Length: 256 Bit Score: 67.82 E-value: 1.61e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS 133
Cdd:PRK06124  68 DIADEEAVAAAFARIDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITS 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 498358419 134 IAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK06124 148 IAGQVARAGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE 196

TR_SDR_c

cd05329

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...

73-218

1.61e-13

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: 67.86 E-value: 1.61e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  73 GPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFA 152
Cdd:cd05329   83 GKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGA 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 153 VHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD--ERIKAGYHdwKDQMGGVIAPEVIADAVLY 218
Cdd:cd05329  163 LNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQqkENLDKVIE--RTPLKRFGEPEEVAALVAF 228

PRK06935

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

35-182

1.75e-13

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

Pssm-ID: 180761 [Multi-domain] Cd Length: 258 Bit Score: 67.84 E-value: 1.75e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  35 RRVEPMQalnlpdtlcigVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVH 114
Cdd:PRK06935  63 RKVTFVQ-----------VDLTKPESAEKVVKEALEEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQ 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 115 AVLAGMKARRSGTIINISSI---AGRKTFPnhaAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK06935 132 AVAKVMAKQGSGKIINIASMlsfQGGKFVP---AYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199

PRK07831

SDR family oxidoreductase;

54-190

1.89e-13

SDR family oxidoreductase;

Pssm-ID: 236110 [Multi-domain] Cd Length: 262 Bit Score: 67.75 E-value: 1.89e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGvmLLGQADVQD--PAEWQQMLNINVMGVLNGVHAVLAGMKAR-RSGTIIN 130
Cdd:PRK07831  77 DVTSEAQVDALIDAAVERLGRLDVLVNNAG--LGGQTPVVDmtDDEWSRVLDVTLTGTFRATRAALRYMRARgHGGVIVN 154

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 131 ISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDE 190
Cdd:PRK07831 155 NASVLGWRAQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKVTSA 214

PRK12935

acetoacetyl-CoA reductase; Provisional

47-190

1.94e-13

acetoacetyl-CoA reductase; Provisional

Pssm-ID: 183832 [Multi-domain] Cd Length: 247 Bit Score: 67.72 E-value: 1.94e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSG 126
Cdd:PRK12935  57 DVYAVQADVSKVEDANRLVEEAVNHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEG 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358419 127 TIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDE 190
Cdd:PRK12935 137 RIISISSIIGQAGGFGQTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEE 200

RDH_SDR_c

cd08933

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...

40-195

3.01e-13

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: 67.17 E-value: 3.01e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  40 MQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQ-ADVQDPAEWQQMLNINVMGVLNGVHAVLA 118
Cdd:cd08933   53 LNRAGPGSCKFVPCDVTKEEDIKTLISVTVERFGRIDCLVNNAGWHPPHQtTDETSAQEFRDLLNLNLISYFLASKYALP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 119 GMKARRsGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET----ELLSHTTDER--I 192
Cdd:cd08933  133 HLRKSQ-GNIINLSSLVGSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRVNCISPGNIWTplweELAAQTPDTLatI 211


                 ...
gi 498358419 193 KAG 195
Cdd:cd08933  212 KEG 214

PRK06139

SDR family oxidoreductase;

4-186

3.49e-13

SDR family oxidoreductase;

Pssm-ID: 235713 [Multi-domain] Cd Length: 330 Bit Score: 67.82 E-value: 3.49e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   4 SLVVITGASAGIGAAIARAFSAAGHPLLLLARRVEPMQALNL------PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGC 77
Cdd:PRK06139   8 AVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEecralgAEVLVVPTDVTDADQVKALATQAASFGGRIDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMLLGQADvQDPAE-WQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHAL 156
Cdd:PRK06139  88 WVNNVGVGAVGRFE-ETPIEaHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLRGF 166

                        170       180       190
                 ....*....|....*....|....*....|.
gi 498358419 157 TENIREEVADV-GVRMVTIAPGAVETELLSH 186
Cdd:PRK06139 167 SEALRGELADHpDIHVCDVYPAFMDTPGFRH 197

PRK09242

SDR family oxidoreductase;

51-185

3.90e-13

SDR family oxidoreductase;

Pssm-ID: 181721 [Multi-domain] Cd Length: 257 Bit Score: 66.69 E-value: 3.90e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIIN 130
Cdd:PRK09242  65 LAADVSDDEDRRAILDWVEDHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVN 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 498358419 131 ISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLS 185
Cdd:PRK09242 145 IGSVSGLTHVRSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTS 199

PRK05855

SDR family oxidoreductase;

5-219

4.56e-13

SDR family oxidoreductase;

Pssm-ID: 235628 [Multi-domain] Cd Length: 582 Bit Score: 68.08 E-value: 4.56e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   5 LVVITGASAGIGAAIARAFSAAGHPLLL-------LARRVEPMQALNlPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGC 77
Cdd:PRK05855 317 LVVVTGAGSGIGRETALAFAREGAEVVAsdideaaAERTAELIRAAG-AVAHAYRVDVSDADAMEAFAEWVRAEHGVPDI 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKAR-RSGTIINISSIAGRKTFPNHAAYCATKFAVHAL 156
Cdd:PRK05855 396 VVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAYAPSRSLPAYATSKAAVLML 475

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358419 157 TENIREEVADVGVRMVTIAPGAVETELLSHT----TDERIKAGYHDWKDQMGGV--IAPEVIADAVLYA 219
Cdd:PRK05855 476 SECLRAELAAAGIGVTAICPGFVDTNIVATTrfagADAEDEARRRGRADKLYQRrgYGPEKVAKAIVDA 544

BKR_2_SDR_c

cd05349

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...

6-218

5.64e-13

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: 66.33 E-value: 5.64e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   6 VVITGASAGIGAAIARAFSAAGHPLLLLARR----VEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNN 81
Cdd:cd05349    3 VLVTGASRGLGAAIARSFAREGARVVVNYYRstesAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIVNN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  82 AGV------MLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS-IAGRKTFPNHaAYCATKFAVH 154
Cdd:cd05349   83 ALIdfpfdpDQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTnLFQNPVVPYH-DYTTAKAALL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 155 ALTENIREEVADVGVRMVTIAPGAVETELLS-HTTDERIkagyhDWKDQ---MGGVIAPEVIADAVLY 218
Cdd:cd05349  162 GFTRNMAKELGPYGITVNMVSGGLLKVTDASaATPKEVF-----DAIAQttpLGKVTTPQDIADAVLF 224

DHRS1_HSDL2-like_SDR_c

cd05338

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...

49-224

6.38e-13

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: 65.88 E-value: 6.38e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLgqADVQD-PAE-WQQMLNINVMGVLNGVHAVLAGMKARRSG 126
Cdd:cd05338   67 LPIVVDVRDEDQVRALVEATVDQFGRLDILVNNAGAIWL--SLVEDtPAKrFDLMQRVNLRGTYLLSQAALPHMVKAGQG 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 127 TIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPG-AVETELLSHTTDERIKAgyhDWKDqmgg 205
Cdd:cd05338  145 HILNISPPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStAIETPAATELSGGSDPA---RARS---- 217

                        170
                 ....*....|....*....
gi 498358419 206 viaPEVIADAVLYAWHQPA 224
Cdd:cd05338  218 ---PEILSDAVLAILSRPA 233

PRK06113

7-alpha-hydroxysteroid dehydrogenase; Validated

54-218

1.07e-12

7-alpha-hydroxysteroid dehydrogenase; Validated

Pssm-ID: 135765 [Multi-domain] Cd Length: 255 Bit Score: 65.64 E-value: 1.07e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMllGQADVQDP-AEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:PRK06113  68 DITSEQELSALADFALSKLGKVDILVNNAGGG--GPKPFDMPmADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTIT 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAGY--HDWKDQMGgviAPE 210
Cdd:PRK06113 146 SMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKMlqHTPIRRLG---QPQ 222


                 ....*...
gi 498358419 211 VIADAVLY 218
Cdd:PRK06113 223 DIANAALF 230

benD

PRK12823

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

70-180

1.07e-12

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

Pssm-ID: 183772 [Multi-domain] Cd Length: 260 Bit Score: 65.74 E-value: 1.07e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  70 AQFGPVGCLVNNAGVMLLGQADVQ-DPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTfpNHAAYCA 148
Cdd:PRK12823  80 EAFGRIDVLINNVGGTIWAKPFEEyEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIATRGI--NRVPYSA 157

                         90       100       110
                 ....*....|....*....|....*....|..
gi 498358419 149 TKFAVHALTENIREEVADVGVRMVTIAPGAVE 180
Cdd:PRK12823 158 AKGGVNALTASLAFEYAEHGIRVNAVAPGGTE 189

PRK08936

glucose-1-dehydrogenase; Provisional

54-181

1.30e-12

glucose-1-dehydrogenase; Provisional

Pssm-ID: 181585 [Multi-domain] Cd Length: 261 Bit Score: 65.52 E-value: 1.30e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGM-KARRSGTIINIS 132
Cdd:PRK08936  65 DVTVESDVVNLIQTAVKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFvEHDIKGNIINMS 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK08936 145 SVHEQIPWPLFVHYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINT 193

PRK09135

pteridine reductase; Provisional

48-218

1.47e-12

pteridine reductase; Provisional

Pssm-ID: 181668 [Multi-domain] Cd Length: 249 Bit Score: 64.95 E-value: 1.47e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  48 TLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVML---LGQADvqdPAEWQQMLNINVMGVLNGVHAVLAGMKARR 124
Cdd:PRK09135  59 AAALQADLLDPDALPELVAACVAAFGRLDALVNNASSFYptpLGSIT---EAQWDDLFASNLKAPFFLSQAAAPQLRKQR 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 125 sGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADvGVRMVTIAPGAV----ETELLSHTTDERIKAgyhdwK 200
Cdd:PRK09135 136 -GAIVNITDIHAERPLKGYPVYCAAKAALEMLTRSLALELAP-EVRVNAVAPGAIlwpeDGNSFDEEARQAILA-----R 208

                        170
                 ....*....|....*...
gi 498358419 201 DQMGGVIAPEVIADAVLY 218
Cdd:PRK09135 209 TPLKRIGTPEDIAEAVRF 226

PRK08063

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

72-218

2.43e-12

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

Pssm-ID: 236145 [Multi-domain] Cd Length: 250 Bit Score: 64.36 E-value: 2.43e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  72 FGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKF 151
Cdd:PRK08063  80 FGRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKA 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358419 152 AVHALTENIREEVADVGVRMVTIAPGAVETELLSH--TTDERIKAGYHdwKDQMGGVIAPEVIADAVLY 218
Cdd:PRK08063 160 ALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHfpNREELLEDARA--KTPAGRMVEPEDVANAVLF 226

PLN02253

xanthoxin dehydrogenase

46-218

2.89e-12

xanthoxin dehydrogenase

Pssm-ID: 177895 [Multi-domain] Cd Length: 280 Bit Score: 64.46 E-value: 2.89e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  46 PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQ--DPAEWQQMLNINVMGVLNGVHAVLAGMKAR 123
Cdd:PLN02253  66 PNVCFFHCDVTVEDDVSRAVDFTVDKFGTLDIMVNNAGLTGPPCPDIRnvELSEFEKVFDVNVKGVFLGMKHAARIMIPL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 124 RSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL-LSH-TTDERIKAGYHDWKD 201
Cdd:PLN02253 146 KKGSIVSLCSVASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALaLAHlPEDERTEDALAGFRA 225

                        170       180
                 ....*....|....*....|....
gi 498358419 202 ------QMGGV-IAPEVIADAVLY 218
Cdd:PLN02253 226 fagknaNLKGVeLTVDDVANAVLF 249

PR_SDR_c

cd05357

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...

48-223

3.04e-12

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

Pssm-ID: 187615 [Multi-domain] Cd Length: 234 Bit Score: 63.84 E-value: 3.04e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  48 TLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGT 127
Cdd:cd05357   52 AVLVQADLSDFAACADLVAAAFRAFGRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGS 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 128 IINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADvGVRMVTIAPGAVeteLLSHTTDERIKAGYHDwKDQMGGVI 207
Cdd:cd05357  132 IINIIDAMTDRPLTGYFAYCMSKAALEGLTRSAALELAP-NIRVNGIAPGLI---LLPEDMDAEYRENALR-KVPLKRRP 206

                        170
                 ....*....|....*.
gi 498358419 208 APEVIADAVLYAWHQP 223
Cdd:cd05357  207 SAEEIADAVIFLLDSN 222

TER_DECR_SDR_a

cd05369

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...

33-218

3.09e-12

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: 64.15 E-value: 3.09e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  33 LARRVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNG 112
Cdd:cd05369   40 LEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 113 VHAVLAG-MKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET---------- 181
Cdd:cd05369  120 TKAVGKRlIEAKHGGSILNISATYAYTGSPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTtegmerlaps 199

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 498358419 182 ELLSHTTDERIKAGyhdwkdQMGgviAPEVIADAVLY 218
Cdd:cd05369  200 GKSEKKMIERVPLG------RLG---TPEEIANLALF 227

PRK07062

SDR family oxidoreductase;

54-181

4.28e-12

SDR family oxidoreductase;

Pssm-ID: 180818 [Multi-domain] Cd Length: 265 Bit Score: 63.91 E-value: 4.28e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQ-ADVQDPAeWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:PRK07062  67 DVLDEADVAAFAAAVEARFGGVDMLVNNAGQGRVSTfADTTDDA-WRDELELKYFSVINPTRAFLPLLRASAAASIVCVN 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK07062 146 SLLALQPEPHMVATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVES 194

fabG

PRK06077

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

72-217

7.22e-12

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

Pssm-ID: 235693 [Multi-domain] Cd Length: 252 Bit Score: 63.20 E-value: 7.22e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  72 FGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMkaRRSGTIINISSIAGRKTFPNHAAYCATKF 151
Cdd:PRK06077  82 YGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKA 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358419 152 AVHALTENIREEVADvGVRMVTIAPGAVETEL------LSHTTDERIKAGYhdwkDQMGGVIAPEVIADAVL 217
Cdd:PRK06077 160 AVINLTKYLALELAP-KIRVNAIAPGFVKTKLgeslfkVLGMSEKEFAEKF----TLMGKILDPEEVAEFVA 226

PRK08085

gluconate 5-dehydrogenase; Provisional

54-183

8.26e-12

gluconate 5-dehydrogenase; Provisional

Pssm-ID: 181225 [Multi-domain] Cd Length: 254 Bit Score: 63.23 E-value: 8.26e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS 133
Cdd:PRK08085  66 NVTHKQEVEAAIEHIEKDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICS 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 498358419 134 IA---GRKTFpnhAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK08085 146 MQselGRDTI---TPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEM 195

mannonate_red_SDR_c

cd08935

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...

47-183

8.28e-12

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: 63.25 E-value: 8.28e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAG---------VMLLGQADVQDPAE-----WQQMLNINVMGVLNG 112
Cdd:cd08935   55 RAIALAADVLDRASLERAREEIVAQFGTVDILINGAGgnhpdattdPEHYEPETEQNFFDldeegWEFVFDLNLNGSFLP 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 113 VHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:cd08935  135 SQVFGKDMLEQKGGSIINISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQ 205

SDR_c1

cd05355

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...

71-193

8.52e-12

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: 63.08 E-value: 8.52e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  71 QFGPVGCLVNNAGVMLLGQ--ADVqDPAEWQQMLNINVMGVLNGVHAVLAGMKarRSGTIINISSIAGRKTFPNHAAYCA 148
Cdd:cd05355  102 EFGKLDILVNNAAYQHPQEsiEDI-TTEQLEKTFRTNIFSMFYLTKAALPHLK--KGSSIINTTSVTAYKGSPHLLDYAA 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 498358419 149 TKFAVHALTENIREEVADVGVRMVTIAPGAVETELL-SHTTDERIK 193
Cdd:cd05355  179 TKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIpSSFPEEKVS 224

SDR

cd02266

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...

77-181

8.99e-12

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: 61.76 E-value: 8.99e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  77 CLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHAL 156
Cdd:cd02266   34 VVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGL 113

                         90       100
                 ....*....|....*....|....*
gi 498358419 157 TENIREEVADVGVRMVTIAPGAVET 181
Cdd:cd02266  114 AQQWASEGWGNGLPATAVACGTWAG 138

PRK08265

short chain dehydrogenase; Provisional

51-219

1.03e-11

short chain dehydrogenase; Provisional

Pssm-ID: 236209 [Multi-domain] Cd Length: 261 Bit Score: 62.72 E-value: 1.03e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADvQDPAEWQQMLNINVMGVLNGVHAVLAGMKaRRSGTIIN 130
Cdd:PRK08265  57 IATDITDDAAIERAVATVVARFGRVDILVNLACTYLDDGLA-SSRADWLAALDVNLVSAAMLAQAAHPHLA-RGGGAIVN 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 131 ISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD------ERIKAGYHdwkdQMG 204
Cdd:PRK08265 135 FTSISAKFAQTGRWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSGgdrakaDRVAAPFH----LLG 210

                        170
                 ....*....|....*
gi 498358419 205 GVIAPEVIADAVLYA 219
Cdd:PRK08265 211 RVGDPEEVAQVVAFL 225

PRK07102

SDR family oxidoreductase;

27-181

3.25e-11

SDR family oxidoreductase;

Pssm-ID: 180838 [Multi-domain] Cd Length: 243 Bit Score: 61.09 E-value: 3.25e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  27 GHPLLLLARRVEPMQAL-------NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNnagvmLLG-QADVQ-DPAE 97
Cdd:PRK07102  25 GARLYLAARDVERLERLaddlrarGAVAVSTHELDILDTASHAAFLDSLPALPDIVLIAVG-----TLGdQAACEaDPAL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  98 WQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPG 177
Cdd:PRK07102 100 ALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTAFLSGLRNRLFKSGVHVLTVKPG 179


                 ....
gi 498358419 178 AVET 181
Cdd:PRK07102 180 FVRT 183

RhlG_SDR_c

cd08942

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...

78-218

3.67e-11

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: 61.34 E-value: 3.67e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVL----AGMKARRSGTIINISSIAG-RKTFPNHAAYCATKFA 152
Cdd:cd08942   86 LVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLpllrAAATAENPARVINIGSIAGiVVSGLENYSYGASKAA 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 153 VHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDEriKAGYHDWKDQ--MGGVIAPEVIADAVLY 218
Cdd:cd08942  166 VHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLND--PAALEAEEKSipLGRWGRPEDMAGLAIM 231

PRK06947

SDR family oxidoreductase;

54-183

4.24e-11

SDR family oxidoreductase;

Pssm-ID: 180771 [Multi-domain] Cd Length: 248 Bit Score: 60.97 E-value: 4.24e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQ--ADVqDPAEWQQMLNINVMGVLngvhaVLAGMKARR------- 124
Cdd:PRK06947  60 DVANEADVIAMFDAVQSAFGRLDALVNNAGIVAPSMplADM-DAARLRRMFDTNVLGAY-----LCAREAARRlstdrgg 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 125 -SGTIINISSIAGRKTFPN-HAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK06947 134 rGGAIVNVSSIASRLGSPNeYVDYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194

Ycik_SDR_c

cd05340

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...

69-181

5.00e-11

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: 60.67 E-value: 5.00e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  69 EAQFGPVGCLVNNAG----VMLLGQadvQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHA 144
Cdd:cd05340   79 AVNYPRLDGVLHNAGllgdVCPLSE---QNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWG 155

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 498358419 145 AYCATKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:cd05340  156 AYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192

PRK09730

SDR family oxidoreductase;

54-220

8.62e-11

SDR family oxidoreductase;

Pssm-ID: 182051 [Multi-domain] Cd Length: 247 Bit Score: 60.25 E-value: 8.62e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVmLLGQADVQD--PAEWQQMLNINVMGVLNGVHAVLAGMKAR---RSGTI 128
Cdd:PRK09730  59 DISDENQVVAMFTAIDQHDEPLAALVNNAGI-LFTQCTVENltAERINRVLSTNVTGYFLCCREAVKRMALKhggSGGAI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 129 INISSIAGRKTFP-NHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD----ERIKAGYhdwKDQM 203
Cdd:PRK09730 138 VNVSSAASRLGAPgEYVDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEpgrvDRVKSNI---PMQR 214

                        170
                 ....*....|....*..
gi 498358419 204 GGviAPEVIADAVlyAW 220
Cdd:PRK09730 215 GG--QPEEVAQAI--VW 227

PRK07201

SDR family oxidoreductase;

53-187

8.80e-11

SDR family oxidoreductase;

Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 61.12 E-value: 8.80e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  53 VDVTDTAAMKAAVAQAEAQFGPVGCLVNNAG------VMLlgqaDVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSG 126
Cdd:PRK07201 427 CDLTDSAAVDHTVKDILAEHGHVDYLVNNAGrsirrsVEN----STDRFHDYERTMAVNYFGAVRLILGLLPHMRERRFG 502

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 127 TIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHT 187
Cdd:PRK07201 503 HVVNVSSIGVQTNAPRFSAYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPMIAPT 563

PRK12742

SDR family oxidoreductase;

70-183

1.02e-10

SDR family oxidoreductase;

Pssm-ID: 183714 [Multi-domain] Cd Length: 237 Bit Score: 59.77 E-value: 1.02e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  70 AQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGvhAVLAGMKARRSGTIINISSIAG-RKTFPNHAAYCA 148
Cdd:PRK12742  71 RKSGALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHA--SVEAARQMPEGGRIIIIGSVNGdRMPVAGMAAYAA 148

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 498358419 149 TKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK12742 149 SKSALQGMARGLARDFGPRGITINVVQPGPIDTDA 183

PRK08251

SDR family oxidoreductase;

6-186

1.10e-10

SDR family oxidoreductase;

Pssm-ID: 181324 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 1.10e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   6 VVITGASAGIGAAIARAFSAAGHPLLLLARRVEPMQAL------NLPDtlcIGV-----DVTDTAAMKAAVAQAEAQFGP 74
Cdd:PRK08251   5 ILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELkaellaRYPG---IKVavaalDVNDHDQVFEVFAEFRDELGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  75 VGCLVNNAGV-----MLLGQADVQdpaewQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNH-AAYCA 148
Cdd:PRK08251  82 LDRVIVNAGIgkgarLGTGKFWAN-----KATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGVkAAYAA 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 498358419 149 TKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSH 186
Cdd:PRK08251 157 SKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAK 194

CR_SDR_c

cd08936

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...

71-181

1.39e-10

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: 59.48 E-value: 1.39e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  71 QFGPVGCLVNNAGVMLLGqADVQDPAE--WQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCA 148
Cdd:cd08936   84 LHGGVDILVSNAAVNPFF-GNILDSTEevWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNV 162

                         90       100       110
                 ....*....|....*....|....*....|...
gi 498358419 149 TKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:cd08936  163 SKTALLGLTKNLAPELAPRNIRVNCLAPGLIKT 195

PRK08017

SDR family oxidoreductase;

78-181

1.53e-10

SDR family oxidoreductase;

Pssm-ID: 181198 [Multi-domain] Cd Length: 256 Bit Score: 59.33 E-value: 1.53e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALT 157
Cdd:PRK08017  78 LFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWS 157

                         90       100
                 ....*....|....*....|....
gi 498358419 158 ENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK08017 158 DALRMELRHSGIKVSLIEPGPIRT 181

PRK05867

SDR family oxidoreductase;

7-218

7.06e-10

SDR family oxidoreductase;

Pssm-ID: 135631 [Multi-domain] Cd Length: 253 Bit Score: 57.74 E-value: 7.06e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   7 VITGASAGIGAAIARAFSAAGHPLLLLARRVEPMQALNLPDT------LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVN 80
Cdd:PRK05867  13 LITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGtsggkvVPVCCDVSQHQQVTSMLDQVTAELGGIDIAVC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  81 NAGVMLLgQADVQDP-AEWQQMLNINVMGV-LNGVHAVLAGMKARRSGTIINISSIAGR-KTFPNHAA-YCATKFAVHAL 156
Cdd:PRK05867  93 NAGIITV-TPMLDMPlEEFQRLQNTNVTGVfLTAQAAAKAMVKQGQGGVIINTASMSGHiINVPQQVShYCASKAAVIHL 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358419 157 TENIREEVADVGVRMVTIAPGAVETELLSHTTDerikagYH-DWKDQ--MGGVIAPEVIADAVLY 218
Cdd:PRK05867 172 TKAMAVELAPHKIRVNSVSPGYILTELVEPYTE------YQpLWEPKipLGRLGRPEELAGLYLY 230

SDR_subfam_2

TIGR04504

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...

7-219

1.05e-09

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]

Pssm-ID: 275297 [Multi-domain] Cd Length: 259 Bit Score: 56.95 E-value: 1.05e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419    7 VITGASAGIGAAIARAFSAAGHPLLLL---------------ARRVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQ 71
Cdd:TIGR04504   5 LVTGAARGIGAATVRRLAADGWRVVAVdlcaddpavgyplatRAELDAVAAACPDQVLPVIADVRDPAALAAAVALAVER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   72 FGPVGCLVNNAGVMLLGQ-ADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKAR---RSGTIINISSIAGRKTFPNHAAYC 147
Cdd:TIGR04504  85 WGRLDAAVAAAGVIAGGRpLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARpdpRGGRFVAVASAAATRGLPHLAAYC 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358419  148 ATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAGYHDWKDQ--MGGVIAPEVIADAVLYA 219
Cdd:TIGR04504 165 AAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAATARLYGLTDVEEFAGHqlLGRLLEPEEVAAAVAWL 238

PRK06200

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

33-183

1.46e-09

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

Pssm-ID: 235739 [Multi-domain] Cd Length: 263 Bit Score: 56.50 E-value: 1.46e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  33 LARRVEPMQAL--NLPDTLCIGV-DVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAE-----WQQMLNI 104
Cdd:PRK06200  36 LERSAEKLASLrqRFGDHVLVVEgDVTSYADNQRAVDQTVDAFGKLDCFVGNAGIWDYNTSLVDIPAEtldtaFDEIFNV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 105 NVMGVLNGVHAVLAGMKARRsGTIINISSIAGrkTFPNHAA--YCATKFAVHALTENIREEVADVgVRMVTIAPGAVETE 182
Cdd:PRK06200 116 NVKGYLLGAKAALPALKASG-GSMIFTLSNSS--FYPGGGGplYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTD 191


                 .
gi 498358419 183 L 183
Cdd:PRK06200 192 L 192

PRK06701

short chain dehydrogenase; Provisional

70-183

1.49e-09

short chain dehydrogenase; Provisional

Pssm-ID: 235853 [Multi-domain] Cd Length: 290 Bit Score: 56.97 E-value: 1.49e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  70 AQFGPVGCLVNNAGVMLlGQADVQDPAE--WQQMLNINVMGVLNGVHAVLAGMKarRSGTIINISSIAGRKTFPNHAAYC 147
Cdd:PRK06701 120 RELGRLDILVNNAAFQY-PQQSLEDITAeqLDKTFKTNIYSYFHMTKAALPHLK--QGSAIINTGSITGYEGNETLIDYS 196

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 498358419 148 ATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK06701 197 ATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPL 232

PRK12384

sorbitol-6-phosphate dehydrogenase; Provisional

48-177

1.50e-09

sorbitol-6-phosphate dehydrogenase; Provisional

Pssm-ID: 183489 [Multi-domain] Cd Length: 259 Bit Score: 56.58 E-value: 1.50e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  48 TLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMG-VLNGVHAVLAGMKARRSG 126
Cdd:PRK12384  55 AYGFGADATSEQSVLALSRGVDEIFGRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGyFLCAREFSRLMIRDGIQG 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 498358419 127 TIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPG 177
Cdd:PRK12384 135 RIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLG 185

PRK08277

D-mannonate oxidoreductase; Provisional

6-182

2.35e-09

D-mannonate oxidoreductase; Provisional

Pssm-ID: 236216 [Multi-domain] Cd Length: 278 Bit Score: 56.06 E-value: 2.35e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   6 VVITGASAGIGAAIARAFSAAGHPLLLLARRVEPMQAL------NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLV 79
Cdd:PRK08277  13 AVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVvaeikaAGGEALAVKADVLDKESLEQARQQILEDFGPCDILI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  80 NNAG----------VMLLGQADVQ-----DPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHA 144
Cdd:PRK08277  93 NGAGgnhpkattdnEFHELIEPTKtffdlDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNAFTPLTKVP 172

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 498358419 145 AYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK08277 173 AYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210

PRK05993

SDR family oxidoreductase;

34-182

2.59e-09

SDR family oxidoreductase;

Pssm-ID: 180343 [Multi-domain] Cd Length: 277 Bit Score: 56.19 E-value: 2.59e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  34 ARRVEPMQALNLPDTLCIGVDVTDTAA-MKAAVAQAEAQFGPVGCLVNNAGvmlLGQAD-VQD-PAE-WQQMLNINVMGV 109
Cdd:PRK05993  35 CRKEEDVAALEAEGLEAFQLDYAEPESiAALVAQVLELSGGRLDALFNNGA---YGQPGaVEDlPTEaLRAQFEANFFGW 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358419 110 LNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK05993 112 HDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETR 184

PRK08324

bifunctional aldolase/short-chain dehydrogenase;

47-179

3.15e-09

bifunctional aldolase/short-chain dehydrogenase;

Pssm-ID: 236241 [Multi-domain] Cd Length: 681 Bit Score: 56.78 E-value: 3.15e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRS- 125
Cdd:PRK08324 471 RALGVACDVTDEAAVQAAFEEAALAFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLg 550

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 126 GTIINISS----IAGrktfPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAV 179
Cdd:PRK08324 551 GSIVFIASknavNPG----PNFGAYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAV 604

SDR_c8

cd08930

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...

44-179

3.86e-09

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: 55.42 E-value: 3.86e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  44 NLPDT--LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQA----DVqDPAEWQQMLNINVMGVLNGVHAVL 117
Cdd:cd08930   48 NLYKNrvIALELDITSKESIKELIESYLEKFGRIDILINNAYPSPKVWGsrfeEF-PYEQWNEVLNVNLGGAFLCSQAFI 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358419 118 AGMKARRSGTIINISSIAG---------RKTFP-NHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAV 179
Cdd:cd08930  127 KLFKKQGKGSIINIASIYGviapdfriyENTQMySPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGI 198

SDR_c10

cd05373

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...

20-223

5.07e-09

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: 55.08 E-value: 5.07e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  20 ARAFSAAGHPLLLLARRVEPMQAL-------NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADV 92
Cdd:cd05373   16 ARRFAAEGFSVALAARREAKLEALlvdiirdAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEVLVYNAGANVWFPILE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  93 QDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMV 172
Cdd:cd05373   96 TTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALAQSMARELGPKGIHVA 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498358419 173 -TIAPGAVETELLSHTTDERIKAGYHDwkdqmgGVIAPEVIADAVLYAWHQP 223
Cdd:cd05373  176 hVIIDGGIDTDFIRERFPKRDERKEED------GILDPDAIAEAYWQLHTQP 221

fabG

PRK05786

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

92-182

1.28e-08

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

Pssm-ID: 235608 [Multi-domain] Cd Length: 238 Bit Score: 53.61 E-value: 1.28e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  92 VQDPAEWQQMLNINVMGVLNGVHAVLAGMkaRRSGTIINISSIAG-RKTFPNHAAYCATKFAVHALTENIREEVADVGVR 170
Cdd:PRK05786  97 VEEFSGLEEMLTNHIKIPLYAVNASLRFL--KEGSSIVLVSSMSGiYKASPDQLSYAVAKAGLAKAVEILASELLGRGIR 174

                         90
                 ....*....|..
gi 498358419 171 MVTIAPGAVETE 182
Cdd:PRK05786 175 VNGIAPTTISGD 186

PRK08278

SDR family oxidoreductase;

49-235

4.14e-08

SDR family oxidoreductase;

Pssm-ID: 181349 [Multi-domain] Cd Length: 273 Bit Score: 52.60 E-value: 4.14e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:PRK08278  65 LPLVGDVRDEDQVAAAVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHI 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 129 INISS--IAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRM------VTIAPGAVETELLShttDERIKagyhDWK 200
Cdd:PRK08278 145 LTLSPplNLDPKWFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVnalwprTTIATAAVRNLLGG---DEAMR----RSR 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 498358419 201 DqmggviaPEVIADAVLYAWHQPA-----NVCVREIVLAA 235
Cdd:PRK08278 218 T-------PEIMADAAYEILSRPAreftgNFLIDEEVLRE 250

PRK06924

(S)-benzoin forming benzil reductase;

78-183

6.91e-08

(S)-benzoin forming benzil reductase;

Pssm-ID: 180753 [Multi-domain] Cd Length: 251 Bit Score: 51.61 E-value: 6.91e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAG-VMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARR-SGTIINISSIAGRKTFPNHAAYCATKFAVHA 155
Cdd:PRK06924  84 LINNAGmVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKvDKRVINISSGAAKNPYFGWSAYCSSKAGLDM 163

                         90       100       110
                 ....*....|....*....|....*....|
gi 498358419 156 LTENIREEVADV--GVRMVTIAPGAVETEL 183
Cdd:PRK06924 164 FTQTVATEQEEEeyPVKIVAFSPGVMDTNM 193

PRK08945

putative oxoacyl-(acyl carrier protein) reductase; Provisional

69-183

8.48e-08

putative oxoacyl-(acyl carrier protein) reductase; Provisional

Pssm-ID: 236357 [Multi-domain] Cd Length: 247 Bit Score: 51.41 E-value: 8.48e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  69 EAQFGPVGCLVNNAGVM-LLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYC 147
Cdd:PRK08945  87 EEQFGRLDGVLHNAGLLgELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYA 166

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 498358419 148 ATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK08945 167 VSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202

R1PA_ADH_SDR_c

cd08943

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...

42-217

9.37e-08

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: 51.24 E-value: 9.37e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  42 ALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMK 121
Cdd:cd08943   45 AQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMK 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 122 AR-RSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLshTTDERIKAGYHDWK 200
Cdd:cd08943  125 SQgIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLARCLALEGGEDGIRVNTVNPDAVFRGSK--IWEGVWRAARAKAY 202

                        170       180
                 ....*....|....*....|....*..
gi 498358419 201 DQ----------MGGVIAPEVIADAVL 217
Cdd:cd08943  203 GLleeeyrtrnlLKREVLPEDVAEAVV 229

BphB-like_SDR_c

cd05348

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...

70-184

1.25e-07

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: 51.20 E-value: 1.25e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  70 AQFGPVGCLVNNAGVMLLGQADVQDPAE-----WQQMLNINVMGVLNGVHAVLAGMKARRsGTIINISSIAGrkTFPNHA 144
Cdd:cd05348   74 ERFGKLDCFIGNAGIWDYSTSLVDIPEEkldeaFDELFHINVKGYILGAKAALPALYATE-GSVIFTVSNAG--FYPGGG 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 498358419 145 A--YCATKFAVHALTENIREEVADVgVRMVTIAPGAVETELL 184
Cdd:cd05348  151 GplYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLR 191

PRK07478

short chain dehydrogenase; Provisional

7-218

1.28e-07

short chain dehydrogenase; Provisional

Pssm-ID: 180993 [Multi-domain] Cd Length: 254 Bit Score: 51.08 E-value: 1.28e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   7 VITGASAGIGAAIARAFSAAGHPLLLLARRVEPMQALNLP------DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVN 80
Cdd:PRK07478  10 IITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEiraeggEAVALAGDVRDEAYAKALVALAVERFGGLDIAFN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  81 NAGVM-LLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKT-FPNHAAYCATKFAVHALTE 158
Cdd:PRK07478  90 NAGTLgEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAgFPGMAAYAASKAGLIGLTQ 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358419 159 NIREEVADVGVRMVTIAPGAVETELLSHTTDERIK----AGYHDWKDqmggVIAPEVIADAVLY 218
Cdd:PRK07478 170 VLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEAlafvAGLHALKR----MAQPEEIAQAALF 229

A3DFK9-like_SDR_c

cd09761

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...

46-224

1.62e-07

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: 50.66 E-value: 1.62e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  46 PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRs 125
Cdd:cd09761   47 PNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 126 GTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADvGVRMVTIAPGAVETELLSHTTDERIKAGYHDwKDQMGG 205
Cdd:cd09761  126 GRIINIASTRAFQSEPDSEAYAASKGGLVALTHALAMSLGP-DIRVNCISPGWINTTEQQEFTAAPLTQEDHA-QHPAGR 203

                        170
                 ....*....|....*....
gi 498358419 206 VIAPEVIADAVLYAWHQPA 224
Cdd:cd09761  204 VGTPKDIANLVLFLCQQDA 222

PRK08628

SDR family oxidoreductase;

46-183

1.82e-07

SDR family oxidoreductase;

Pssm-ID: 181508 [Multi-domain] Cd Length: 258 Bit Score: 50.34 E-value: 1.82e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  46 PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVmllgqadvQD-------PAEWQQMLNINVMGVLNGVHAVLA 118
Cdd:PRK08628  55 PRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGLVNNAGV--------NDgvgleagREAFVASLERNLIHYYVMAHYCLP 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 119 GMKARRsGTIINISSIAGRKTFPNHAAYCATKFAVHALTeniRE---EVADVGVRMVTIAPGAVETEL 183
Cdd:PRK08628 127 HLKASR-GAIVNISSKTALTGQGGTSGYAAAKGAQLALT---REwavALAKDGVRVNAVIPAEVMTPL 190

PRK12748

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

69-181

2.12e-07

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

Pssm-ID: 237189 [Multi-domain] Cd Length: 256 Bit Score: 50.46 E-value: 2.12e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  69 EAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCA 148
Cdd:PRK12748  90 SERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLGPMPDELAYAA 169

                         90       100       110
                 ....*....|....*....|....*....|...
gi 498358419 149 TKFAVHALTENIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK12748 170 TKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT 202

PRK06500

SDR family oxidoreductase;

46-218

2.15e-07

SDR family oxidoreductase;

Pssm-ID: 235816 [Multi-domain] Cd Length: 249 Bit Score: 50.34 E-value: 2.15e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  46 PDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAgMKARRS 125
Cdd:PRK06500  52 ESALVIRADAGDVAAQKALAQALAEAFGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLP-LLANPA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 126 GTIINiSSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHT--TDERIKAGYHDWKDQ- 202
Cdd:PRK06500 131 SIVLN-GSINAHIGMPNSSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLglPEATLDAVAAQIQALv 209

                        170
                 ....*....|....*..
gi 498358419 203 -MGGVIAPEVIADAVLY 218
Cdd:PRK06500 210 pLGRFGTPEEIAKAVLY 226

PRK07856

SDR family oxidoreductase;

19-183

2.74e-07

SDR family oxidoreductase;

Pssm-ID: 236116 [Multi-domain] Cd Length: 252 Bit Score: 49.93 E-value: 2.74e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  19 IARAFSAAGHPLLLLARRvEPMQALNLPDTLcIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEW 98
Cdd:PRK07856  22 IARAFLAAGATVVVCGRR-APETVDGRPAEF-HAADVRDPDQVAALVDAIVERHGRLDVLVNNAGGSPYALAAEASPRFH 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  99 QQMLNINVMGVLNGVHAVLAGMKARRS-GTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVAdVGVRMVTIAPG 177
Cdd:PRK07856 100 EKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNLTRSLAVEWA-PKVRVNAVVVG 178


                 ....*.
gi 498358419 178 AVETEL 183
Cdd:PRK07856 179 LVRTEQ 184

hydroxyacyl-CoA-like_DH_SDR_c-like

cd05353

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...

72-222

2.81e-07

(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: 50.01 E-value: 2.81e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  72 FGPVGCLVNNAGV----MLLGQADvqdpAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYC 147
Cdd:cd05353   86 FGRVDILVNNAGIlrdrSFAKMSE----EDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYS 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358419 148 ATKFAVHALTENIREEVADVGVRMVTIAPGAvETELLSHTTDERIKAGYHdwkdqmggviaPEVIADAVLYAWHQ 222
Cdd:cd05353  162 AAKLGLLGLSNTLAIEGAKYNITCNTIAPAA-GSRMTETVMPEDLFDALK-----------PEYVAPLVLYLCHE 224

DHPR_SDR_c_like

cd05334

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...

70-181

3.06e-07

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: 49.63 E-value: 3.06e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  70 AQFGPVGCLVNNAGVMLLGQADVQDPAE-WQQMLNINVMGVLNGVHAVLAGMKArrSGTIINISSIAGRKTFPNHAAYCA 148
Cdd:cd05334   64 RLSGKVDALICVAGGWAGGSAKSKSFVKnWDLMWKQNLWTSFIASHLATKHLLS--GGLLVLTGAKAALEPTPGMIGYGA 141

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 498358419 149 TKFAVHALTENIREE--VADVGVRMVTIAPGAVET 181
Cdd:cd05334  142 AKAAVHQLTQSLAAEnsGLPAGSTANAILPVTLDT 176

PRK08993

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

70-195

4.53e-07

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

Pssm-ID: 181605 [Multi-domain] Cd Length: 253 Bit Score: 49.49 E-value: 4.53e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  70 AQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKAR-RSGTIINISSIAGRKTFPNHAAYCA 148
Cdd:PRK08993  81 AEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMLSFQGGIRVPSYTA 160

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 498358419 149 TKFAVHALTENIREEVADVGVRMVTIAPGAVET---------ELLSHTTDERIKAG 195
Cdd:PRK08993 161 SKSGVMGVTRLMANEWAKHNINVNAIAPGYMATnntqqlradEQRSAEILDRIPAG 216

retinol-DH_like_SDR_c

cd09807

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...

78-187

4.60e-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: 49.39 E-value: 4.60e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMLLGQADVQDPAEWQqmLNINVMGVLNGVHAVLAGMKARRSGTIINISSIA------------GRKTFPNHAA 145
Cdd:cd09807   84 LINNAGVMRCPYSKTEDGFEMQ--FGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAhkagkinfddlnSEKSYNTGFA 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 498358419 146 YCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHT 187
Cdd:cd09807  162 YCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHT 203

PRK06128

SDR family oxidoreductase;

38-183

5.92e-07

SDR family oxidoreductase;

Pssm-ID: 180413 [Multi-domain] Cd Length: 300 Bit Score: 49.09 E-value: 5.92e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  38 EPMQALNLPDtlcigvDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGvmllGQADVQDPAE-----WQQMLNINVMGVLNG 112
Cdd:PRK06128 104 EGRKAVALPG------DLKDEAFCRQLVERAVKELGGLDILVNIAG----KQTAVKDIADitteqFDATFKTNVYAMFWL 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 113 VHAVLAGMKArrSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK06128 174 CKAAIPHLPP--GASIINTGSIQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242

haloalcohol_DH_SDR_c-like

cd05361

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...

113-182

1.13e-06

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: 47.96 E-value: 1.13e-06

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 113 VHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:cd05361  112 LQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSP 181

PRK05866

SDR family oxidoreductase;

6-189

1.28e-06

SDR family oxidoreductase;

Pssm-ID: 235631 [Multi-domain] Cd Length: 293 Bit Score: 48.20 E-value: 1.28e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   6 VVITGASAGIGAAIARAFSAAGHPLLLLARRVEPMQAL------NLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLV 79
Cdd:PRK05866  43 ILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVadritrAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  80 NNAGvmllgqADVQDPAE-----W---QQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS---IAGrkTFPNHAAYCA 148
Cdd:PRK05866 123 NNAG------RSIRRPLAesldrWhdvERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATwgvLSE--ASPLFSVYNA 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 498358419 149 TKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD 189
Cdd:PRK05866 195 SKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIAPTKA 235

PRK12746

SDR family oxidoreductase;

78-218

1.59e-06

SDR family oxidoreductase;

Pssm-ID: 183718 [Multi-domain] Cd Length: 254 Bit Score: 47.72 E-value: 1.59e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARrsGTIINISSIAGRKTFPNHAAYCATKFAVHALT 157
Cdd:PRK12746  94 LVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAEVRLGFTGSIAYGLSKGALNTMT 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358419 158 ENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAGYHDWKDQMGGVIAPEVIADAVLY 218
Cdd:PRK12746 172 LPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRNFATNSSVFGRIGQVEDIADAVAF 232

PRK06101

SDR family oxidoreductase;

99-188

2.33e-06

SDR family oxidoreductase;

Pssm-ID: 180399 [Multi-domain] Cd Length: 240 Bit Score: 47.17 E-value: 2.33e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  99 QQMLNINVMGVLNGVHAVLAGMKarRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGA 178
Cdd:PRK06101  96 ARVFNVNVLGVANCIEGIQPHLS--CGHRVVIVGSIASELALPRAEAYGASKAAVAYFARTLQLDLRPKGIEVVTVFPGF 173

                         90
                 ....*....|
gi 498358419 179 VETELLSHTT 188
Cdd:PRK06101 174 VATPLTDKNT 183

PLN02780

ketoreductase/ oxidoreductase

75-185

2.51e-06

ketoreductase/ oxidoreductase

Pssm-ID: 166421 [Multi-domain] Cd Length: 320 Bit Score: 47.55 E-value: 2.51e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  75 VGCLVNNAGVMLLGQADVQDPAE--WQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAGR--KTFPNHAAYCATK 150
Cdd:PLN02780 133 VGVLINNVGVSYPYARFFHEVDEelLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIviPSDPLYAVYAATK 212

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 498358419 151 FAVHALTENIREEVADVGVRMVTIAPGAVETELLS 185
Cdd:PLN02780 213 AYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMAS 247

3alpha_HSD_SDR_c

cd05328

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...

78-218

3.09e-06

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: 46.72 E-value: 3.09e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMllGQADVQDpaewqqMLNINVMGVLNGVHAVLAGMKARRSGTIINISSIAG--------------------- 136
Cdd:cd05328   64 LVNCAGVG--GTTVAGL------VLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGagwaqdklelakalaagtear 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 137 ------RKTFPNHAAYCATKFAVHALT-ENIREEVADVGVRMVTIAPGAVETELLSH-TTDERIKAGYHDWKDQMGGVIA 208
Cdd:cd05328  136 avalaeHAGQPGYLAYAGSKEALTVWTrRRAATWLYGAGVRVNTVAPGPVETPILQAfLQDPRGGESVDAFVTPMGRRAE 215

                        170
                 ....*....|
gi 498358419 209 PEVIADAVLY 218
Cdd:cd05328  216 PDEIAPVIAF 225

PRK12747

short chain dehydrogenase; Provisional

78-183

3.51e-06

short chain dehydrogenase; Provisional

Pssm-ID: 183719 [Multi-domain] Cd Length: 252 Bit Score: 46.61 E-value: 3.51e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  78 LVNNAGVMllGQADVQDPAE--WQQMLNINVMGVLNGVHAVLAgmKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHA 155
Cdd:PRK12747  92 LINNAGIG--PGAFIEETTEqfFDRMVSVNAKAPFFIIQQALS--RLRDNSRIINISSAATRISLPDFIAYSMTKGAINT 167

                         90       100
                 ....*....|....*....|....*...
gi 498358419 156 LTENIREEVADVGVRMVTIAPGAVETEL 183
Cdd:PRK12747 168 MTFTLAKQLGARGITVNAILPGFIKTDM 195

PRK07904

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

86-189

3.60e-06

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

Pssm-ID: 181162 [Multi-domain] Cd Length: 253 Bit Score: 46.62 E-value: 3.60e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  86 LLGQADV--QDPAEWQQMLNINV-----MGVLNGvhavlAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTE 158
Cdd:PRK07904  97 LLGDAEElwQNQRKAVQIAEINYtaavsVGVLLG-----EKMRAQGFGQIIAMSSVAGERVRRSNFVYGSTKAGLDGFYL 171

                         90       100       110
                 ....*....|....*....|....*....|.
gi 498358419 159 NIREEVADVGVRMVTIAPGAVETELLSHTTD 189
Cdd:PRK07904 172 GLGEALREYGVRVLVVRPGQVRTRMSAHAKE 202

HSDL2_SDR_c

cd09762

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...

49-224

5.05e-06

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

Pssm-ID: 187663 [Multi-domain] Cd Length: 243 Bit Score: 46.28 E-value: 5.05e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTI 128
Cdd:cd09762   62 LPCIVDIRDEDQVRAAVEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHI 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 129 INISS--IAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAP-GAVET---ELLSHTTDERIKAgyhdwkdq 202
Cdd:cd09762  142 LNLSPplNLNPKWFKNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWPrTAIATaamNMLGGVDVAACCR-------- 213

                        170       180
                 ....*....|....*....|..
gi 498358419 203 mggviAPEVIADAVLYAWHQPA 224
Cdd:cd09762  214 -----KPEIMADAAYAILTKPS 230

PRK07035

SDR family oxidoreductase;

15-218

6.08e-06

SDR family oxidoreductase;

Pssm-ID: 180802 [Multi-domain] Cd Length: 252 Bit Score: 46.16 E-value: 6.08e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  15 IGAAIARAFSAAGHPLLLLARRVEPMQAlnLPDTLC--------IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVM- 85
Cdd:PRK07035  20 IGEAIAKLLAQQGAHVIVSSRKLDGCQA--VADAIVaaggkaeaLACHIGEMEQIDALFAHIRERHGRLDILVNNAAANp 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  86 LLGQADVQDPAEWQQMLNINVMGVLngVHAVLAG--MKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREE 163
Cdd:PRK07035  98 YFGHILDTDLGAFQKTVDVNIRGYF--FMSVEAGklMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAAVISMTKAFAKE 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498358419 164 VADVGVRMVTIAPGAVETELLSH-TTDERIkagYHDWKDQ--MGGVIAPEVIADAVLY 218
Cdd:PRK07035 176 CAPFGIRVNALLPGLTDTKFASAlFKNDAI---LKQALAHipLRRHAEPSEMAGAVLY 230

sepiapter_red

TIGR01500

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...

77-219

6.50e-06

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.

Pssm-ID: 273660 [Multi-domain] Cd Length: 256 Bit Score: 46.06 E-value: 6.50e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   77 CLVNNAGVML---LGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSG--TIINISSIAGRKTFPNHAAYCATKF 151
Cdd:TIGR01500  90 LLINNAGTLGdvsKGFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGLnrTVVNISSLCAIQPFKGWALYCAGKA 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358419  152 AVHALTENIREEVADVGVRMVTIAPGAVETELLSH----TTDERIKAGYHDWKDQmGGVIAPEVIAD---AVLYA 219
Cdd:TIGR01500 170 ARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQvreeSVDPDMRKGLQELKAK-GKLVDPKVSAQkllSLLEK 243

PRK12481

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

71-182

7.98e-06

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

Pssm-ID: 171531 [Multi-domain] Cd Length: 251 Bit Score: 45.67 E-value: 7.98e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  71 QFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSG-TIINISSIAGRKTFPNHAAYCAT 149
Cdd:PRK12481  80 VMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNGgKIINIASMLSFQGGIRVPSYTAS 159

                         90       100       110
                 ....*....|....*....|....*....|...
gi 498358419 150 KFAVHALTENIREEVADVGVRMVTIAPGAVETE 182
Cdd:PRK12481 160 KSAVMGLTRALATELSQYNINVNAIAPGYMATD 192

PRK07677

short chain dehydrogenase; Provisional

49-180

1.10e-05

short chain dehydrogenase; Provisional

Pssm-ID: 181077 [Multi-domain] Cd Length: 252 Bit Score: 45.05 E-value: 1.10e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  49 LCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNInvmgVLNGV----HAVLAG-MKAR 123
Cdd:PRK07677  53 LTVQMDVRNPEDVQKMVEQIDEKFGRIDALINNAAGNFICPAEDLSVNGWNSVIDI----VLNGTfycsQAVGKYwIEKG 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358419 124 RSGTIINISSI----AGRKTFPNHAAycatKFAVHALTENIREEVA-DVGVRMVTIAPGAVE 180
Cdd:PRK07677 129 IKGNIINMVATyawdAGPGVIHSAAA----KAGVLAMTRTLAVEWGrKYGIRVNAIAPGPIE 186

PRK12743

SDR family oxidoreductase;

7-181

1.10e-05

SDR family oxidoreductase;

Pssm-ID: 237187 [Multi-domain] Cd Length: 256 Bit Score: 45.41 E-value: 1.10e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   7 VITGASAGIGAAIARAFSAAGHPLLLL-------ARRVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLV 79
Cdd:PRK12743   6 IVTASDSGIGKACALLLAQQGFDIGITwhsdeegAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRIDVLV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  80 NNAGVMLLGQADVQDPAEWQQMLNINVMGV-LNGVHAVLAGMKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTE 158
Cdd:PRK12743  86 NNAGAMTKAPFLDMDFDEWRKIFTVDVDGAfLCSQIAARHMVKQGQGGRIINITSVHEHTPLPGASAYTAAKHALGGLTK 165

                        170       180
                 ....*....|....*....|...
gi 498358419 159 NIREEVADVGVRMVTIAPGAVET 181
Cdd:PRK12743 166 AMALELVEHGILVNAVAPGAIAT 188

PRK05875

short chain dehydrogenase; Provisional

54-189

1.36e-05

short chain dehydrogenase; Provisional

Pssm-ID: 180300 [Multi-domain] Cd Length: 276 Bit Score: 45.18 E-value: 1.36e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  54 DVTDTAAMKAAVAQAEAQFGPVGCLVNNAG-VMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINIS 132
Cdd:PRK05875  66 DVTDEDQVARAVDAATAWHGRLHGVVHCAGgSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGIS 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498358419 133 SIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD 189
Cdd:PRK05875 146 SIAASNTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITE 202

PRK07985

SDR family oxidoreductase;

89-183

1.50e-05

SDR family oxidoreductase;

Pssm-ID: 181188 [Multi-domain] Cd Length: 294 Bit Score: 44.99 E-value: 1.50e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  89 QADVQDPA-----EWQQMLNINVMGVLNGVHAVLAGMKArrSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREE 163
Cdd:PRK07985 139 QVAIPDIAdltseQFQKTFAINVFALFWLTQEAIPLLPK--GASIITTSSIQAYQPSPHLLDYAATKAAILNYSRGLAKQ 216

                         90       100
                 ....*....|....*....|
gi 498358419 164 VADVGVRMVTIAPGAVETEL 183
Cdd:PRK07985 217 VAEKGIRVNIVAPGPIWTAL 236

SDH_SDR_c_like

cd05322

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...

47-177

2.87e-05

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

Pssm-ID: 187583 [Multi-domain] Cd Length: 257 Bit Score: 43.99 E-value: 2.87e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  47 DTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGM-KARRS 125
Cdd:cd05322   53 KAYGFGADATNEQSVIALSKGVDEIFKRVDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMiRDGIQ 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 498358419 126 GTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPG 177
Cdd:cd05322  133 GRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLG 184

PRK07791

short chain dehydrogenase; Provisional

52-178

3.25e-05

short chain dehydrogenase; Provisional

Pssm-ID: 236099 [Multi-domain] Cd Length: 286 Bit Score: 43.89 E-value: 3.25e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  52 GVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGV----MLLGQADvqdpAEWQQMLNINVMGvlngvHAVLAGMKARR--- 124
Cdd:PRK07791  70 GDDIADWDGAANLVDAAVETFGGLDVLVNNAGIlrdrMIANMSE----EEWDAVIAVHLKG-----HFATLRHAAAYwra 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358419 125 --------SGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGA 178
Cdd:PRK07791 141 eskagravDARIINTSSGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAA 202

Tthb094_like_SDR_c

cd11730

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...

6-183

3.72e-05

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: 43.28 E-value: 3.72e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   6 VVITGASAGIGAAIARAFSAAGHPLLLLARRVEPMQAlnLPDTLCIGVDVTDTAAMKAAVAQAEaQFGPVGCLVNNAGVM 85
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAG--LAAEVGALARPADVAAELEVWALAQ-ELGPLDLLVYAAGAI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  86 LLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAGMKArrSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVA 165
Cdd:cd11730   78 LGKPLARTKPAAWRRILDANLTGAALVLKHALALLAA--GARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVARKEVR 155

                        170
                 ....*....|....*...
gi 498358419 166 dvGVRMVTIAPGAVETEL 183
Cdd:cd11730  156 --GLRLTLVRPPAVDTGL 171

PRK05717

SDR family oxidoreductase;

51-181

4.24e-05

SDR family oxidoreductase;

Pssm-ID: 168204 [Multi-domain] Cd Length: 255 Bit Score: 43.34 E-value: 4.24e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  51 IGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVmllgqADVQDP-------AEWQQMLNINVMGVLNGVHAVLAGMKAR 123
Cdd:PRK05717  61 IAMDVADEAQVAAGVAEVLGQFGRLDALVCNAAI-----ADPHNTtleslslAHWNRVLAVNLTGPMLLAKHCAPYLRAH 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 124 RsGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIreeVADVG--VRMVTIAPGAVET 181
Cdd:PRK05717 136 N-GAIVNLASTRARQSEPDTEAYAASKGGLLALTHAL---AISLGpeIRVNAVSPGWIDA 191

PRK05876

short chain dehydrogenase; Provisional

7-193

4.49e-04

short chain dehydrogenase; Provisional

Pssm-ID: 135637 [Multi-domain] Cd Length: 275 Bit Score: 40.71 E-value: 4.49e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   7 VITGASAGIGAAIARAFSAAGHPLLL-------LARRVEPMQALNLpDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLV 79
Cdd:PRK05876  10 VITGGASGIGLATGTEFARRGARVVLgdvdkpgLRQAVNHLRAEGF-DVHGVMCDVRHREEVTHLADEAFRLLGHVDVVF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  80 NNAGVMLLGQADVQDPAEWQQMLNINVMGVLNGVHAVLAG-MKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTE 158
Cdd:PRK05876  89 SNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRlLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAE 168

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 498358419 159 NIREEVADVGVRMVTIAPGAVETELLSHTtdERIK 193
Cdd:PRK05876 169 TLAREVTADGIGVSVLCPMVVETNLVANS--ERIR 201

PRK06057

short chain dehydrogenase; Provisional

7-184

8.03e-04

short chain dehydrogenase; Provisional

Pssm-ID: 180371 [Multi-domain] Cd Length: 255 Bit Score: 39.71 E-value: 8.03e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   7 VITGASAGIGAAIARAFSAAG-HPLLLLARRVEPMQALNLPDTLCIGVDVTDTAAMKAAVAQAEAQFGPVGCLVNNAGVM 85
Cdd:PRK06057  11 VITGGGSGIGLATARRLAAEGaTVVVGDIDPEAGKAAADEVGGLFVPTDVTDEDAVNALFDTAAETYGSVDIAFNNAGIS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  86 LLGQADVQD--PAEWQQMLNINVMGVLNGVHAVLAGMKARRSGTIINISS-IAGRKTFPNHAAYCATKFAVHALTENIRE 162
Cdd:PRK06057  91 PPEDDSILNtgLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASfVAVMGSATSQISYTASKGGVLAMSRELGV 170

                        170       180
                 ....*....|....*....|..
gi 498358419 163 EVADVGVRMVTIAPGAVETELL 184
Cdd:PRK06057 171 QFARQGIRVNALCPGPVNTPLL 192

DHRS1-like_SDR_c

cd09763

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...

1-216

1.13e-03

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: 39.35 E-value: 1.13e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419   1 MSKSLVVITGASAGIGAAIARAFSAAGHPLLLLARRVEPmqalNLPDTL---------CIGVDV---TDTAAMKAAVAQA 68
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILP----QLPGTAeeiearggkCIPVRCdhsDDDEVEALFERVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  69 EAQFGPVGCLVNNA--GVMLLGQADVQ-----DPAEWQQMLNINVMGVL-NGVHAVLAgMKARRSGTIINISSIAGRKTF 140
Cdd:cd09763   77 REQQGRLDILVNNAyaAVQLILVGVAKpfweePPTIWDDINNVGLRAHYaCSVYAAPL-MVKAGKGLIVIISSTGGLEYL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498358419 141 PNhAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTDERIKAGYHDWKDQMGGVIAPEVIADAV 216
Cdd:cd09763  156 FN-VAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEGSWHAKERDAFLNGETTEYSGRCV 230

PRK08416

enoyl-ACP reductase;

120-194

1.93e-03

enoyl-ACP reductase;

Pssm-ID: 181417 [Multi-domain] Cd Length: 260 Bit Score: 38.60 E-value: 1.93e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498358419 120 MKARRSGTIINISSIAGRKTFPNHAAYCATKFAVHALTENIREEVADVGVRMVTIAPGAVETELLSHTTD-ERIKA 194
Cdd:PRK08416 139 MEKVGGGSIISLSSTGNLVYIENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNyEEVKA 214

PRK12428

coniferyl-alcohol dehydrogenase;

73-218

2.60e-03

coniferyl-alcohol dehydrogenase;

Pssm-ID: 237099 [Multi-domain] Cd Length: 241 Bit Score: 38.06 E-value: 2.60e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419  73 GPVGCLVNNAGVMllGQADVQDpaewqqMLNINVMGVLNGVHAVLAGMkaRRSGTIINISSIAGRK-------------- 138
Cdd:PRK12428  47 GRIDALFNIAGVP--GTAPVEL------VARVNFLGLRHLTEALLPRM--APGGAIVNVASLAGAEwpqrlelhkalaat 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358419 139 -TFPNHAAYCA------------TKFAVHALT-ENIREEVADVGVRMVTIAPGAVET----ELLSHTTDERIKAGYHdwk 200
Cdd:PRK12428 117 aSFDEGAAWLAahpvalatgyqlSKEALILWTmRQAQPWFGARGIRVNCVAPGPVFTpilgDFRSMLGQERVDSDAK--- 193

                        170
                 ....*....|....*...
gi 498358419 201 dQMGGVIAPEVIADAVLY 218
Cdd:PRK12428 194 -RMGRPATADEQAAVLVF 210

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