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Conserved domains on  [gi|738157197|ref|WP_036114533|]
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MULTISPECIES: SDR family oxidoreductase [Gammaproteobacteria]

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
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]; ...
6-244 1.35e-95

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: 279.76  E-value: 1.35e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   6 SETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:COG4221    2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:COG4221   79 RLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 166 RAISDGLRQETDA--IRVTLVSPGVVESELADHITDETARAAMREFRRI-ALPQEPVAQAIAYAIEQPAGVDISELIVRP 242
Cdd:COG4221  159 RGLSESLRAELRPtgIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLePLTPEDVAEAVLFALTQPAHVNVNELVLRP 238

                 ..
gi 738157197 243 VA 244
Cdd:COG4221  239 TA 240
 
Name Accession Description Interval E-value
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
6-244 1.35e-95

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: 279.76  E-value: 1.35e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   6 SETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:COG4221    2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:COG4221   79 RLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 166 RAISDGLRQETDA--IRVTLVSPGVVESELADHITDETARAAMREFRRI-ALPQEPVAQAIAYAIEQPAGVDISELIVRP 242
Cdd:COG4221  159 RGLSESLRAELRPtgIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLePLTPEDVAEAVLFALTQPAHVNVNELVLRP 238

                 ..
gi 738157197 243 VA 244
Cdd:COG4221  239 TA 240
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
12-231 1.06e-66

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: 206.37  E-value: 1.06e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALAtELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDALI 91
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA-AIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISDG 171
Cdd:cd05233   80 NNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRS 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 172 LRQET--DAIRVTLVSPGVVESELADHITDETARAAMRE---FRRIALPQEpVAQAIAYAIEQPA 231
Cdd:cd05233  160 LALELapYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAaipLGRLGTPEE-VAEAVVFLASDEA 223
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
10-194 1.45e-58

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 183.97  E-value: 1.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160
                         170       180
                  ....*....|....*....|....*..
gi 738157197  170 DGLRQE--TDAIRVTLVSPGVVESELA 194
Cdd:pfam00106 161 RSLALElaPHGIRVNAVAPGGVDTDMT 187
PRK07454 PRK07454
SDR family oxidoreductase;
9-244 3.10e-54

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 174.76  E-value: 3.10e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK07454   6 MPRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK07454  86 VLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAF 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 169 SDGLRQE--TDAIRVTLVSPGVVESELADhitDETARAamrEFRRIA-LPQEPVAQAIAYAIEQPAGVDISELIVRPVA 244
Cdd:PRK07454 166 TKCLAEEerSHGIRVCTITLGAVNTPLWD---TETVQA---DFDRSAmLSPEQVAQTILHLAQLPPSAVIEDLTLMPSA 238
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
12-225 3.38e-40

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 138.50  E-value: 3.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   12 VILTGASSGIGEATARHLSRKGHHLFI-GARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDAL 90
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIItYRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   91 INNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISD 170
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTK 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  171 GLRQE--TDAIRVTLVSPGVVESELADHITDETaRAAMREF---RRIALPQEpVAQAIAY 225
Cdd:TIGR01830 161 SLAKElaSRNITVNAVAPGFIDTDMTDKLSEKV-KKKILSQiplGRFGQPEE-VANAVAF 218
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
10-123 6.83e-16

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 72.90  E-value: 6.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197    10 KVVILTGASSGIGEATARHLSRKG--HHLFIGARRI--EKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGarRLVLLSRSGPdaPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEG 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 738157197    86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLH 123
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWN 118
 
Name Accession Description Interval E-value
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
6-244 1.35e-95

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: 279.76  E-value: 1.35e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   6 SETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:COG4221    2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:COG4221   79 RLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 166 RAISDGLRQETDA--IRVTLVSPGVVESELADHITDETARAAMREFRRI-ALPQEPVAQAIAYAIEQPAGVDISELIVRP 242
Cdd:COG4221  159 RGLSESLRAELRPtgIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLePLTPEDVAEAVLFALTQPAHVNVNELVLRP 238

                 ..
gi 738157197 243 VA 244
Cdd:COG4221  239 TA 240
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
8-230 2.18e-74

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 226.29  E-value: 2.18e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:COG0300   84 DVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEG 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 168 ISDGLRQETDA--IRVTLVSPGVVESELadhitdeTARAAMREFRRIALPQEpVAQAIAYAIEQP 230
Cdd:COG0300  164 FSESLRAELAPtgVRVTAVCPGPVDTPF-------TARAGAPAGRPLLSPEE-VARAILRALERG 220
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
12-231 1.06e-66

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: 206.37  E-value: 1.06e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALAtELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDALI 91
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA-AIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISDG 171
Cdd:cd05233   80 NNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRS 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 172 LRQET--DAIRVTLVSPGVVESELADHITDETARAAMRE---FRRIALPQEpVAQAIAYAIEQPA 231
Cdd:cd05233  160 LALELapYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAaipLGRLGTPEE-VAEAVVFLASDEA 223
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
8-244 5.04e-66

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: 204.69  E-value: 5.04e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd08934    2 QGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:cd08934   82 DILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 168 ISDGLRQET--DAIRVTLVSPGVVESELADHITDE-TARAAMREFRRI-ALPQEPVAQAIAYAIEQPAGVDISELIVRPV 243
Cdd:cd08934  162 FSEGLRQEVteRGVRVVVIEPGTVDTELRDHITHTiTKEAYEERISTIrKLQAEDIAAAVRYAVTAPHHVTVNEILIRPT 241

                 .
gi 738157197 244 A 244
Cdd:cd08934  242 D 242
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
10-232 1.00e-65

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: 204.25  E-value: 1.00e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:COG1028    7 KVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLDI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:COG1028   87 LVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLT 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 170 DGLRQE--TDAIRVTLVSPGVVESELADHI-TDETARAAMRE---FRRIALPQEpVAQAIAYAIEQPAG 232
Cdd:COG1028  167 RSLALElaPRGIRVNAVAPGPIDTPMTRALlGAEEVREALAAripLGRLGTPEE-VAAAVLFLASDAAS 234
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
10-244 1.35e-62

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: 196.35  E-value: 1.35e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRA-TGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAkFPVKVLPLQLDVSDRESIEAALENLPEEFRDID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAG-VMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:cd05346   81 ILVNNAGlALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 168 ISDGLRQETDA--IRVTLVSPGVVESELAD---HITDETARAAMREFrrIALPQEPVAQAIAYAIEQPAGVDISELIVRP 242
Cdd:cd05346  161 FSLNLRKDLIGtgIRVTNIEPGLVETEFSLvrfHGDKEKADKVYEGV--EPLTPEDIAETILWVASRPAHVNINDIEIMP 238

                 ..
gi 738157197 243 VA 244
Cdd:cd05346  239 VN 240
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
10-231 2.26e-59

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: 187.82  E-value: 2.26e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALAtelRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd05374    1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLG---ELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:cd05374   78 LVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALS 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 170 DGLRQETDA--IRVTLVSPGVVESELADHIT---------------DETARAAMREFRRIALPQEPVAQAIAYAIEQPA 231
Cdd:cd05374  158 ESLRLELAPfgIKVTIIEPGPVRTGFADNAAgsaledpeispyapeRKEIKENAAGVGSNPGDPEKVADVIVKALTSES 236
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
10-194 1.45e-58

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 183.97  E-value: 1.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160
                         170       180
                  ....*....|....*....|....*..
gi 738157197  170 DGLRQE--TDAIRVTLVSPGVVESELA 194
Cdd:pfam00106 161 RSLALElaPHGIRVNAVAPGGVDTDMT 187
PRK07454 PRK07454
SDR family oxidoreductase;
9-244 3.10e-54

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 174.76  E-value: 3.10e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK07454   6 MPRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK07454  86 VLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAF 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 169 SDGLRQE--TDAIRVTLVSPGVVESELADhitDETARAamrEFRRIA-LPQEPVAQAIAYAIEQPAGVDISELIVRPVA 244
Cdd:PRK07454 166 TKCLAEEerSHGIRVCTITLGAVNTPLWD---TETVQA---DFDRSAmLSPEQVAQTILHLAQLPPSAVIEDLTLMPSA 238
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
10-229 1.71e-51

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: 168.15  E-value: 1.71e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGG-NVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd05332    4 KVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGApSPHVVPLDMSDLEDAEQVVEEALKLFGGLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:cd05332   84 ILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGF 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 169 SDGLRQET--DAIRVTLVSPGVVESELADHITDETARAAMREFRRIA--LPQEPVAQAIAYAIEQ 229
Cdd:cd05332  164 FDSLRAELsePNISVTVVCPGLIDTNIAMNALSGDGSMSAKMDDTTAngMSPEECALEILKAIAL 228
PRK06182 PRK06182
short chain dehydrogenase; Validated
9-247 3.99e-51

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 167.83  E-value: 3.99e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALAtelrATGgnVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK06182   3 KKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLA----SLG--VHPLSLDVTDEASIKAAVDTIIAEEGRID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK06182  77 VLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 169 SDGLRQETDA--IRVTLVSPGVVESELADHITD---ETARAAmrefrrialPQEPVAQAIAYAIEQPAGVD-------IS 236
Cdd:PRK06182 157 SDALRLEVAPfgIDVVVIEPGGIKTEWGDIAADhllKTSGNG---------AYAEQAQAVAASMRSTYGSGrlsdpsvIA 227
                        250
                 ....*....|.
gi 738157197 237 ELIVRPVASPH 247
Cdd:PRK06182 228 DAISKAVTARR 238
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
8-242 3.87e-50

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: 164.61  E-value: 3.87e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATG-GNVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:cd05343    5 RGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGyPTLFPYQCDLSNEEQILSMFSAIRTQHQG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY--GHIINIASTGAYTV--SPTAAVYCASK 162
Cdd:cd05343   85 VDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSMSGHRVppVSVFHFYAATK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 163 FAVRAISDGLRQE----TDAIRVTLVSPGVVESELADHITDETARAAMREFRRI-ALPQEPVAQAIAYAIEQPAGVDISE 237
Cdd:cd05343  165 HAVTALTEGLRQElreaKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIpCLKPEDVANAVLYVLSTPPHVQIHD 244

                 ....*
gi 738157197 238 LIVRP 242
Cdd:cd05343  245 ILLRP 249
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
10-232 6.87e-50

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 163.83  E-value: 6.87e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLT-ALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK05557   6 KVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAeALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK05557  86 ILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGVIGF 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 169 SDGLRQE--TDAIRVTLVSPGVVESELADHITDETARA--AMREFRRIALPQEpVAQAIAYAIEQPAG 232
Cdd:PRK05557 166 TKSLARElaSRGITVNAVAPGFIETDMTDALPEDVKEAilAQIPLGRLGQPEE-IASAVAFLASDEAA 232
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
8-225 5.16e-49

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 161.48  E-value: 5.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGAL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK05653  84 DILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIG 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738157197 168 ISDGLRQET--DAIRVTLVSPGVVESELADHITDETARAAMRE--FRRIALPQEpVAQAIAY 225
Cdd:PRK05653 164 FTKALALELasRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEipLGRLGQPEE-VANAVAF 224
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-225 1.70e-48

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 160.01  E-value: 1.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIG-ARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK05565   6 KVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKID 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK05565  86 ILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAVNAF 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197 169 SDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMRE--FRRIALPQEpVAQAIAY 225
Cdd:PRK05565 166 TKALAKElaPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEipLGRLGKPEE-IAKVVLF 225
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-225 4.46e-48

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 158.88  E-value: 4.46e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGAR-RIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK12825   7 RVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRID 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK12825  87 ILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGLVGL 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197 169 SDGLRQE--TDAIRVTLVSPGVVESELADHITDE--TARAAMREFRRIALPQEpVAQAIAY 225
Cdd:PRK12825 167 TKALARElaEYGITVNMVAPGDIDTDMKEATIEEarEAKDAETPLGRSGTPED-IARAVAF 226
FabG-like PRK07231
SDR family oxidoreductase;
10-225 1.64e-47

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 157.68  E-value: 1.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA-GGRAIAVAADVSDEADVEAAVAAALERFGSVDI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPL-SPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK07231  85 LVNNAGTTHRnGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITL 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 169 SDGLRQE--TDAIRVTLVSPGVVESELADH---ITDETARAAMRE---FRRIALPQEpVAQAIAY 225
Cdd:PRK07231 165 TKALAAElgPDKIRVNAVAPVVVETGLLEAfmgEPTPENRAKFLAtipLGRLGTPED-IANAALF 228
PRK07109 PRK07109
short chain dehydrogenase; Provisional
8-230 1.51e-46

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 157.78  E-value: 1.51e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK07109   7 GRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGPI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK07109  87 DTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRG 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 168 ISDGLRQETDA----IRVTLVSPGVVESELADHitdetARAAM-REFRRIALPQEP--VAQAIAYAIEQP 230
Cdd:PRK07109 167 FTDSLRCELLHdgspVSVTMVQPPAVNTPQFDW-----ARSRLpVEPQPVPPIYQPevVADAILYAAEHP 231
PRK07326 PRK07326
SDR family oxidoreductase;
6-242 1.52e-45

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 152.09  E-value: 1.52e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   6 SETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNN-KGNVLGLAADVRDEADVQRAVDAIVAAFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK07326  82 GLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTNFFAGGAAYNASKFGL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVESELADHITDEtaraamREFRRIAlpQEPVAQAIAYAIEQPAGVDISELIVRP 242
Cdd:PRK07326 161 VGFSEAAMLDlrQYGIKVSTIMPGSVATHFNGHTPSE------KDAWKIQ--PEDIAQLVLDLLKMPPRTLPSKIEVRP 231
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
11-230 4.94e-44

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: 148.30  E-value: 4.94e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  11 VVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDAL 90
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  91 INNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISD 170
Cdd:cd05360   82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTE 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 171 GLRQETD----AIRVTLVSPGVVESELADHitdetarAAMREFRRIALPQ-----EPVAQAIAYAIEQP 230
Cdd:cd05360  162 SLRAELAhdgaPISVTLVQPTAMNTPFFGH-------ARSYMGKKPKPPPpiyqpERVAEAIVRAAEHP 223
PRK06180 PRK06180
short chain dehydrogenase; Provisional
6-228 1.83e-43

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 148.14  E-value: 1.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   6 SETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:PRK06180   1 MSSMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALH---PDRALARLLDVTDFDAIDAVVADAEATFG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAG-----VMPLSPLAALKveewnRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCA 160
Cdd:PRK06180  78 PIDVLVNNAGyghegAIEESPLAEMR-----RQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 161 SKFAVRAISDGLRQETD--AIRVTLVSPG----------VVESE--LADHitDETA--RAAMREFRRIALPQEPV--AQA 222
Cdd:PRK06180 153 SKFALEGISESLAKEVApfGIHVTAVEPGsfrtdwagrsMVRTPrsIADY--DALFgpIRQAREAKSGKQPGDPAkaAQA 230

                 ....*.
gi 738157197 223 IAYAIE 228
Cdd:PRK06180 231 ILAAVE 236
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-194 1.85e-43

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 146.76  E-value: 1.85e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   6 SETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:PRK07666   4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK07666  84 SIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGV 163
                        170       180       190
                 ....*....|....*....|....*....|.
gi 738157197 166 RAISDGLRQET--DAIRVTLVSPGVVESELA 194
Cdd:PRK07666 164 LGLTESLMQEVrkHNIRVTALTPSTVATDMA 194
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
12-212 2.04e-43

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: 146.71  E-value: 2.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDALI 91
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISDG 171
Cdd:cd05350   81 INAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAES 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738157197 172 LRQE--TDAIRVTLVSPGVVESELADHITD-----ETARAAMREFRRI 212
Cdd:cd05350  161 LRYDvkKRGIRVTVINPGFIDTPLTANMFTmpflmSVEQAAKRIYKAI 208
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
10-231 1.15e-42

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: 145.14  E-value: 1.15e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTAlaTELRATGGNVDA--MAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAA--AELQAINPKVKAtfVQCDVTSWEQLAAAFKKAIEKFGRV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVM-PLSPLAALKVEE-WNRMLDVNVRGVLHGIAAVLPIM---QEQGYGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:cd05323   79 DILINNAGILdEKSYLFAGKLPPpWEKTIDVNLTGVINTTYLALHYMdknKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 163 FAV----RAISDGLRQETDaIRVTLVSPGVVESELadhITDETARAAMREFRRIALPQEPVAQAIAYAIEQPA 231
Cdd:cd05323  159 HGVvgftRSLADLLEYKTG-VRVNAICPGFTNTPL---LPDLVAKEAEMLPSAPTQSPEVVAKAIVYLIEDDE 227
PRK07825 PRK07825
short chain dehydrogenase; Provisional
8-194 1.36e-42

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 145.47  E-value: 1.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratgGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK07825   4 RGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL----GLVVGGPLDVTDPASFAAFLDAVEADLGPI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK07825  80 DVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVG 159
                        170       180
                 ....*....|....*....|....*....
gi 738157197 168 ISDGLRQETD--AIRVTLVSPGVVESELA 194
Cdd:PRK07825 160 FTDAARLELRgtGVHVSVVLPSFVNTELI 188
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
10-232 1.37e-42

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: 144.61  E-value: 1.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197 170 DGLRQETDA--IRVTLVSPGVVESELADHITDETARAAMRE--FRRIALPQEpVAQAIAYAIEQPAG 232
Cdd:cd05333  161 KSLAKELASrgITVNAVAPGFIDTDMTDALPEKVKEKILKQipLGRLGTPEE-VANAVAFLASDDAS 226
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
10-241 4.93e-42

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: 142.89  E-value: 4.93e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALatelRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAAL----SASGGDVEAVPYDARDPEDARALVDALRDRFGRIDV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:cd08932   77 LVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197 170 DGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMrefrRIALPQEpVAQAIAYAIEQPAGvdISELIVR 241
Cdd:cd08932  157 HALRQEgwDHGVRVSAVCPGFVDTPMAQGLTLVGAFPPE----EMIQPKD-IANLVRMVIELPEN--ITSVAVL 223
PRK07063 PRK07063
SDR family oxidoreductase;
10-217 7.58e-42

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 143.27  E-value: 7.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRA--TGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARdvAGARVLAVPADVTDAASVAAAVAAAEEAFGPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK07063  88 DVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAKHGLLG 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 168 ISDGLRQETDA--IRVTLVSPGVVESELA--------DHITDETARAAMREFRRIALPQE 217
Cdd:PRK07063 168 LTRALGIEYAArnVRVNAIAPGYIETQLTedwwnaqpDPAAARAETLALQPMKRIGRPEE 227
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
10-192 2.05e-41

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: 141.62  E-value: 2.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRA----TGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:cd08939    2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAeanaSGQKVSYISADLSDYEEVEQAFAQAVEKGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:cd08939   82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFAL 161
                        170       180
                 ....*....|....*....|....*....
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVESE 192
Cdd:cd08939  162 RGLAESLRQElkPYNIRVSVVYPPDTDTP 190
PRK12826 PRK12826
SDR family oxidoreductase;
8-225 2.46e-41

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 141.59  E-value: 2.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAS-TGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK12826  85 DILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSvAGPRVGYPGLAHYAASKAGLV 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMRefRRIALPQ----EPVAQAIAY 225
Cdd:PRK12826 165 GFTRALALElaARNITVNSVHPGGVDTPMAGNLGDAQWAEAIA--AAIPLGRlgepEDIAAAVLF 227
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
19-225 1.16e-40

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: 139.49  E-value: 1.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   19 SGIGEATARHLSRKGHHLF---IGARRIEKLTALATELratggNVDAMAIDVTRPEDLQRIAARALEKHGRIDALINNAG 95
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVltdLNEALAKRVEELAEEL-----GAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   96 VMPL--SPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQgyGHIINIASTGAYTVSPTAAVYCASKFAVRAISDGLR 173
Cdd:pfam13561  81 FAPKlkGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLA 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197  174 QE--TDAIRVTLVSPGVVESELADHITD-ETARAAMRE---FRRIALPQEpVAQAIAY 225
Cdd:pfam13561 159 VElgPRGIRVNAISPGPIKTLAASGIPGfDELLAAAEArapLGRLGTPEE-VANAAAF 215
PRK12939 PRK12939
short chain dehydrogenase; Provisional
3-226 1.75e-40

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 139.34  E-value: 1.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   3 TVVSETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALE 82
Cdd:PRK12939   1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  83 KHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:PRK12939  81 ALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 163 FAVRAISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMREFRRIALPQEP--VAQAIAYA 226
Cdd:PRK12939 161 GAVIGMTRSLARElgGRGITVNAIAPGLTATEATAYVPADERHAYYLKGRALERLQVPddVAGAVLFL 228
PRK07832 PRK07832
SDR family oxidoreductase;
10-228 2.17e-40

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 139.79  E-value: 2.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNV-DAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVpEHRALDISDYDAVAAFAADIHAAHGSMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK07832  81 VVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRgGHLVNVSSAAGLVALPWHAAYSASKFGLRG 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESELADHI-------TDETARAAMREFRRIALPQEPVAQAIAYAIE 228
Cdd:PRK07832 161 LSEVLRFDlaRHGIGVSVVVPGAVKTPLVNTVeiagvdrEDPRVQKWVDRFRGHAVTPEKAAEKILAGVE 230
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
12-225 3.38e-40

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 138.50  E-value: 3.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   12 VILTGASSGIGEATARHLSRKGHHLFI-GARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDAL 90
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIItYRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   91 INNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISD 170
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSGRIINISSVVGLMGNAGQANYAASKAGVIGFTK 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  171 GLRQE--TDAIRVTLVSPGVVESELADHITDETaRAAMREF---RRIALPQEpVAQAIAY 225
Cdd:TIGR01830 161 SLAKElaSRNITVNAVAPGFIDTDMTDKLSEKV-KKKILSQiplGRFGQPEE-VANAVAF 218
PRK08219 PRK08219
SDR family oxidoreductase;
10-243 6.36e-40

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 137.37  E-value: 6.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRkGHHLFIGARRIEKLTALATELRatggNVDAMAIDVTRPEDLqriaARALEKHGRIDA 89
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELAAELP----GATPFPVDLTDPEAI----AAAVEQLGRLDV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK08219  75 LVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAASKFALRALA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 170 DGLRQ-ETDAIRVTLVSPGVVESELADHITDETAraamREFR-RIALPQEPVAQAIAYAIEQPAGVDISELIVRPV 243
Cdd:PRK08219 154 DALREeEPGNVRVTSVHPGRTDTDMQRGLVAQEG----GEYDpERYLRPETVAKAVRFAVDAPPDAHITEVVVRPR 225
PRK05855 PRK05855
SDR family oxidoreductase;
10-244 1.04e-39

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 144.35  E-value: 1.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK05855 316 KLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDI 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK05855 396 VVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTgGHIVNVASAAAYAPSRSLPAYATSKAAVLML 475
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 169 SDGLRQETDA--IRVTLVSPGVVESELADHI----TDETARAAMRE-----FRRIALPQEPVAQAIAYAIEQpagvdisE 237
Cdd:PRK05855 476 SECLRAELAAagIGVTAICPGFVDTNIVATTrfagADAEDEARRRGradklYQRRGYGPEKVAKAIVDAVKR-------N 548

                 ....*..
gi 738157197 238 LIVRPVA 244
Cdd:PRK05855 549 KAVVPVT 555
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
6-223 1.28e-39

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 137.10  E-value: 1.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   6 SETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:cd05347    2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:cd05347   82 KIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGV 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMREFR----RIALPQEPVAQAI 223
Cdd:cd05347  162 AGLTKALATEwaRHGIQVNAIAPGYFATEMTEAVVADPEFNDDILKRipagRWGQPEDLVGAAV 225
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
10-225 1.45e-39

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: 137.40  E-value: 1.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd05344    2 KVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:cd05344   82 LVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGLV 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197 170 DGLRQE--TDAIRVTLVSPGVVESE-----LADH-----ITDETARAAMRE---FRRIALPQEpVAQAIAY 225
Cdd:cd05344  162 KTLSRElaPDGVTVNSVLPGYIDTErvrrlLEARaekegISVEEAEKEVASqipLGRVGKPEE-LAALIAF 231
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
10-242 3.26e-39

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: 135.71  E-value: 3.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRatgGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQEL---EGVLGLAGDVRDEADVRRAVDAMEEAFGGLDA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLD-VNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:cd08929   78 LVNNAGVGVMKPVEELTPEEWRLVLDtNLTGAFYCIHKAAPALLRRGG-GTIVNVGSLAGKNAFKGGAAYNASKFGLLGL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 169 SDGLRQE--TDAIRVTLVSPGVVESELADHITDETARaamrefrriaLPQEPVAQAIAYAIEQPAGVDISELIVRP 242
Cdd:cd08929  157 SEAAMLDlrEANIRVVNVMPGSVDTGFAGSPEGQAWK----------LAPEDVAQAVLFALEMPARALVSRIELRP 222
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
11-198 3.30e-39

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 135.83  E-value: 3.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  11 VVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDAL 90
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  91 INNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISD 170
Cdd:cd05339   81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHE 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 738157197 171 GLRQETDA-----IRVTLVSPGVVESELADHIT 198
Cdd:cd05339  161 SLRLELKAygkpgIKTTLVCPYFINTGMFQGVK 193
PRK06179 PRK06179
short chain dehydrogenase; Provisional
8-189 4.48e-39

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 136.57  E-value: 4.48e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATelratggnVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPG--------VELLELDVTDDASVQAAVDEVIARAGRI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK06179  75 DVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVEG 154
                        170       180
                 ....*....|....*....|....
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVV 189
Cdd:PRK06179 155 YSESLDHEvrQFGIRVSLVEPAYT 178
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
9-225 5.18e-39

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: 135.97  E-value: 5.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEK-LTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEaAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGI-AAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:cd05366   82 DVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIqAAARQFKKLGHGGKIINASSIAGVQGFPNLGAYSASKFAVR 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAA-------MREF-RRIAL--PQEP--VAQAIAY 225
Cdd:cd05366  162 GLTQTAAQElaPKGITVNAYAPGIVKTEMWDYIDEEVGEIAgkpegegFAEFsSSIPLgrLSEPedVAGLVSF 234
PRK06181 PRK06181
SDR family oxidoreductase;
10-228 2.34e-38

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 134.34  E-value: 2.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK06181   2 KVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEW-NRMLDVNVRGVLHGIAAVLPIMQEQgYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK06181  82 LVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKHALHGF 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 169 SDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAA----MREfRRIALPQEpVAQAIAYAIE 228
Cdd:PRK06181 161 FDSLRIElaDDGVAVTVVCPGFVATDIRKRALDGDGKPLgkspMQE-SKIMSAEE-CAEAILPAIA 224
PRK08267 PRK08267
SDR family oxidoreductase;
10-230 4.14e-38

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 133.52  E-value: 4.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHhlFIGARRIEK--LTALATELraTGGNVDAMAIDVTRPEDLQRIAAR-ALEKHGR 86
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGW--RVGAYDINEagLAALAAEL--GAGNAWTGALDVTDRAAWDAALADfAAATGGR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK08267  78 LDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVR 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMREFRRIALPQEpVAQAIAYAIEQP 230
Cdd:PRK08267 158 GLTEALDLEwrRHGIRVADVMPLFVDTAMLDGTSNEVDAGSTKRLGVRLTPED-VAEAVWAAVQHP 222
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
10-223 8.68e-38

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: 131.80  E-value: 8.68e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHhlFIGARRIEK--LTALATELRAtgGNVDAMAIDVTRPEDL-QRIAARALEKHGR 86
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGW--FVGLYDIDEdgLAALAAELGA--ENVVAGALDVTDRAAWaAALADFAAATGGR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:cd08931   77 LDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 167 AISDGLRQETDA--IRVTLVSPGVVESELADHITDEtarAAMREFRRIALPQEPVAQAI 223
Cdd:cd08931  157 GLTEALDVEWARhgIRVADVWPWFVDTPILTKGETG---AAPKKGLGRVLPVSDVAKVV 212
PRK09072 PRK09072
SDR family oxidoreductase;
9-229 2.23e-37

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 131.99  E-value: 2.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtGGNVDAMAIDVTRPEDLQRIAARALEkHGRID 88
Cdd:PRK09072   5 DKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPY-PGRHRWVVADLTSEAGREAVLARARE-MGGIN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK09072  83 VLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRGF 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 169 SDGLRQETDA--IRVTLVSPGVVESELadhiTDETARAAMREFRRIALPQEPVAQAIAYAIEQ 229
Cdd:PRK09072 163 SEALRRELADtgVRVLYLAPRATRTAM----NSEAVQALNRALGNAMDDPEDVAAAVLQAIEK 221
PRK06914 PRK06914
SDR family oxidoreductase;
10-187 3.57e-37

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 131.68  E-value: 3.57e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATG--GNVDAMAIDVTRPEDLQRIAArALEKHGRI 87
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNlqQNIKVQQLDVTDQNSIHNFQL-VLKEIGRI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK06914  83 DLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYALEG 162
                        170       180
                 ....*....|....*....|..
gi 738157197 168 ISDGLRQETDA--IRVTLVSPG 187
Cdd:PRK06914 163 FSESLRLELKPfgIDVALIEPG 184
PRK06841 PRK06841
short chain dehydrogenase; Provisional
8-225 8.45e-37

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 130.16  E-value: 8.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK06841  14 SGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLL---GGNAKGLVCDVSDSQSVEAAVAAVISAFGRI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK06841  91 DILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGVVG 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMREF---RRIALPQEpVAQAIAY 225
Cdd:PRK06841 171 MTKVLALEwgPYGITVNAISPTVVLTELGKKAWAGEKGERAKKLipaGRFAYPEE-IAAAALF 232
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
10-204 1.41e-36

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 129.62  E-value: 1.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK12429   5 KVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVDI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK12429  85 LVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIGLT 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 738157197 170 DGLRQET--DAIRVTLVSPGVVESELADHITDETARA 204
Cdd:PRK12429 165 KVVALEGatHGVTVNAICPGYVDTPLVRKQIPDLAKE 201
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
8-225 1.77e-36

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: 129.04  E-value: 1.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd05341    4 KGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAEL---GDAARFFHLDVTDEDGWTAVVDTAREAFGRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:cd05341   81 DVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197 168 ISDG----LRQETDAIRVTLVSPGVVESELADHITDETARAAMREFRRIALPQEP--VAQAIAY 225
Cdd:cd05341  161 LTKSaaleCATQGYGIRVNSVHPGYIYTPMTDELLIAQGEMGNYPNTPMGRAGEPdeIAYAVVY 224
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
10-228 2.10e-36

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: 128.99  E-value: 2.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELR-ATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd05352    9 KVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAkKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGKID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTV--SPTAAVYCASKFAVR 166
Cdd:cd05352   89 ILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVnrPQPQAAYNASKAAVI 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESELADHITDET--ARAAMREFRRIALPQEPVAQAIAYAIE 228
Cdd:cd05352  169 HLAKSLAVEwaKYFIRVNSISPGYIDTDLTDFVDKELrkKWESYIPLKRIALPEELVGAYLYLASD 234
PRK05650 PRK05650
SDR family oxidoreductase;
12-195 2.41e-36

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 129.39  E-value: 2.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDALI 91
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISDG 171
Cdd:PRK05650  83 NNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSET 162
                        170       180
                 ....*....|....*....|....*.
gi 738157197 172 LRQE--TDAIRVTLVSPGVVESELAD 195
Cdd:PRK05650 163 LLVElaDDEIGVHVVCPSFFQTNLLD 188
PRK08263 PRK08263
short chain dehydrogenase; Provisional
7-208 3.79e-36

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 129.00  E-value: 3.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   7 ETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:PRK08263   1 MMEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKY---GDRLLPLALDVTDRAAVFAAVETAVEHFGR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK08263  78 LDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALE 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738157197 167 AISDGLRQETDA--IRVTLVSPGVVESEL----ADHITDETARAAMRE 208
Cdd:PRK08263 158 GMSEALAQEVAEfgIKVTLVEPGGYSTDWagtsAKRATPLDAYDTLRE 205
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
12-232 5.80e-36

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: 127.47  E-value: 5.80e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTA-LATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDAL 90
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAeVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  91 INNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISD 170
Cdd:cd05359   81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 171 GLRQET--DAIRVTLVSPGVVESELADHITD-ETARAAMRE---FRRIALPQEpVAQAIAYAIEQPAG 232
Cdd:cd05359  161 YLAVELgpRGIRVNAVSPGVIDTDALAHFPNrEDLLEAAAAntpAGRVGTPQD-VADAVGFLCSDAAR 227
PRK07774 PRK07774
SDR family oxidoreductase;
8-206 6.40e-36

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 127.55  E-value: 6.40e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK07774   5 DDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNA---GVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSptaAVYCASKFA 164
Cdd:PRK07774  85 DYLVNNAaiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYS---NFYGLAKVG 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 738157197 165 VRAISDGLRQETDA--IRVTLVSPGVVESELADHITDETARAAM 206
Cdd:PRK07774 162 LNGLTQQLARELGGmnIRVNAIAPGPIDTEATRTVTPKEFVADM 205
PRK06138 PRK06138
SDR family oxidoreductase;
10-225 1.46e-35

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 126.80  E-value: 1.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK06138   6 RVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA-GGRAFARQGDVGSAEAVEALVDFVAARWGRLDV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK06138  85 LVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIASLT 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 170 DGLRQE--TDAIRVTLVSPGVVESELADHITDETA-RAAMREFRRIALPQ------EPVAQAIAY 225
Cdd:PRK06138 165 RAMALDhaTDGIRVNAVAPGTIDTPYFRRIFARHAdPEALREALRARHPMnrfgtaEEVAQAALF 229
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
7-194 2.11e-35

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: 126.50  E-value: 2.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   7 ETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:cd08945    1 QDSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPI--MQEQGYGHIINIASTGAYTVSPTAAVYCASKFA 164
Cdd:cd08945   81 IDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHG 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 738157197 165 VRAISD--GLRQETDAIRVTLVSPGVVESELA 194
Cdd:cd08945  161 VVGFTKalGLELARTGITVNAVCPGFVETPMA 192
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
12-232 2.61e-35

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 126.04  E-value: 2.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLfIGARRIEkltalaTELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDALI 91
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATV-IALDLPF------VLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISD- 170
Cdd:cd05331   74 NCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKc 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 171 -GLRQETDAIRVTLVSPGVVESEL------ADHITDETARAAMREFR------RIALPQEpVAQAIAYAIEQPAG 232
Cdd:cd05331  154 lGLELAPYGVRCNVVSPGSTDTAMqrtlwhDEDGAAQVIAGVPEQFRlgiplgKIAQPAD-IANAVLFLASDQAG 227
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
8-225 2.70e-35

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 126.38  E-value: 2.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK08643  81 NVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHgGKIINATSQAGVVGNPELAVYSSTKFAVR 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAA-------MREF-RRIALPQ----EPVAQAIAY 225
Cdd:PRK08643 161 GLTQTAARDlaSEGITVNAYAPGIVKTPMMFDIAHQVGENAgkpdewgMEQFaKDITLGRlsepEDVANCVSF 233
PRK05693 PRK05693
SDR family oxidoreductase;
10-196 4.35e-35

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 126.06  E-value: 4.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALAtelrATGGNvdAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALA----AAGFT--AVQLDVNDGAALARLAEELEAEHGGLDV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEqGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK05693  76 LINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRR-SRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALS 154
                        170       180
                 ....*....|....*....|....*....
gi 738157197 170 DGLRQETD--AIRVTLVSPGVVESELADH 196
Cdd:PRK05693 155 DALRLELApfGVQVMEVQPGAIASQFASN 183
PRK07035 PRK07035
SDR family oxidoreductase;
8-225 6.26e-35

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 125.13  E-value: 6.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK07035   7 TGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMP-LSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK07035  87 DILVNNAAANPyFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAAVI 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESELADHIT--DETARAAMRE--FRRIALPQEpVAQAIAY 225
Cdd:PRK07035 167 SMTKAFAKEcaPFGIRVNALLPGLTDTKFASALFknDAILKQALAHipLRRHAEPSE-MAGAVLY 230
PRK06139 PRK06139
SDR family oxidoreductase;
10-191 6.88e-35

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 127.14  E-value: 6.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK06139   8 AVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAASFGGRIDV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK06139  88 WVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLRGFS 167
                        170       180
                 ....*....|....*....|....*
gi 738157197 170 DGLRQE-TD--AIRVTLVSPGVVES 191
Cdd:PRK06139 168 EALRGElADhpDIHVCDVYPAFMDT 192
PRK07201 PRK07201
SDR family oxidoreductase;
10-198 1.37e-34

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 130.46  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDY 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAG------VMplspLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKF 163
Cdd:PRK07201 452 LVNNAGrsirrsVE----NSTDRFHDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNAPRFSAYVASKA 527
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 738157197 164 AVRAISDglrqetdairvtlvspgVVESE-LADHIT 198
Cdd:PRK07201 528 ALDAFSD-----------------VAASEtLSDGIT 546
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
1-193 1.42e-34

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: 124.12  E-value: 1.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   1 MKTvvseTSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratgGNVDAMAIDVTRPEDLQRIAARA 80
Cdd:COG3967    1 MKL----TGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAAN----PGLHTIVLDVADPASIAALAEQV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  81 LEKHGRIDALINNAGVMPLSPL--AALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVY 158
Cdd:COG3967   73 TAEFPDLNVLINNAGIMRAEDLldEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTY 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 738157197 159 CASKFAVRAISDGLRQ--ETDAIRVTLVSPGVVESEL 193
Cdd:COG3967  153 SATKAALHSYTQSLRHqlKDTSVKVIELAPPAVDTDL 189
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
10-225 1.66e-34

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: 123.92  E-value: 1.66e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIG-ARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd05362    4 KVALVTGASRGIGRAIAKRLARDGASVVVNyASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQgyGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:cd05362   84 ILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG--GRIINISSSLTAAYTPNYGAYAGSKAAVEAF 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738157197 169 SDGLRQETDA--IRVTLVSPGVVESEL-ADHITDET--ARAAMREFRRIALPqEPVAQAIAY 225
Cdd:cd05362  162 TRVLAKELGGrgITVNAVAPGPVDTDMfYAGKTEEAveGYAKMSPLGRLGEP-EDIAPVVAF 222
PRK06172 PRK06172
SDR family oxidoreductase;
10-225 2.28e-34

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 123.71  E-value: 2.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK06172   8 KVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLDY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGV-MPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK06172  88 AFNNAGIeIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHAVIGL 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197 169 --SDGLRQETDAIRVTLVSPGVVESELADHITDETAR-----AAMREFRRIALPQEpVAQAIAY 225
Cdd:PRK06172 168 tkSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEADPRkaefaAAMHPVGRIGKVEE-VASAVLY 230
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
10-225 9.20e-34

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: 122.11  E-value: 9.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFI------GARRIekltalateLRATGGNVDAMAIDVTRPEDLQRIAARALEK 83
Cdd:cd05345    6 KVAIVTGAGSGFGEGIARRFAQEGARVVIadinadGAERV---------AADIGEAAIAIQADVTKRADVEAMVEAALSK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  84 HGRIDALINNAGVMPLS-PLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:cd05345   77 FGRLDILVNNAGITHRNkPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197 163 FAVRAISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMREFR------RIALPQEpVAQAIAY 225
Cdd:cd05345  157 GWVVTATKAMAVElaPRNIRVNCLCPVAGETPLLSMFMGEDTPENRAKFRatiplgRLSTPDD-IANAALY 226
PRK05872 PRK05872
short chain dehydrogenase; Provisional
10-229 1.01e-33

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 123.16  E-value: 1.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAiDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK05872  10 KVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLTVVA-DVTDLAAMQAAAEEAVERFGGIDV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK05872  89 VVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPGMAAYCASKAGVEAFA 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 170 DGLRQET--DAIRVTLVSPGVVESELADHITDETarAAMREFR-------RIALPQEPVAQAIAYAIEQ 229
Cdd:PRK05872 168 NALRLEVahHGVTVGSAYLSWIDTDLVRDADADL--PAFRELRarlpwplRRTTSVEKCAAAFVDGIER 234
PRK07478 PRK07478
short chain dehydrogenase; Provisional
10-225 1.95e-33

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 121.19  E-value: 1.95e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK07478   7 KVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGGLDI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVS-PTAAVYCASKFAVRA 167
Cdd:PRK07478  87 AFNNAGTLgEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGfPGMAAYAASKAGLIG 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197 168 ISDGLRQETDA--IRVTLVSPGVVESELADHIT-DETARAAMREF---RRIALPQEpVAQAIAY 225
Cdd:PRK07478 167 LTQVLAAEYGAqgIRVNALLPGGTDTPMGRAMGdTPEALAFVAGLhalKRMAQPEE-IAQAALF 229
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
9-232 2.52e-33

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 121.03  E-value: 2.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLfIGARRIEKLTALATELR--ATGGNVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:PRK12824   2 KKIALVTGAKRGIGSAIARELLNDGYRV-IATYFSGNDCAKDWFEEygFTEDQVRLKELDVTDTEECAEALAEIEEEEGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK12824  81 VDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 167 AISDGLRQET--DAIRVTLVSPGVVESELADHITDETAR--AAMREFRRIALPQEpVAQAIAYAIEQPAG 232
Cdd:PRK12824 161 GFTKALASEGarYGITVNCIAPGYIATPMVEQMGPEVLQsiVNQIPMKRLGTPEE-IAAAVAFLVSEAAG 229
PRK12937 PRK12937
short chain dehydrogenase; Provisional
7-225 6.74e-33

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 119.85  E-value: 6.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   7 ETSKVVILTGASSGIGEATARHLSRKGHHLFIG-ARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMqEQGyGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK12937  83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL-GQG-GRIINLSTSVIALPLPGYGPYAASKAAV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 166 RAISDGLRQET--DAIRVTLVSPGVVESELADHITDETARAAMRE---FRRIALPQEpVAQAIAY 225
Cdd:PRK12937 161 EGLVHVLANELrgRGITVNAVAPGPVATELFFNGKSAEQIDQLAGlapLERLGTPEE-IAAAVAF 224
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
11-243 1.38e-32

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 119.09  E-value: 1.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  11 VVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDAL 90
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDEL---GDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  91 INNAGV-MPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK10538  79 VNNAGLaLGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 170 DGLRqeTD----AIRVTLVSPGVV---ESELADHITDEtARAAMREFRRIALPQEPVAQAIAYAIEQPAGVDISELIVRP 242
Cdd:PRK10538 159 LNLR--TDlhgtAVRVTDIEPGLVggtEFSNVRFKGDD-GKAEKTYQNTVALTPEDVSEAVWWVATLPAHVNINTLEMMP 235

                 .
gi 738157197 243 V 243
Cdd:PRK10538 236 V 236
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
10-203 3.35e-32

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 118.30  E-value: 3.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIgarrieklTALATELRAT-------GGNVDAMAIDVTRPEDLQRIAARALE 82
Cdd:PRK06935  16 KVAIVTGGNTGLGQGYAVALAKAGADIII--------TTHGTNWDETrrliekeGRKVTFVQVDLTKPESAEKVVKEALE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  83 KHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAS----TGAYTVSPtaavY 158
Cdd:PRK06935  88 EFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASmlsfQGGKFVPA----Y 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 738157197 159 CASKFAVRAISDGLRQETDA--IRVTLVSPGVVESELADHITDETAR 203
Cdd:PRK06935 164 TASKHGVAGLTKAFANELAAynIQVNAIAPGYIKTANTAPIRADKNR 210
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
10-225 3.86e-32

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: 117.90  E-value: 3.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGG---NVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:cd05364    4 KVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVsekKILLVVADLTEEEGQDRIISTTLAKFGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAV- 165
Cdd:cd05364   84 LDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYCISKAALd 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197 166 ---RAISDGLRQEtdAIRVTLVSPGVVESELADHI-TDETARAAMREFR-------RIALPQEpVAQAIAY 225
Cdd:cd05364  163 qftRCTALELAPK--GVRVNSVSPGVIVTGFHRRMgMPEEQYIKFLSRAkethplgRPGTVDE-VAEAIAF 230
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
10-197 5.01e-32

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 117.82  E-value: 5.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK07067   7 KVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEI---GPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYG-HIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK07067  84 LFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGgKIINMASQAGRRGEALVSHYCATKAAVISY 163
                        170       180       190
                 ....*....|....*....|....*....|.
gi 738157197 169 --SDGLRQETDAIRVTLVSPGVVESELADHI 197
Cdd:PRK07067 164 tqSAALALIRHGINVNAIAPGVVDTPMWDQV 194
PRK06194 PRK06194
hypothetical protein; Provisional
10-195 7.08e-32

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 118.19  E-value: 7.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK06194   7 KVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQG------YGHIINIASTGAYTVSPTAAVYCASKF 163
Cdd:PRK06194  87 LFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAekdpayEGHIVNTASMAGLLAPPAMGIYNVSKH 166
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 738157197 164 AVRAISDG----LRQETDAIRVTLVSPGVVESELAD 195
Cdd:PRK06194 167 AVVSLTETlyqdLSLVTDQVGASVLCPYFVPTGIWQ 202
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
10-214 9.61e-32

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: 116.18  E-value: 9.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKG-HHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAStgayTVSPTAAVYCASKFAVRA 167
Cdd:cd05324   81 ILVNNAGIAfKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSS----GLGSLTSAYGVSKAALNA 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMREFRRIAL 214
Cdd:cd05324  157 LTRILAKElkETGIKVNACCPGWVKTDMGGGKAPKTPEEGAETPVYLAL 205
PRK06398 PRK06398
aldose dehydrogenase; Validated
8-246 2.20e-31

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 116.08  E-value: 2.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTAlatelratggnVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK06398   5 KDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYND-----------VDYFKVDVSNKEQVIKGIDYVISKYGRI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK06398  74 DILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVLG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 168 ISDGLRQE-TDAIRVTLVSPGVVESELAD------------HITDETAR-AAMREFRRIALPQEpVAQAIAYAIEQPAG- 232
Cdd:PRK06398 154 LTRSIAVDyAPTIRCVAVCPGSIRTPLLEwaaelevgkdpeHVERKIREwGEMHPMKRVGKPEE-VAYVVAFLASDLASf 232
                        250       260
                 ....*....|....*....|.
gi 738157197 233 -------VDISELIVRPVASP 246
Cdd:PRK06398 233 itgecvtVDGGLRALIPLSTP 253
PRK05866 PRK05866
SDR family oxidoreductase;
8-169 2.22e-31

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 117.15  E-value: 2.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK05866  39 TGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGV 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAAlKVEEWN---RMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYT-VSPTAAVYCASKF 163
Cdd:PRK05866 119 DILINNAGRSIRRPLAE-SLDRWHdveRTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATWGVLSeASPLFSVYNASKA 197

                 ....*.
gi 738157197 164 AVRAIS 169
Cdd:PRK05866 198 ALSAVS 203
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
10-193 4.29e-31

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 115.24  E-value: 4.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARR--IEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAAGANIVLNGFGdaAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGGV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:cd08940   83 DILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVVG 162
                        170       180
                 ....*....|....*....|....*...
gi 738157197 168 ISD--GLRQETDAIRVTLVSPGVVESEL 193
Cdd:cd08940  163 LTKvvALETAGTGVTCNAICPGWVLTPL 190
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
8-206 4.41e-31

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 114.33  E-value: 4.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTalatELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd05370    4 TGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLA----EAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALK--VEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:cd05370   80 DILINNAGIQRPIDLRDPAsdLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAAL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 738157197 166 RAISDGLRQ--ETDAIRVTLVSPGVVESEL--ADHITDETARAAM 206
Cdd:cd05370  160 HSYTLALRHqlKDTGVEVVEIVPPAVDTELheERRNPDGGTPRKM 204
PRK12829 PRK12829
short chain dehydrogenase; Provisional
1-239 7.67e-31

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 114.77  E-value: 7.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   1 MKTVVSETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELraTGGNVDAMAIDVTRPEDLQRIAARA 80
Cdd:PRK12829   3 IDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARL--PGAKVTATVADVADPAQVERVFDTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  81 LEKHGRIDALINNAGV-MPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYG-HIINIASTGAYTVSPTAAVY 158
Cdd:PRK12829  81 VERFGGLDVLVNNAGIaGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGgVIIALSSVAGRLGYPGRTPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 159 CASKFAVRAISDGLRQET--DAIRVTLVSPGVVESELADHITDETARAAMREFRRIAlpQEPVAQAIAYAIEQPAgvDIS 236
Cdd:PRK12829 161 AASKWAVVGLVKSLAIELgpLGIRVNAILPGIVRGPRMRRVIEARAQQLGIGLDEME--QEYLEKISLGRMVEPE--DIA 236

                 ...
gi 738157197 237 ELI 239
Cdd:PRK12829 237 ATA 239
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
10-193 1.19e-30

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 113.47  E-value: 1.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGG-NVDAMAIDVT-RPEDLQRIaaRALEKHGRI 87
Cdd:cd05356    2 TWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGvETKTIAADFSaGDDIYERI--EKELEGLDI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMP--LSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:cd05356   80 GILVNNVGISHsiPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFL 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVESEL 193
Cdd:cd05356  160 DFFSRALYEEykSQGIDVQSLLPYLVATKM 189
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
10-236 1.40e-30

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 114.24  E-value: 1.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGN--VDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd05327    2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNakVEVIQLDLSSLASVRQFAEEFLARFPRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMplSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAStGAYTVSP-------------- 153
Cdd:cd05327   82 DILINNAGIM--APPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSS-IAHRAGPidfndldlennkey 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 154 -TAAVYCASKFAV----RAISDGLrqETDAIRVTLVSPGVVESEL-ADHITDETARAAMREFrrIALPQEPVAQAIAYAI 227
Cdd:cd05327  159 sPYKAYGQSKLANilftRELARRL--EGTGVTVNALHPGVVRTELlRRNGSFFLLYKLLRPF--LKKSPEQGAQTALYAA 234

                 ....*....
gi 738157197 228 EQPAGVDIS 236
Cdd:cd05327  235 TSPELEGVS 243
PRK06198 PRK06198
short chain dehydrogenase; Provisional
8-233 2.43e-30

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 113.56  E-value: 2.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKG-HHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:PRK06198   5 DGKVALVTGGTQGLGAAIARAFAERGaAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK06198  85 LDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAAYCASKGAL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 166 raisDGLRQET------DAIRVTLVSPGVVESELADHITDET---------ARAAMREFRRIALPQEpVAQAIAYAIEQP 230
Cdd:PRK06198 165 ----ATLTRNAayallrNRIRVNGLNIGWMATEGEDRIQREFhgapddwleKAAATQPFGRLLDPDE-VARAVAFLLSDE 239

                 ...
gi 738157197 231 AGV 233
Cdd:PRK06198 240 SGL 242
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
10-223 2.78e-30

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 113.06  E-value: 2.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLfIGARRiekltalaTELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFVEAGAKV-IGFDQ--------AFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLDV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK08220  80 LVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSLA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 170 D--GLRQETDAIRVTLVSPGVVESELADHI--TDETARAAMREF----------RRIALPQEpVAQAI 223
Cdd:PRK08220 160 KcvGLELAPYGVRCNVVSPGSTDTDMQRTLwvDEDGEQQVIAGFpeqfklgiplGKIARPQE-IANAV 226
PRK07775 PRK07775
SDR family oxidoreductase;
12-244 3.29e-30

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 113.31  E-value: 3.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDALI 91
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISDG 171
Cdd:PRK07775  93 SGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTN 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 172 LRQETD--AIRVTLVSPGVVESELADHITDETARAAMREFRRIALPQEP-------VAQAIAYAIEQPAGVDISELIVRP 242
Cdd:PRK07775 173 LQMELEgtGVRASIVHPGPTLTGMGWSLPAEVIGPMLEDWAKWGQARHDyflrasdLARAITFVAETPRGAHVVNMEVQP 252

                 ..
gi 738157197 243 VA 244
Cdd:PRK07775 253 EA 254
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
8-232 4.25e-30

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: 112.61  E-value: 4.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAI--DVTRPEDLQRIAARALEKHG 85
Cdd:cd05330    2 KDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIkaDVSDEAQVEAYVDATVEQFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFA 164
Cdd:cd05330   82 RIDGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 165 VRAIS--DGLRQETDAIRVTLVSPGVVESELAD----HITDETARAAMREF------RRIALPQEpVAQAIAYAIEQPAG 232
Cdd:cd05330  162 VVGLTrnSAVEYGQYGIRINAIAPGAILTPMVEgslkQLGPENPEEAGEEFvsvnpmKRFGEPEE-VAAVVAFLLSDDAG 240
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
8-225 7.17e-30

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 112.09  E-value: 7.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGAR-RIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:cd05358    2 KGKVALVTGASSGIGKAIAIRLATAGANVVVNYRsKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFGT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQ-GYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:cd05358   82 LDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSkIKGKIINMSSVHEKIPWPGHVNYAASKGGV 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 166 RAISDGLRQET--DAIRVTLVSPGVVESEL-ADHITDETARAA---MREFRRIALPQEpVAQAIAY 225
Cdd:cd05358  162 KMMTKTLAQEYapKGIRVNAIAPGAINTPInAEAWDDPEQRADllsLIPMGRIGEPEE-IAAAAAW 226
PRK08251 PRK08251
SDR family oxidoreductase;
8-218 1.75e-29

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 110.80  E-value: 1.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAT--GGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:PRK08251   1 TRQKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEFRDELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTA-AVYCASKFA 164
Cdd:PRK08251  81 GLDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGVkAAYAASKAG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 165 VRAISDGLRQETD--AIRVTLVSPGVVESELADHITD-------ETARAAM-----REFRRIALPQEP 218
Cdd:PRK08251 161 VASLGEGLRAELAktPIKVSTIEPGYIRSEMNAKAKStpfmvdtETGVKALvkaieKEPGRAAVPWWP 228
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
8-240 2.08e-29

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: 110.71  E-value: 2.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd08936    9 ANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPL-SPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:cd08936   89 DILVSNAAVNPFfGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKTALL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 167 AISDGLRQETDA--IRVTLVSPGVVESELADHI-TDETARAAMRE---FRRIALPQEpVAQAIAYAIEQPAGVDISELIV 240
Cdd:cd08936  169 GLTKNLAPELAPrnIRVNCLAPGLIKTSFSSALwMDKAVEESMKEtlrIRRLGQPED-CAGIVSFLCSEDASYITGETVV 247
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
10-203 2.11e-29

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 111.14  E-value: 2.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIM-QEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK13394  88 LVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGL 167
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 738157197 169 SDGLRQETDAIRVT--LVSPGVVESELADHITDETAR 203
Cdd:PRK13394 168 ARVLAKEGAKHNVRshVVCPGFVRTPLVDKQIPEQAK 204
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
8-217 2.12e-29

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 111.05  E-value: 2.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRiEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK08226   5 TGKTALITGALQGIGEGIARVFARHGANLILLDIS-PEIEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAS-TGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK08226  84 DILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSvTGDMVADPGETAYALTKAAIV 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESELADHITDE----------TARAAMREFRRIALPQE 217
Cdd:PRK08226 164 GLTKSLAVEyaQSGIRVNAICPGYVRTPMAESIARQsnpedpesvlTEMAKAIPLRRLADPLE 226
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
10-225 2.48e-29

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: 110.37  E-value: 2.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGN-VDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd05369    4 KVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGrAHPIQCDVRDPEAVEAAVDETLKEFGKID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLP-IMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:cd05369   84 ILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKrLIEAKHGGSILNISATYAYTGSPFQVHSAAAKAGVDA 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESE--LADHITDETARAAMRE---FRRIALPQEpVAQAIAY 225
Cdd:cd05369  164 LTRSLAVEwgPYGIRVNAIAPGPIPTTegMERLAPSGKSEKKMIErvpLGRLGTPEE-IANLALF 227
PRK07890 PRK07890
short chain dehydrogenase; Provisional
10-225 4.46e-29

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 110.05  E-value: 4.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK07890   6 KVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMP-LSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK07890  86 LVNNAFRVPsMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHSQPKYGAYKMAKGALLAA 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 169 SDGLRQE--TDAIRVTLVSP-------------------GVVESELADHITDETAraamreFRRIALPQEpVAQAIAY 225
Cdd:PRK07890 165 SQSLATElgPQGIRVNSVAPgyiwgdplkgyfrhqagkyGVTVEQIYAETAANSD------LKRLPTDDE-VASAVLF 235
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
8-187 4.59e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 110.04  E-value: 4.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK08213  11 SGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVL---HGIAAVLpiMQEQGYGHIINIAST----GAYTVSPTAAVYCA 160
Cdd:PRK08213  91 DILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFllsQAVAKRS--MIPRGYGRIINVASVaglgGNPPEVMDTIAYNT 168
                        170       180
                 ....*....|....*....|....*....
gi 738157197 161 SKFAVRAISDGLRQE--TDAIRVTLVSPG 187
Cdd:PRK08213 169 SKGAVINFTRALAAEwgPHGIRVNAIAPG 197
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
10-203 1.02e-28

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: 108.86  E-value: 1.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd05363    4 KTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEI---GPAACAISLDVTDQASIDRCVAALVDRWGSIDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:cd05363   81 LVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRgGKIINMASQAGRRGEALVGVYCATKAAVISL 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 738157197 169 --SDGLRQETDAIRVTLVSPGVVESELADHITDETAR 203
Cdd:cd05363  161 tqSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKFAR 197
PRK12828 PRK12828
short chain dehydrogenase; Provisional
10-225 1.37e-28

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 108.35  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAmaIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGG--IDLVDPQAARRAVDEVNRQFGRLDA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK12828  86 LVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVARLT 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 170 DGLRQE--TDAIRVTLVSPGVVESeladhitdETARAAM--REFRRIALPQEpVAQAIAY 225
Cdd:PRK12828 166 EALAAEllDRGITVNAVLPSIIDT--------PPNRADMpdADFSRWVTPEQ-IAAVIAF 216
PRK08589 PRK08589
SDR family oxidoreductase;
8-225 1.41e-28

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 109.10  E-value: 1.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRiEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK08589   5 ENKVAVITGASTGIGQASAIALAQEGAYVLAVDIA-EAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVmplsPLAALKVEE-----WNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:PRK08589  84 DVLFNNAGV----DNAAGRIHEypvdvFDKIMAVDMRGTFLMTKMLLPLMMEQG-GSIINTSSFSGQAADLYRSGYNAAK 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197 163 FAV----RAISdgLRQETDAIRVTLVSPGVVESELADHITDETARAAMREFR----------RIALPQEpVAQAIAY 225
Cdd:PRK08589 159 GAVinftKSIA--IEYGRDGIRANAIAPGTIETPLVDKLTGTSEDEAGKTFRenqkwmtplgRLGKPEE-VAKLVVF 232
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
8-232 1.91e-28

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 108.08  E-value: 1.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK12936   5 SGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAEL---GERVKIFPANLSDRDEVKALGQKAEADLEGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK12936  82 DILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIG 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMREF--RRIALPQEpVAQAIAYAIEQPAG 232
Cdd:PRK12936 162 FSKSLAQEiaTRNVTVNCVAPGFIESAMTGKLNDKQKEAIMGAIpmKRMGTGAE-VASAVAYLASSEAA 229
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
10-230 2.62e-28

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: 107.93  E-value: 2.62e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSR---KGHHLFIGARRIEKLTALATELRAT-GGNVDAMAIDVTRPEDLQriAARALEKHG 85
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLKKKGRLWEAAGALaGGTLETLQLDVCDSKSVA--AAVERVTER 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:cd09806   79 HVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 166 RAISDGLRQETDA--IRVTLVSPGVVESELADHITDETARA--------AMREFRRIALP----------QEP--VAQAI 223
Cdd:cd09806  159 EGLCESLAVQLLPfnVHLSLIECGPVHTAFMEKVLGSPEEVldrtaddiTTFHFFYQYLAhskqvfreaaQNPeeVAEVF 238

                 ....*..
gi 738157197 224 AYAIEQP 230
Cdd:cd09806  239 LTAIRAP 245
PRK05867 PRK05867
SDR family oxidoreductase;
10-199 2.85e-28

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 107.81  E-value: 2.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK05867  10 KRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAV--YCASKFAVR 166
Cdd:PRK05867  90 AVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQgGVIINTASMSGHIINVPQQVshYCASKAAVI 169
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESELADHITD 199
Cdd:PRK05867 170 HLTKAMAVElaPHKIRVNSVSPGYILTELVEPYTE 204
PRK12827 PRK12827
short chain dehydrogenase; Provisional
9-225 3.28e-28

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 107.50  E-value: 3.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGA----RRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKH 84
Cdd:PRK12827   6 SRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  85 GRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGI-AAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKF 163
Cdd:PRK12827  86 GRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTqAALPPMIRARRGGRIVNIASVAGVRGNRGQVNYAASKA 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197 164 ----AVRAISDGLRqeTDAIRVTLVSPGVVESELADHIT-DETARAAMrEFRRIALPQEpVAQAIAY 225
Cdd:PRK12827 166 gligLTKTLANELA--PRGITVNAVAPGAINTPMADNAApTEHLLNPV-PVQRLGEPDE-VAALVAF 228
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
10-240 5.25e-28

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: 107.18  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELrATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd08942    7 KIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEEL-SAYGECIAIPADLSSEEGIEALVARVAERSDRLDV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY----GHIINIASTGAYTVSPTAA-VYCASKFA 164
Cdd:cd08942   86 LVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIVVSGLENySYGASKAA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 165 VRAISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMRE----FRRIALPQEPVAQAIAYAieQPAGVDISEL 238
Cdd:cd08942  166 VHQLTRKLAKElaGEHITVNAIAPGRFPSKMTAFLLNDPAALEAEEksipLGRWGRPEDMAGLAIMLA--SRAGAYLTGA 243

                 ..
gi 738157197 239 IV 240
Cdd:cd08942  244 VI 245
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
10-240 5.25e-28

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 106.81  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd08944    4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQI---AGGALALRVDVTDEQQVAALFERAVEEFGGLDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSP-LAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:cd08944   81 LVNNAGAMHLTPaIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 169 SDGLRQETDA--IRVTLVSPGVVESELAD-HITDETARAAMREFR--------RIALPQEPVAQAIAYAIEQPAGVDISE 237
Cdd:cd08944  161 TRTLAAELRHagIRCNALAPGLIDTPLLLaKLAGFEGALGPGGFHllihqlqgRLGRPEDVAAAVVFLLSDDASFITGQV 240

                 ...
gi 738157197 238 LIV 240
Cdd:cd08944  241 LCV 243
PRK06057 PRK06057
short chain dehydrogenase; Provisional
10-225 5.54e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 107.12  E-value: 5.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratggNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK06057   8 RVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEV-----GGLFVPTDVTDEDAVNALFDTAAETYGSVDI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALK--VEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAV-YCASKFAVR 166
Cdd:PRK06057  83 AFNNAGISPPEDDSILNtgLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQIsYTASKGGVL 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 167 AISD--GLRQETDAIRVTLVSPGVVESELADHI-TDETARAAMR----EFRRIALPQEpVAQAIAY 225
Cdd:PRK06057 163 AMSRelGVQFARQGIRVNALCPGPVNTPLLQELfAKDPERAARRlvhvPMGRFAEPEE-IAAAVAF 227
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
7-196 5.57e-28

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 107.11  E-value: 5.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   7 ETSKVVILTGASSGIGEATARHLSRKGHHLFIG-ARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK08063  82 RLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKAAL 161
                        170       180       190
                 ....*....|....*....|....*....|...
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVESELADH 196
Cdd:PRK08063 162 EALTRYLAVElaPKGIAVNAVSGGAVDTDALKH 194
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
11-209 6.69e-28

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: 106.60  E-value: 6.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  11 VVILTGASSGIGEATARHLSRKGHH--LFIGARRIEKLTALATELRAtGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEELRP-GLRVTTVKADLSDAAGVEQLLEAIRKLDGERD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:cd05367   80 LLINNAGSLgPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAARD 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 738157197 167 AISDGLRQETDAIRVTLVSPGVVESELADHITDETARAAMREF 209
Cdd:cd05367  160 MFFRVLAAEEPDVRVLSYAPGVVDTDMQREIRETSADPETRSR 202
PRK05993 PRK05993
SDR family oxidoreductase;
10-194 7.53e-28

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 107.42  E-value: 7.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATElratggNVDAMAIDVTRPEDLQRIAARALEK-HGRID 88
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAE------GLEAFQLDYAEPESIAALVAQVLELsGGRLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINN-----AGVMPLSPLAALKVEewnrmLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAST---------GAYTvspt 154
Cdd:PRK05993  79 ALFNNgaygqPGAVEDLPTEALRAQ-----FEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSIlglvpmkyrGAYN---- 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 738157197 155 aavycASKFAVRAISDGLRQETDA--IRVTLVSPGVVESELA 194
Cdd:PRK05993 150 -----ASKFAIEGLSLTLRMELQGsgIHVSLIEPGPIETRFR 186
PRK07069 PRK07069
short chain dehydrogenase; Validated
14-225 1.06e-27

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 106.33  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  14 LTGASSGIGEATARHLSRKGHHLFIGARRIEK-LTALATELRATGGNVDAMAI--DVTRPEDLQRIAARALEKHGRIDAL 90
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLTDINDAAgLDAFAAEINAAHGEGVAFAAvqDVTDEAQWQALLAQAADAMGGLSVL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  91 INNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISD 170
Cdd:PRK07069  84 VNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVASLTK 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197 171 GL-----RQETDaIRVTLVSPGVVESELADHITDETA-RAAMREF------RRIALPQEpVAQAIAY 225
Cdd:PRK07069 164 SIaldcaRRGLD-VRCNSIHPTFIRTGIVDPIFQRLGeEEATRKLargvplGRLGEPDD-VAHAVLY 228
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
8-240 1.28e-27

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: 105.63  E-value: 1.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATelratGGNVDAMAIDVTRPEDLQRIAARAlekhGRI 87
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELER-----GPGITTRVLDVTDKEQVAALAKEE----GRI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAS-TGAYTVSPTAAVYCASKFAVR 166
Cdd:cd05368   72 DVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSvASSIKGVPNRFVYSTTKAAVI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVES-----ELADHITDETARAAMRE---FRRIALPQEPVAQAIAYAIEQPAGVDIS 236
Cdd:cd05368  152 GLTKSVAADfaQQGIRCNAICPGTVDTpsleeRIQAQPDPEEALKAFAArqpLGRLATPEEVAALAVYLASDESAYVTGT 231

                 ....
gi 738157197 237 ELIV 240
Cdd:cd05368  232 AVVI 235
PRK07677 PRK07677
short chain dehydrogenase; Provisional
10-190 2.30e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 105.53  E-value: 2.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK07677  82 LINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIkGNIINMVATYAWDAGPGVIHSAAAKAGVLAM 161
                        170       180
                 ....*....|....*....|....*
gi 738157197 169 SDGLRQE---TDAIRVTLVSPGVVE 190
Cdd:PRK07677 162 TRTLAVEwgrKYGIRVNAIAPGPIE 186
PRK06125 PRK06125
short chain dehydrogenase; Provisional
8-192 2.53e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 105.51  E-value: 2.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGG-NVDAMAIDVTRPEDLQRIAARAlekhGR 86
Cdd:PRK06125   6 AGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGvDVAVHALDLSSPEAREQLAAEA----GD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIasTGAYTVSPTAAVYCAS--KFA 164
Cdd:PRK06125  82 IDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV--IGAAGENPDADYICGSagNAA 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 738157197 165 VRAISDGL--RQETDAIRVTLVSPGVVESE 192
Cdd:PRK06125 160 LMAFTRALggKSLDDGVRVVGVNPGPVATD 189
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
8-187 2.81e-27

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: 105.11  E-value: 2.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGN-VDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNrVIALELDITSKESIKELIESYLEKFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMP---LSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAS------------TGAYTV 151
Cdd:cd08930   81 IDILINNAYPSPkvwGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASiygviapdfriyENTQMY 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 738157197 152 SPtaAVYCASKFAVRAISDGLRQE--TDAIRVTLVSPG 187
Cdd:cd08930  161 SP--VEYSVIKAGIIHLTKYLAKYyaDTGIRVNAISPG 196
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
10-186 4.48e-27

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 109.16  E-value: 4.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGgNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAAVQAAFEEAALAFGGVDI 501
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQG-YGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK08324 502 VVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIASKNAVNPGPNFGAYGAAKAAELHL 581
                        170       180
                 ....*....|....*....|
gi 738157197 169 SDGLRQE--TDAIRVTLVSP 186
Cdd:PRK08324 582 VRQLALElgPDGIRVNGVNP 601
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
10-225 5.28e-27

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: 104.46  E-value: 5.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtgGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd05326    5 KVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGD--PDISFVHCDVTVEADVRAAVDTAVARFGRLDI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVM--PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:cd05326   83 MFNNAGVLgaPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLG 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 168 ISDGLRQETDA--IRVTLVSPGVVESELADHITDETARAAMREFRRIALPQ------EPVAQAIAY 225
Cdd:cd05326  163 LTRSAATELGEhgIRVNCVSPYGVATPLLTAGFGVEDEAIEEAVRGAANLKgtalrpEDIAAAVLY 228
PRK09291 PRK09291
SDR family oxidoreductase;
8-188 6.25e-27

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 104.31  E-value: 6.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLqriaARALEKHgrI 87
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDR----AQAAEWD--V 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK09291  75 DVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEA 154
                        170       180
                 ....*....|....*....|...
gi 738157197 168 ISDGLRQETDA--IRVTLVSPGV 188
Cdd:PRK09291 155 IAEAMHAELKPfgIQVATVNPGP 177
PRK07060 PRK07060
short chain dehydrogenase; Provisional
1-225 6.45e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 104.03  E-value: 6.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   1 MKTVVSETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtggnvDAMAIDVTRPEDlqriAARA 80
Cdd:PRK07060   1 MNMAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC-----EPLRLDVGDDAA----IRAA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  81 LEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYC 159
Cdd:PRK07060  72 LAAAGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRgGSIVNVSSQAALVGLPDHLAYC 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738157197 160 ASKFAVRAISDGLRQETDA--IRVTLVSPGVVESELADHITDE-TARAAMRE---FRRIALPQEpVAQAIAY 225
Cdd:PRK07060 152 ASKAALDAITRVLCVELGPhgIRVNSVNPTVTLTPMAAEAWSDpQKSGPMLAaipLGRFAEVDD-VAAPILF 222
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
10-225 7.20e-27

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: 104.07  E-value: 7.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPED----LQRIAARAlekHG 85
Cdd:cd05329    7 KTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSErqelMDTVASHF---GG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:cd05329   84 KLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGAL 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVESELADHITDE-------TARAAMrefRRIALPQEpVAQAIAY 225
Cdd:cd05329  164 NQLTRSLACEwaKDNIRVNAVAPWVIATPLVEPVIQQkenldkvIERTPL---KRFGEPEE-VAALVAF 228
PRK06949 PRK06949
SDR family oxidoreductase;
10-196 7.48e-27

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 104.07  E-value: 7.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGTIDI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRG---VLHGIAAVLpIMQEQGYGH------IINIASTGAYTVSPTAAVYCA 160
Cdd:PRK06949  90 LVNNSGVSTTQKLVDVTPADFDFVFDTNTRGaffVAQEVAKRM-IARAKGAGNtkpggrIINIASVAGLRVLPQIGLYCM 168
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 738157197 161 SKFAVRAISDGLRQE--TDAIRVTLVSPGVVESELADH 196
Cdd:PRK06949 169 SKAAVVHMTRAMALEwgRHGINVNAICPGYIDTEINHH 206
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
10-187 8.52e-27

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 104.67  E-value: 8.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGArrIEKLTALATELR-ATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGC--LTKNGPGAKELRrVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 --ALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQeQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:cd09805   79 lwGLVNNAGILgFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLR-RAKGRVVNVSSMGGRVPFPAGGAYCASKAAV 157
                        170       180
                 ....*....|....*....|....
gi 738157197 166 RAISDGLRQETDA--IRVTLVSPG 187
Cdd:cd09805  158 EAFSDSLRRELQPwgVKVSIIEPG 181
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
8-197 1.11e-26

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: 103.26  E-value: 1.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARH-LSRKGHHLFIGARRIEKLTALATElraTGGNVDAMAIDVTRPEDLQRIAARALEkhgr 86
Cdd:cd05354    2 KDKTVLVTGANRGIGKAFVESlLAHGAKKVYAAVRDPGSAAHLVAK---YGDKVVPLRLDVTDPESIKAAAAQAKD---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:cd05354   75 VDVVINNAGVLkPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAA 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVESELADHI 197
Cdd:cd05354  155 YSLTQGLRAElaAQGTLVLSVHPGPIDTRMAAGA 188
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
11-224 2.43e-26

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: 102.93  E-value: 2.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  11 VVILTGASSGIGEATARHLSRKGHHLFIGA-RRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAINDlPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEE--WNRMLDVNVRGVLHGIAAVLPIMQEQ------GYGHIINIASTGAYTVSPTAAVYCAS 161
Cdd:cd05337   83 LVNNAGIAVRPRGDLLDLTEdsFDRLIAINLRGPFFLTQAVARRMVEQpdrfdgPHRSIIFVTSINAYLVSPNRGEYCIS 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 162 KFAVRAISD--GLRQETDAIRVTLVSPGVVESEL---ADHITDETARAAMREFRRIALPqEPVAQAIA 224
Cdd:cd05337  163 KAGLSMATRllAYRLADEGIAVHEIRPGLIHTDMtapVKEKYDELIAAGLVPIRRWGQP-EDIAKAVR 229
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-224 5.78e-26

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 101.58  E-value: 5.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFI-GARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAInDRPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLS--PLAALKVEEWNRMLDVNVRGVLHGIAAVLPIM------QEQGYGHIINIASTGAYTVSPTAAVYCA 160
Cdd:PRK12745  83 CLVNNAGVGVKVrgDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMlaqpepEELPHRSIVFVSSVNAIMVSPNRGEYCI 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 161 SKFAVRAISDG--LRQETDAIRVTLVSPGVVESELADHIT---DETARAAMREFRRIALPQEpVAQAIA 224
Cdd:PRK12745 163 SKAGLSMAAQLfaARLAEEGIGVYEVRPGLIKTDMTAPVTakyDALIAKGLVPMPRWGEPED-VARAVA 230
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
1-202 8.02e-26

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 101.37  E-value: 8.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   1 MKTVVSETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARa 80
Cdd:PRK08085   1 MNDLFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEH- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  81 LEKH-GRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAST----GAYTVSPta 155
Cdd:PRK08085  80 IEKDiGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMqselGRDTITP-- 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 738157197 156 avYCASKFAVRAISDGLRQETDA--IRVTLVSPGVVESELADHITDETA 202
Cdd:PRK08085 158 --YAASKGAVKMLTRGMCVELARhnIQVNGIAPGYFKTEMTKALVEDEA 204
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
10-233 9.23e-26

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 101.34  E-value: 9.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEK-LTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK08936   8 KVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEeANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFGTLD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK08936  88 VMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIkGNIINMSSVHEQIPWPLFVHYAASKGGVKL 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESEL-ADHITDETARA---AMREFRRIALPQEPVAQAIAYAIEQPAGV 233
Cdd:PRK08936 168 MTETLAMEyaPKGIRVNNIGPGAINTPInAEKFADPKQRAdveSMIPMGYIGKPEEIAAVAAWLASSEASYV 239
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
11-225 1.03e-25

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: 100.72  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  11 VVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDAL 90
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  91 INNA---GVMPLSPlaALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:cd05365   81 VNNAgggGPKPFDM--PMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNH 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESE-LADHITDETARAAMRE--FRRIALPQEpVAQAIAY 225
Cdd:cd05365  159 MTRNLAFDlgPKGIRVNAVAPGAVKTDaLASVLTPEIERAMLKHtpLGRLGEPED-IANAALF 220
PRK07024 PRK07024
SDR family oxidoreductase;
12-196 1.42e-25

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 100.77  E-value: 1.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDALI 91
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPK-AARVSVYAADVRDADALAAAAADFIAAHGLPDVVI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGV---MPLSPLAALKVEEwnRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK07024  84 ANAGIsvgTLTEEREDLAVFR--EVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKY 161
                        170       180       190
                 ....*....|....*....|....*....|
gi 738157197 169 SDGLRQE--TDAIRVTLVSPGVVESELADH 196
Cdd:PRK07024 162 LESLRVElrPAGVRVVTIAPGYIRTPMTAH 191
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-228 1.74e-25

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 100.42  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK08217   6 KVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALK---------VEEWNRMLDVNVRGV-LHGI-AAVLPIMQEQGyGHIINIASTgAYTVSPTAAVY 158
Cdd:PRK08217  86 LINNAGILRDGLLVKAKdgkvtskmsLEQFQSVIDVNLTGVfLCGReAAAKMIESGSK-GVIINISSI-ARAGNMGQTNY 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 159 CASKFAVRAISDGLRQETD--AIRVTLVSPGVVESELADHITDEtARAAMRE---FRRIALPQEpVAQAIAYAIE 228
Cdd:PRK08217 164 SASKAGVAAMTVTWAKELAryGIRVAAIAPGVIETEMTAAMKPE-ALERLEKmipVGRLGEPEE-IAHTVRFIIE 236
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
1-190 1.88e-25

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 100.47  E-value: 1.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   1 MKTVVSETSKVVILTGASSGIGEATARHLSRKGHHLFI-----GARRIEKLTALATelratggnvdamaiDVTRPEDLQR 75
Cdd:PRK06171   1 MQDWLNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNadihgGDGQHENYQFVPT--------------DVSSAEEVNH 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  76 IAARALEKHGRIDALINNAG-------VMPLSPLAA--LKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAST 146
Cdd:PRK06171  67 TVAEIIEKFGRIDGLVNNAGiniprllVDEKDPAGKyeLNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSE 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738157197 147 GAYTVSPTAAVYCASKFAV----RAISDGLRQETdaIRVTLVSPGVVE 190
Cdd:PRK06171 147 AGLEGSEGQSCYAATKAALnsftRSWAKELGKHN--IRVVGVAPGILE 192
PRK08017 PRK08017
SDR family oxidoreductase;
10-230 2.27e-25

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 100.16  E-value: 2.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALaTELRATGgnvdaMAIDVTRPEDLQRIAARALE-KHGRID 88
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARM-NSLGFTG-----ILLDLDDPESVERAADEVIAlTDNRLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK08017  77 GLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAW 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197 169 SDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMRE---FRRIALPQEPVAQAIAYAIEQP 230
Cdd:PRK08017 157 SDALRMElrHSGIKVSLIEPGPIRTRFTDNVNQTQSDKPVENpgiAARFTLGPEAVVPKLRHALESP 223
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
8-210 2.38e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 100.23  E-value: 2.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK07523   9 TGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK07523  89 DILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAVGN 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 738157197 168 ISDGLrqETD----AIRVTLVSPGVVESELADHITDETARAAMREFR 210
Cdd:PRK07523 169 LTKGM--ATDwakhGLQCNAIAPGYFDTPLNAALVADPEFSAWLEKR 213
PRK09135 PRK09135
pteridine reductase; Provisional
6-229 3.27e-25

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 99.62  E-value: 3.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   6 SETSKVVILTGASSGIGEATARHLSRKGHHLFIGARR-IEKLTALATELRAT-GGNVDAMAIDVTRPEDLQRIAARALEK 83
Cdd:PRK09135   3 TDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELNALrPGSAAALQADLLDPDALPELVAACVAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  84 HGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKF 163
Cdd:PRK09135  83 FGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQR-GAIVNITDIHAERPLKGYPVYCAAKA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 164 AVRAISDGLRQE-TDAIRVTLVSPGVVESELADHITDETARAAMRE---FRRIALPQEpVAQAIAYAIEQ 229
Cdd:PRK09135 162 ALEMLTRSLALElAPEVRVNAVAPGAILWPEDGNSFDEEARQAILArtpLKRIGTPED-IAEAVRFLLAD 230
PRK08264 PRK08264
SDR family oxidoreductase;
10-228 4.65e-25

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 98.81  E-value: 4.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKG-HHLFIGARRIEKLTALatelratGGNVDAMAIDVTRPEDLQRIAARAlekhGRID 88
Cdd:PRK08264   7 KVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVTDL-------GPRVVPLQLDVTDPASVAAAAEAA----SDVT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK08264  76 ILVNNAGIFrTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWS 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 168 ISDGLRQETDA--IRVTLVSPGVVESELADHITDETARAAMrefrrialpqepVAQAIAYAIE 228
Cdd:PRK08264 156 LTQALRAELAPqgTRVLGVHPGPIDTDMAAGLDAPKASPAD------------VARQILDALE 206
PRK08265 PRK08265
short chain dehydrogenase; Provisional
10-235 5.60e-25

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 99.31  E-value: 5.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK08265   7 KVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVARFGRVDI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKvEEWNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK08265  84 LVNLACTYLDDGLASSR-ADWLAALDVNLVSAAMLAQAAHPHLARGG-GAIVNFTSISAKFAQTGRWLYPASKAAIRQLT 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197 170 DGLRQE--TDAIRVTLVSPGVVESELADHI-------TDETArAAMREFRRIALPQEpVAQAIAYAIEQPA----GVDI 235
Cdd:PRK08265 162 RSMAMDlaPDGIRVNSVSPGWTWSRVMDELsggdrakADRVA-APFHLLGRVGDPEE-VAQVVAFLCSDAAsfvtGADY 238
PRK09242 PRK09242
SDR family oxidoreductase;
10-225 8.70e-25

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 98.67  E-value: 8.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRA--TGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK09242  10 QTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEefPEREVHGLAADVSDDEDRRAILDWVEDHWDGL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK09242  90 HILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKAALLQ 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESELADHITDET-------ARAAMrefRRIALPQEpVAQAIAY 225
Cdd:PRK09242 170 MTRNLAVEwaEDGIRVNAVAPWYIRTPLTSGPLSDPdyyeqviERTPM---RRVGEPEE-VAAAVAF 232
PRK12743 PRK12743
SDR family oxidoreductase;
10-247 1.06e-24

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 98.57  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEK-LTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEgAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRG--VLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK12743  83 VLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGafLCSQIAARHMVKQGQG-GRIINITSVHEHTPLPGASAYTAAKHALG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESELADhITDETARAAMRE---FRRIALPQEpVAQAIAYAIEQPAG--------V 233
Cdd:PRK12743 162 GLTKAMALElvEHGILVNAVAPGAIATPMNG-MDDSDVKPDSRPgipLGRPGDTHE-IASLVAWLCSEGASyttgqsliV 239
                        250
                 ....*....|....
gi 738157197 234 DISELIVRPVASPH 247
Cdd:PRK12743 240 DGGFMLANPQFNSE 253
PRK06124 PRK06124
SDR family oxidoreductase;
6-214 1.25e-24

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 98.25  E-value: 1.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   6 SETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:PRK06124   8 SLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK06124  88 RLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVESEL-ADHITDETARAAMRefRRIAL 214
Cdd:PRK06124 168 TGLMRALAAEfgPHGITSNAIAPGYFATETnAAMAADPAVGPWLA--QRTPL 217
PRK06482 PRK06482
SDR family oxidoreductase;
8-230 1.81e-24

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 98.26  E-value: 1.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK06482   1 MSKTWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARY---GDRLWVLQLDVTDSAAVRAVVDRAFAALGRI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK06482  78 DVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEG 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 168 ISDGLRQETDA--IRVTLVSPGVVESEL-----ADHITDETARAAMREFRR------IALPQEPV--AQAIAYAIEQP 230
Cdd:PRK06482 158 FVEAVAQEVAPfgIEFTIVEPGPARTNFgagldRGAPLDAYDDTPVGDLRRaladgsFAIPGDPQkmVQAMIASADQT 235
PRK07831 PRK07831
SDR family oxidoreductase;
10-225 2.36e-24

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 97.80  E-value: 2.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGAS-SGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGG--NVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:PRK07831  18 KVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGlgRVEAVVCDVTSEAQVDALIDAAVERLGR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK07831  98 LDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHgGVIVNNASVLGWRAQHGQAHYAAAKAGV 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 166 RAIS--DGLRQETDAIRVTLVSPGVVESELADHITDET--ARAAMRE-FRRIALPQEpVAQAIAY 225
Cdd:PRK07831 178 MALTrcSALEAAEYGVRINAVAPSIAMHPFLAKVTSAEllDELAAREaFGRAAEPWE-VANVIAF 241
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
10-193 2.37e-24

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: 97.91  E-value: 2.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd08935    6 KVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGTVDI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAG--------------VMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTA 155
Cdd:cd08935   86 LINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFSPLTKV 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 738157197 156 AVYCASKFAVRAISDGLRQE--TDAIRVTLVSPGVVESEL 193
Cdd:cd08935  166 PAYSAAKAAVSNFTQWLAVEfaTTGVRVNAIAPGFFVTPQ 205
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
9-210 3.16e-24

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 97.16  E-value: 3.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLtalATELRATGgnVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENE---AKELREKG--VFTIKCDVGNRDQVKKSKEVVEKEFGRVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAS-TGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK06463  82 VLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASnAGIGTAAEGTTFYAITKAGIII 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 738157197 168 ISDGLRQETD--AIRVTLVSPGVVESELA-DHITDETARAAMREFR 210
Cdd:PRK06463 162 LTRRLAFELGkyGIRVNAVAPGWVETDMTlSGKSQEEAEKLRELFR 207
PRK06500 PRK06500
SDR family oxidoreductase;
10-240 6.48e-24

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 96.18  E-value: 6.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATEL-------RATGGNVDAmaidvtrpedlQRIAARALE 82
Cdd:PRK06500   7 KTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELgesalviRADAGDVAA-----------QKALAQALA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  83 KH-GRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQeQGYGHIINiASTGAYTVSPTAAVYCAS 161
Cdd:PRK06500  76 EAfGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLA-NPASIVLN-GSINAHIGMPNSSVYAAS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 162 KFAVRAISDGLRQE--TDAIRVTLVSPGVVESELADHI-TDETARAAMRE-------FRRIALPQEpVAQAIAY-AIEQP 230
Cdd:PRK06500 154 KAALLSLAKTLSGEllPRGIRVNAVSPGPVQTPLYGKLgLPEATLDAVAAqiqalvpLGRFGTPEE-IAKAVLYlASDES 232
                        250
                 ....*....|
gi 738157197 231 AGVDISELIV 240
Cdd:PRK06500 233 AFIVGSEIIV 242
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
1-187 8.66e-24

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 96.51  E-value: 8.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   1 MKTVVSETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARA 80
Cdd:PRK08277   2 MPNLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  81 LEKHGRIDALINNAG------------VMPLSPLAA---LKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAS 145
Cdd:PRK08277  82 LEDFGPCDILINGAGgnhpkattdnefHELIEPTKTffdLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISS 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 738157197 146 TGAYTVSPTAAVYCASKFAVRAISDGLRQE--TDAIRVTLVSPG 187
Cdd:PRK08277 162 MNAFTPLTKVPAYSAAKAAISNFTQWLAVHfaKVGIRVNAIAPG 205
PRK07856 PRK07856
SDR family oxidoreductase;
8-225 1.51e-23

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 95.39  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRiekltalatELRATGGNV-DAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:PRK07856   5 TGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR---------APETVDGRPaEFHAADVRDPDQVAALVDAIVERHGR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQ-GYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK07856  76 LDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQpGGGSIVNIGSVSGRRPSPGTAAYGAAKAGL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 166 RAISDGLRQE-TDAIRVTLVSPGVVESELA-DHITDETARAAMRE---FRRIALPQEpVAQAIAY 225
Cdd:PRK07856 156 LNLTRSLAVEwAPKVRVNAVVVGLVRTEQSeLHYGDAEGIAAVAAtvpLGRLATPAD-IAWACLF 219
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
10-225 1.79e-23

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 94.83  E-value: 1.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIG-ARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNyYRSTESAEAVAAEA---GERAIAIQADVRDRDQVQAMIEEAKNHFGPVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNA-GVMPLSPLAALKVEE-----WNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:cd05349   78 TIVNNAlIDFPFDPDQRKTFDTidwedYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAK 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 163 FAV----RAISDGLRQEtdAIRVTLVSPGVVESELADHITDETARAAMRE---FRRIALPQEpVAQAIAY 225
Cdd:cd05349  158 AALlgftRNMAKELGPY--GITVNMVSGGLLKVTDASAATPKEVFDAIAQttpLGKVTTPQD-IADAVLF 224
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
10-225 2.41e-23

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 94.69  E-value: 2.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRI-EKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK12935   7 KVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSkEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK12935  87 ILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGMLGF 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 169 SDGLRQETDAIRVTL--VSPGVVESELADHITDETARAAMREFRRIALPQ-EPVAQAIAY 225
Cdd:PRK12935 167 TKSLALELAKTNVTVnaICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFGQaDEIAKGVVY 226
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
10-227 2.91e-23

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: 94.38  E-value: 2.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEkltALATELRATGGNVDAMAI--DVTRPEDLQRIAARALEKHGRI 87
Cdd:cd08943    2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPE---IAEKVAEAAQGGPRALGVqcDVTSEAQVQSAFEQAVLEFGGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFA-- 164
Cdd:cd08943   79 DIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIgGNIVFNASKNAVAPGPNAAAYSAAKAAea 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197 165 --VRAISdgLRQETDAIRVTLVSPGVVESELAdhITDETARAA--------MREFR-RIALPQEPVAQAIAYAI 227
Cdd:cd08943  159 hlARCLA--LEGGEDGIRVNTVNPDAVFRGSK--IWEGVWRAArakaygllEEEYRtRNLLKREVLPEDVAEAV 228
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
9-225 4.70e-23

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 94.00  E-value: 4.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRI-EKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGR- 86
Cdd:PRK08642   5 EQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSeDAAEALADEL---GDRAIALQADVTDREQVQAMFATATEHFGKp 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGV------MPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIaSTGAYTvSPTAAV--Y 158
Cdd:PRK08642  82 ITTVVNNALAdfsfdgDARKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINI-GTNLFQ-NPVVPYhdY 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738157197 159 CASKFAVRAISDGLRQE--TDAIRVTLVSPGVVESELADHITDET---ARAAMREFRRIALPQEpVAQAIAY 225
Cdd:PRK08642 160 TTAKAALLGLTRNLAAElgPYGITVNMVSGGLLRTTDASAATPDEvfdLIAATTPLRKVTTPQE-FADAVLF 230
PRK06484 PRK06484
short chain dehydrogenase; Validated
9-232 6.95e-23

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 96.84  E-value: 6.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSL---GPDHHALAMDVSDEAQIREGFEQLHREFGRID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKV--EEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGH-IINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK06484  82 VLVNNAGVTDPTMTATLDTtlEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAAV 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197 166 RAISDGLRQETDA--IRVTLVSPGVVESE-LADHIT----DETARAAMREFRRIALPQEpVAQAIAYAIEQPAG 232
Cdd:PRK06484 162 ISLTRSLACEWAAkgIRVNAVLPGYVRTQmVAELERagklDPSAVRSRIPLGRLGRPEE-IAEAVFFLASDQAS 234
PRK05876 PRK05876
short chain dehydrogenase; Provisional
13-193 8.01e-23

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 93.87  E-value: 8.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  13 ILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDALIN 92
Cdd:PRK05876  10 VITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  93 NAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAVRAISDG 171
Cdd:PRK05876  90 NAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTgGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAET 169
                        170       180
                 ....*....|....*....|....
gi 738157197 172 LRQET--DAIRVTLVSPGVVESEL 193
Cdd:PRK05876 170 LAREVtaDGIGVSVLCPMVVETNL 193
PRK06523 PRK06523
short chain dehydrogenase; Provisional
10-225 8.22e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 93.43  E-value: 8.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARriekltalaTELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK06523  10 KRALVTGGTKGIGAATVARLLEAGARVVTTAR---------SRPDDLPEGVEFVAADLTTAEGCAAVARAVLERLGGVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAG--VMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTA-AVYCASKFAVR 166
Cdd:PRK06523  81 LVHVLGgsSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPEStTAYAAAKAALS 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 167 AISDGLRQET--DAIRVTLVSPGVVESELADHITDETARAA-----------MREFRRIAL--PQEP--VAQAIAY 225
Cdd:PRK06523 161 TYSKSLSKEVapKGVRVNTVSPGWIETEAAVALAERLAEAAgtdyegakqiiMDSLGGIPLgrPAEPeeVAELIAF 236
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
12-195 1.05e-22

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


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 92.74  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHL-SRKGHHLFIGARRIEKLTALATeLRATGGNVDAMAIDVTRPED--LQRIAARALEKHgrID 88
Cdd:cd05325    1 VLITGASRGIGLELVRQLlARGNNTVIATCRDPSAATELAA-LGASHSRLHILELDVTDEIAesAEAVAERLGDAG--LD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAS---TGAYTVSPTAAVYCASKFA 164
Cdd:cd05325   78 VLINNAGILhSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSrvgSIGDNTSGGWYSYRASKAA 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 738157197 165 ----VRAISDGLRQetDAIRVTLVSPGVVESELAD 195
Cdd:cd05325  158 lnmlTKSLAVELKR--DGITVVSLHPGWVRTDMGG 190
PRK06947 PRK06947
SDR family oxidoreductase;
9-193 1.23e-22

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 92.95  E-value: 1.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIG-ARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK06947   2 RKVVLITGASRGIGRATAVLAAARGWSVGINyARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAG-VMPLSPLAALKVEEWNRMLDVNVRG---VLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAV-YCASK 162
Cdd:PRK06947  82 DALVNNAGiVAPSMPLADMDAARLRRMFDTNVLGaylCAREAARRLSTDRGGRGGAIVNVSSIASRLGSPNEYVdYAGSK 161
                        170       180       190
                 ....*....|....*....|....*....|...
gi 738157197 163 FAVRAISDGLRQET--DAIRVTLVSPGVVESEL 193
Cdd:PRK06947 162 GAVDTLTLGLAKELgpHGVRVNAVRPGLIETEI 194
PRK06114 PRK06114
SDR family oxidoreductase;
10-187 1.27e-22

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 92.92  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEK-LTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK06114   9 QVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAELGALT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSP--TAAVYCASKFAVR 166
Cdd:PRK06114  89 LAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRglLQAHYNASKAGVI 168
                        170       180
                 ....*....|....*....|...
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPG 187
Cdd:PRK06114 169 HLSKSLAMEwvGRGIRVNSISPG 191
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
10-230 1.59e-22

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: 92.35  E-value: 1.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATelraTGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd05371    3 LVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK----LGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALK------VEEWNRMLDVNVRGVLHGIAAVLPIMQEQG------YGHIINIASTGAYTVSPTAAV 157
Cdd:cd05371   79 VVNCAGIAVAAKTYNKKgqqphsLELFQRVINVNLIGTFNVIRLAAGAMGKNEpdqggeRGVIINTASVAAFEGQIGQAA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 158 YCASKFAVRAISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAAMREF---RRIALPQEpVAQAIAYAIEQP 230
Cdd:cd05371  159 YSASKGGIVGMTLPIARDlaPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVpfpSRLGDPAE-YAHLVQHIIENP 235
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
10-226 1.67e-22

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 92.60  E-value: 1.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK06113  12 KCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGKVDI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLaALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK06113  92 LVNNAGGGGPKPF-DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLV 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738157197 170 DGLRQETDA--IRVTLVSPGVVESE-LADHITDETARAAMRE--FRRIALPQEpvaqaIAYA 226
Cdd:PRK06113 171 RNMAFDLGEknIRVNGIAPGAILTDaLKSVITPEIEQKMLQHtpIRRLGQPQD-----IANA 227
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
11-242 1.97e-22

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: 92.06  E-value: 1.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  11 VVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATE-LRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDiIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:cd05373   81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALA 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 170 DGLRQE--TDAIRVT-LVSPGVVESELADhiTDETARAAMREFRRIaLPQEPVAQAIAYAIEQPAGVDISELIVRP 242
Cdd:cd05373  161 QSMARElgPKGIHVAhVIIDGGIDTDFIR--ERFPKRDERKEEDGI-LDPDAIAEAYWQLHTQPRSAWTHELDLRP 233
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
8-193 2.81e-22

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: 91.76  E-value: 2.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtggnVDAMAIDVTRPEDLQRiaarALEKHGRI 87
Cdd:cd05351    6 AGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVRECPG----IEPVCVDLSDWDATEE----ALGSVGPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:cd05351   78 DLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQRALTNHTVYCSTKAALD 157
                        170       180
                 ....*....|....*....|....*....
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESEL 193
Cdd:cd05351  158 MLTKVMALElgPHKIRVNSVNPTVVMTDM 186
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
10-192 3.12e-22

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: 91.82  E-value: 3.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLfIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd08937    5 KVVVVTGAAQGIGRGVAERLAGEGARV-LLVDRSELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNA-GVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAavYCASKFAVRAI 168
Cdd:cd08937   84 LINNVgGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGIYRIP--YSAAKGGVNAL 161
                        170       180
                 ....*....|....*....|....*.
gi 738157197 169 SDGLRQET--DAIRVTLVSPGVVESE 192
Cdd:cd08937  162 TASLAFEHarDGIRVNAVAPGGTEAP 187
PRK07062 PRK07062
SDR family oxidoreductase;
8-225 3.41e-22

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 92.03  E-value: 3.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAT--GGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:PRK07062   7 EGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKfpGARLLAARCDVLDEADVAAFAAAVEARFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK07062  87 GVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAARAGL 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVES-----------ELADHITDETAR-AAMREFR--RIALPQEPvAQAIAY 225
Cdd:PRK07062 167 LNLVKSLATElaPKGVRVNSILLGLVESgqwrrryearaDPGQSWEAWTAAlARKKGIPlgRLGRPDEA-ARALFF 241
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
10-228 4.22e-22

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: 91.44  E-value: 4.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATG-GNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd08933   10 KVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGpGSCKFVPCDVTKEEDIKTLISVTVERFGRID 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQeQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:cd08933   90 CLVNNAGWHpPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLR-KSQGNIINLSSLVGSIGQKQAAPYVATKGAITA 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197 168 ISDGLRQETD--AIRVTLVSPGVVESELADHITDETA--RAAMRE------FRRIALPQEPVAQAIAYAIE 228
Cdd:cd08933  169 MTKALAVDESryGVRVNCISPGNIWTPLWEELAAQTPdtLATIKEgelaqlLGRMGTEAESGLAALFLAAE 239
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
8-206 8.05e-22

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 90.78  E-value: 8.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK06200   5 HGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRF---GDHVLVVEGDVTSYADNQRAVDQTVDAFGKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGV----MPLSPLAALKVEE-WNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:PRK06200  82 DCFVGNAGIwdynTSLVDIPAETLDTaFDEIFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYPGGGGPLYTASK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738157197 163 FAVRAISDGLRQE-TDAIRVTLVSPGVVESEL---------ADHITDETARAAM 206
Cdd:PRK06200 161 HAVVGLVRQLAYElAPKIRVNGVAPGGTVTDLrgpaslgqgETSISDSPGLADM 214
PLN02253 PLN02253
xanthoxin dehydrogenase
9-225 8.99e-22

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 91.04  E-value: 8.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEkltaLATELRAT-GGNVDAMAI--DVTRPEDLQRIAARALEKHG 85
Cdd:PLN02253  18 GKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDD----LGQNVCDSlGGEPNVCFFhcDVTVEDDVSRAVDFTVDKFG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVM--PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYT--VSPTAavYCAS 161
Cdd:PLN02253  94 TLDIMVNNAGLTgpPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIggLGPHA--YTGS 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 162 KFAVRAISDGLRQE--TDAIRVTLVSPGVVESELA-DHI-TDETARAAMREFRRIA----------LPQEPVAQAIAY 225
Cdd:PLN02253 172 KHAVLGLTRSVAAElgKHGIRVNCVSPYAVPTALAlAHLpEDERTEDALAGFRAFAgknanlkgveLTVDDVANAVLF 249
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
10-200 1.95e-21

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: 89.37  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGAR-----RIEKLTAL-------ATELRATGGNVDAMAIDVTRPEDLQRIA 77
Cdd:cd05338    4 KVAFVTGASRGIGRAIALRLAKAGATVVVAAKtasegDNGSAKSLpgtieetAEEIEAAGGQALPIVVDVRDEDQVRALV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  78 ARALEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAV 157
Cdd:cd05338   84 EATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARGDVA 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 738157197 158 YCASKFAVRAISDGLRQE--TDAIRVTLVSPG-VVESELADHITDE 200
Cdd:cd05338  164 YAAGKAGMSRLTLGLAAElrRHGIAVNSLWPStAIETPAATELSGG 209
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
10-190 2.32e-21

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 89.62  E-value: 2.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIgARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK12823   9 KVVVVTGAAQGIGRGVALRAAAEGARVVL-VDRSELVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINN-AGVMPLSPLAALKVEEwnrmLDVNVR----GVLHGIAAVLPIMQEQGYGHIIN---IASTGAYTVSptaavYCAS 161
Cdd:PRK12823  88 LINNvGGTIWAKPFEEYEEEQ----IEAEIRrslfPTLWCCRAVLPHMLAQGGGAIVNvssIATRGINRVP-----YSAA 158
                        170       180       190
                 ....*....|....*....|....*....|.
gi 738157197 162 KFAVRAISDGLRQET--DAIRVTLVSPGVVE 190
Cdd:PRK12823 159 KGGVNALTASLAFEYaeHGIRVNAVAPGGTE 189
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
10-189 3.12e-21

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 89.27  E-value: 3.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFI--------GARRIEKLtalateLRATGGNVDAMAIDVTRPEDLQRIAARAL 81
Cdd:cd05355   27 KKALITGGDSGIGRAVAIAFAREGADVAInylpeeedDAEETKKL------IEEEGRKCLLIPGDLGDESFCRDLVKEVV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  82 EKHGRIDALINNAGV-MPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQgyGHIINIASTGAYTVSPTAAVYCA 160
Cdd:cd05355  101 KEFGKLDILVNNAAYqHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG--SSIINTTSVTAYKGSPHLLDYAA 178
                        170       180       190
                 ....*....|....*....|....*....|.
gi 738157197 161 SKFAVRAISDGLRQE--TDAIRVTLVSPGVV 189
Cdd:cd05355  179 TKGAIVAFTRGLSLQlaEKGIRVNAVAPGPI 209
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
9-193 4.83e-21

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: 88.66  E-value: 4.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIE-KLTALATELRATGGNVDAMAIDVTRPEDLQRIAAR-ALEKHGR 86
Cdd:cd09763    3 GKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERvAREQQGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNA-------GVMPLSPLAALKVEEWNRMLDVNVRGvlHGIAAV--LPIMQEQGYGHIINIASTGA----YTVSp 153
Cdd:cd09763   83 LDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRA--HYACSVyaAPLMVKAGKGLIVIISSTGGleylFNVA- 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 738157197 154 taavYCASKFAVRAISDGLRQE--TDAIRVTLVSPGVVESEL 193
Cdd:cd09763  160 ----YGVGKAAIDRMAADMAHElkPHGVAVVSLWPGFVRTEL 197
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-221 1.41e-20

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 86.94  E-value: 1.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFigARRIEKLTALATELRAtggnvdaMAIDVTRPedlqriAARALEKHGRI 87
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQVY--GVDKQDKPDLSGNFHF-------LQLDLSDD------LEPLFDWVPSV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK06550  69 DILCNTAGILdDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALA 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVES----------ELADHITDETAraamreFRRIALPQEpVAQ 221
Cdd:PRK06550 149 GFTKQLALDyaKDGIQVFGIAPGAVKTpmtaadfepgGLADWVARETP------IKRWAEPEE-VAE 208
PRK06484 PRK06484
short chain dehydrogenase; Validated
1-225 1.69e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.91  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   1 MKTVVSETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARA 80
Cdd:PRK06484 261 APSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEAL---GDEHLSVQADITDEAAVESAFAQI 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  81 LEKHGRIDALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMqeQGYGHIINIASTGAYTVSPTAAVYC 159
Cdd:PRK06484 338 QARWGRLDVLVNNAGIAeVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYC 415
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738157197 160 ASKFAVRAISDGLRQETDA--IRVTLVSPGVVESELADHITDETARAAMREFRRIALPQ----EPVAQAIAY 225
Cdd:PRK06484 416 ASKAAVTMLSRSLACEWAPagIRVNTVAPGYIETPAVLALKASGRADFDSIRRRIPLGRlgdpEEVAEAIAF 487
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
8-164 2.14e-20

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 87.01  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAI--DVTRPEDLQRIAARALEKHG 85
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMAYGFgaDATSEQSVLALSRGVDEIFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFA 164
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAKFG 160
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
8-194 2.33e-20

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: 86.64  E-value: 2.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd05348    3 KGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADF---GDAVVGVEGDVRSLADNERAVARCVERFGKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGV----MPLSPLAALKVEE-WNRMLDVNVRGVLHGIAAVLPIMQeQGYGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:cd05348   80 DCFIGNAGIwdysTSLVDIPEEKLDEaFDELFHINVKGYILGAKAALPALY-ATEGSVIFTVSNAGFYPGGGGPLYTASK 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 738157197 163 FAVRAISDGLRQE-TDAIRVTLVSPGVVESELA 194
Cdd:cd05348  159 HAVVGLVKQLAYElAPHIRVNGVAPGGMVTDLR 191
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
10-226 3.05e-20

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: 86.61  E-value: 3.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   10 KVVILTGASSGIGEATARHLSRKGHHLFIGAR------------RIEKLTALAtelRATGGNVDAMAIDVTRPEDLQRIA 77
Cdd:TIGR04504   2 RVALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpavgyplaTRAELDAVA---AACPDQVLPVIADVRDPAALAAAV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   78 ARALEKHGRIDALINNAGVMPL-SPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIM---QEQGYGHIINIASTGAYTVSP 153
Cdd:TIGR04504  79 ALAVERWGRLDAAVAAAGVIAGgRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMlarPDPRGGRFVAVASAAATRGLP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  154 TAAVYCASKFAVRAISDGLRQE--TDAIRVTLVSPGVVESELadhiTDETAR----------AAMREFRRIALPQEpVAQ 221
Cdd:TIGR04504 159 HLAAYCAAKHAVVGLVRGLAADlgGTGVTANAVSPGSTRTAM----LAATARlygltdveefAGHQLLGRLLEPEE-VAA 233

                  ....*
gi 738157197  222 AIAYA 226
Cdd:TIGR04504 234 AVAWL 238
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
10-230 3.64e-20

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: 85.79  E-value: 3.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIE-KLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEaEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:cd05357   81 VLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197 169 SDGLRQE-TDAIRVTLVSPGvvESELADHITDETARAAMrefRRIALPQEP----VAQAIAYAIEQP 230
Cdd:cd05357  161 TRSAALElAPNIRVNGIAPG--LILLPEDMDAEYRENAL---RKVPLKRRPsaeeIADAVIFLLDSN 222
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
10-156 3.96e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 86.27  E-value: 3.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDI 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAST----GAYTVSPTAA 156
Cdd:PRK07097  91 LVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMmselGRETVSAYAA 161
PRK07577 PRK07577
SDR family oxidoreductase;
8-232 7.07e-20

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 85.16  E-value: 7.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKltALATELratggnvdaMAIDVTRPEDLQRIAARALEKHGrI 87
Cdd:PRK07577   2 SSRTVLVTGATKGIGLALSLRLANLGHQVIGIARSAID--DFPGEL---------FACDLADIEQTAATLAQINEIHP-V 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTgAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK07577  70 DAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSR-AIFGALDRTSYSAAKSALVG 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738157197 168 ISD--GLRQETDAIRVTLVSPGVVESELADHI----TDETARA-AMREFRRIALPQEpVAQAIAYAIEQPAG 232
Cdd:PRK07577 149 CTRtwALELAEYGITVNAVAPGPIETELFRQTrpvgSEEEKRVlASIPMRRLGTPEE-VAAAIAFLLSDDAG 219
PRK06123 PRK06123
SDR family oxidoreductase;
10-193 9.12e-20

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 85.22  E-value: 9.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIG-ARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLNyLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGH---IINIASTGAYTVSPTAAV-YCASKF 163
Cdd:PRK06123  83 ALVNNAGILeAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSPGEYIdYAASKG 162
                        170       180       190
                 ....*....|....*....|....*....|..
gi 738157197 164 AVRAISDGLRQE--TDAIRVTLVSPGVVESEL 193
Cdd:PRK06123 163 AIDTMTIGLAKEvaAEGIRVNAVRPGVIYTEI 194
PRK07814 PRK07814
SDR family oxidoreductase;
10-232 1.67e-19

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 84.45  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK07814  11 QVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINN-AGVMPlSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQ-GYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK07814  91 VVNNvGGTMP-NPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHsGGGSVINISSTMGRLAGRGFAAYGTAKAALAH 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 168 ISDGLRQE-TDAIRVTLVSPG-VVESELADHITDETARAAMRE---FRRIALPQEPVAQAIAYAieQPAG 232
Cdd:PRK07814 170 YTRLAALDlCPRIRVNAIAPGsILTSALEVVAANDELRAPMEKatpLRRLGDPEDIAAAAVYLA--SPAG 237
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-199 3.27e-19

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 83.62  E-value: 3.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGA-RRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK06077   7 KVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAkKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVAD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQgyGHIINIASTGAYTVSPTAAVYCASKFAVRAI 168
Cdd:PRK06077  87 ILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREG--GAIVNIASVAGIRPAYGLSIYGAMKAAVINL 164
                        170       180       190
                 ....*....|....*....|....*....|..
gi 738157197 169 SDGLRQE-TDAIRVTLVSPGVVESELADHITD 199
Cdd:PRK06077 165 TKYLALElAPKIRVNAIAPGFVKTKLGESLFK 196
PRK09730 PRK09730
SDR family oxidoreductase;
10-231 4.31e-19

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 83.36  E-value: 4.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIG-ARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNyQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAGVM-PLSPLAALKVEEWNRMLDVNVRG-VLHGIAAVLPIMQEQG--YGHIINIASTGAYTVSPTAAV-YCASKF 163
Cdd:PRK09730  82 ALVNNAGILfTQCTVENLTAERINRVLSTNVTGyFLCCREAVKRMALKHGgsGGAIVNVSSAASRLGAPGEYVdYAASKG 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197 164 AVRAISDGLRQETDA--IRVTLVSPGVVESELadHIT-DETAR----AAMREFRRIALPQEpVAQAIAYAIEQPA 231
Cdd:PRK09730 162 AIDTLTTGLSLEVAAqgIRVNCVRPGFIYTEM--HASgGEPGRvdrvKSNIPMQRGGQPEE-VAQAIVWLLSDKA 233
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-225 6.87e-19

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 84.89  E-value: 6.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFI----GARriEKLTALATELRATggnvdAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:PRK08261 211 KVALVTGAARGIGAAIAEVLARDGAHVVCldvpAAG--EALAAVANRVGGT-----ALALDITAPDAPARIAEHLAERHG 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNvrgvlhgIAAVLPIMQ---EQGY----GHIINIASTGAYTVSPTAAVY 158
Cdd:PRK08261 284 GLDIVVHNAGITRDKTLANMDEARWDSVLAVN-------LLAPLRITEallAAGAlgdgGRIVGVSSISGIAGNRGQTNY 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 159 CASKFA----VRAISDGLRQEtdAIRVTLVSPGVVEseladhiTDETAR--AAMREF-RRIA------LPQEpVAQAIAY 225
Cdd:PRK08261 357 AASKAGviglVQALAPLLAER--GITINAVAPGFIE-------TQMTAAipFATREAgRRMNslqqggLPVD-VAETIAW 426
PRK05875 PRK05875
short chain dehydrogenase; Provisional
10-199 7.07e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 83.31  E-value: 7.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRA--TGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK05875   8 RTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEAlkGAGAVRYEPADVTDEDQVARAVDAATAWHGRL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNA-GVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK05875  88 HGVVHCAgGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKSAVD 167
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 738157197 167 AISDGLRQETDA--IRVTLVSPGVVESELADHITD 199
Cdd:PRK05875 168 HLMKLAADELGPswVRVNSIRPGLIRTDLVAPITE 202
PRK07074 PRK07074
SDR family oxidoreductase;
8-225 8.16e-19

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 82.51  E-value: 8.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtgGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGD--ARFVPVACDLTDAASLAAALANAAAERGPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAvYCASKFAVRA 167
Cdd:PRK07074  79 DVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPA-YSAAKAGLIH 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESELADhitdetARAAMR-----------EFRRIALPQEpVAQAIAY 225
Cdd:PRK07074 158 YTKLLAVEygRFGIRANAVAPGTVKTQAWE------ARVAANpqvfeelkkwyPLQDFATPDD-VANAVLF 221
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
10-221 8.90e-19

(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: 82.37  E-value: 8.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFI----GARRIEKLTALAT-----ELRATGGNVDAMAIDVtrpEDLQRIAARA 80
Cdd:cd05353    6 RVVLVTGAGGGLGRAYALAFAERGAKVVVndlgGDRKGSGKSSSAAdkvvdEIKAAGGKAVANYDSV---EDGEKIVKTA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  81 LEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCA 160
Cdd:cd05353   83 IDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYSA 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 161 SKFAVRAISDGLRQE--TDAIRVTLVSPgvveseladhitdeTARAAMREfrrIALPQEPVAQ 221
Cdd:cd05353  163 AKLGLLGLSNTLAIEgaKYNITCNTIAP--------------AAGSRMTE---TVMPEDLFDA 208
PRK08278 PRK08278
SDR family oxidoreductase;
10-144 1.06e-18

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 82.64  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIE---KL-----TAlATELRATGGNVDAMAIDVTRPEDLQRIAARAL 81
Cdd:PRK08278   7 KTLFITGASRGIGLAIALRAARDGANIVIAAKTAEphpKLpgtihTA-AEEIEAAGGQALPLVGDVRDEDQVAAAVAKAV 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197  82 EKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIA 144
Cdd:PRK08278  86 ERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLS 148
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
10-221 1.57e-18

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: 81.47  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIgARRIEKLTALATELRatGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVF-ADIDEERGADFAEAE--GPNLFFVHGDVADETLVKFVVYAMLEKLGRIDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:cd09761   79 LVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAASKGGLVALT 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738157197 170 DGLRQETDA-IRVTLVSPGVVEseladhiTDETARAAMREFRRIALPQEPVAQ 221
Cdd:cd09761  158 HALAMSLGPdIRVNCISPGWIN-------TTEQQEFTAAPLTQEDHAQHPAGR 203
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
12-193 1.65e-18

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: 80.64  E-value: 1.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtggnvdamaidVTRPEDL-QRIAARAL-EKHGRIDA 89
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGA-----------LARPADVaAELEVWALaQELGPLDL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQgyGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:cd11730   70 LVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAG--ARLVFLGAYPELVMLPGLSAYAAAKAALEAYV 147
                        170       180
                 ....*....|....*....|....
gi 738157197 170 DGLRQETDAIRVTLVSPGVVESEL 193
Cdd:cd11730  148 EVARKEVRGLRLTLVRPPAVDTGL 171
PRK07041 PRK07041
SDR family oxidoreductase;
16-230 2.64e-18

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 80.85  E-value: 2.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  16 GASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtGGNVDAMAIDVTRPEDLQRIAARalekHGRIDALINNAG 95
Cdd:PRK07041   4 GGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGG-GAPVRTAALDITDEAAVDAFFAE----AGPFDHVVITAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  96 VMPLSPLAALKVEEWNRMLDVNVRGVLHgiAAVLPIMQEQgyGHIINIASTGAYTVSPTAAVYCASKFAVRAISDGLRQE 175
Cdd:PRK07041  79 DTPGGPVRALPLAAAQAAMDSKFWGAYR--VARAARIAPG--GSLTFVSGFAAVRPSASGVLQGAINAALEALARGLALE 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738157197 176 TDAIRVTLVSPGVVESELADHITDEtARAAMRE-------FRRIALPqEPVAQAIAYAIEQP 230
Cdd:PRK07041 155 LAPVRVNTVSPGLVDTPLWSKLAGD-AREAMFAaaaerlpARRVGQP-EDVANAILFLAANG 214
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
8-232 1.51e-17

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 78.90  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGA-----RR---IEKLTALATELRATGGNVDAMaiDVTRpEDLQRIAAR 79
Cdd:PRK12938   2 SQRIAYVTGGMGGIGTSICQRLHKDGFKVVAGCgpnspRRvkwLEDQKALGFDFIASEGNVGDW--DSTK-AAFDKVKAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  80 AlekhGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYC 159
Cdd:PRK12938  79 V----GEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYS 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197 160 ASKFAVRAISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARA--AMREFRRIALPQEpVAQAIAYAIEQPAG 232
Cdd:PRK12938 155 TAKAGIHGFTMSLAQEvaTKGVTVNTVSPGYIGTDMVKAIRPDVLEKivATIPVRRLGSPDE-IGSIVAWLASEESG 230
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
10-187 1.76e-17

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 78.76  E-value: 1.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDA-MAIDVTR--PEDLQRIAARALEKHGR 86
Cdd:PRK08945  13 RIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAiIPLDLLTatPQNYQQLADTIEEQFGR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIAST---------GAYTVsptaa 156
Cdd:PRK08945  93 LDGVLHNAGLLgELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSvgrqgranwGAYAV----- 167
                        170       180       190
                 ....*....|....*....|....*....|...
gi 738157197 157 vycaSKFAVRAISDGLRQETD--AIRVTLVSPG 187
Cdd:PRK08945 168 ----SKFATEGMMQVLADEYQgtNLRVNCINPG 196
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
10-197 1.82e-17

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: 79.43  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMA--IDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVrhLDLASLKSIRAFAAEFLAEEDRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVM--PLSplaalKVEEWNRM-LDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTgAYTVSP----------- 153
Cdd:cd09807   82 DVLINNAGVMrcPYS-----KTEDGFEMqFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSL-AHKAGKinfddlnseks 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738157197 154 --TAAVYCASKFAVRAISDGL--RQETDAIRVTLVSPGVVESELADHI 197
Cdd:cd09807  156 ynTGFAYCQSKLANVLFTRELarRLQGTGVTVNALHPGVVRTELGRHT 203
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
10-191 5.06e-17

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 77.23  E-value: 5.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGG---NVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:cd05340    5 RIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGrqpQWFILDLLTCTSENCQQLAQRIAVNYPR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:cd05340   85 LDGVLHNAGLLgDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFAT 164
                        170       180
                 ....*....|....*....|....*...
gi 738157197 166 RAISDGLRQETD--AIRVTLVSPGVVES 191
Cdd:cd05340  165 EGL*QVLADEYQqrNLRVNCINPGGTRT 192
PRK08628 PRK08628
SDR family oxidoreductase;
10-186 1.01e-16

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 76.92  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLtALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK08628   8 KVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDD-EFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAAlKVEEWNRMLDVNvrgVLHGIAAV---LPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK08628  87 LVNNAGVNDGVGLEA-GREAFVASLERN---LIHYYVMAhycLPHLKASR-GAIVNISSKTALTGQGGTSGYAAAKGAQL 161
                        170       180
                 ....*....|....*....|....
gi 738157197 167 AISD----GLRQetDAIRVTLVSP 186
Cdd:PRK08628 162 ALTRewavALAK--DGVRVNAVIP 183
PRK06197 PRK06197
short chain dehydrogenase; Provisional
4-97 1.94e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 76.99  E-value: 1.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   4 VVSETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAT--GGNVDAMAIDVTRPEDLqRIAARAL 81
Cdd:PRK06197  11 IPDQSGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAAtpGADVTLQELDLTSLASV-RAAADAL 89
                         90
                 ....*....|....*..
gi 738157197  82 EK-HGRIDALINNAGVM 97
Cdd:PRK06197  90 RAaYPRIDLLINNAGVM 106
PRK06701 PRK06701
short chain dehydrogenase; Provisional
10-225 3.04e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 76.23  E-value: 3.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIgARRIEKLTALATELRATGGNVDAMAI--DVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK06701  47 KVALITGGDSGIGRAVAVLFAKEGADIAI-VYLDEHEDANETKQRVEKEGVKCLLIpgDVSDEAFCKDAVEETVRELGRL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVM-PLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMqEQGyGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK06701 126 DILVNNAAFQyPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL-KQG-SAIINTGSITGYEGNETLIDYSATKGAIH 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPGVVESEL------ADHITDETARAAMREfrrialPQEPVAQAIAY 225
Cdd:PRK06701 204 AFTRSLAQSlvQKGIRVNAVAPGPIWTPLipsdfdEEKVSQFGSNTPMQR------PGQPEELAPAY 264
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
8-208 3.59e-16

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 77.26  E-value: 3.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATEL--RATGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:COG3347  424 AGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELggGYGADAVDATDVDVTAEAAVAAAFGFAGLDIG 503
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQG-YGHIINIASTGAYTVSPTAAVYCASKFA 164
Cdd:COG3347  504 GSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGlGGSSVFAVSKNAAAAAYGAAAAATAKAA 583
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 738157197 165 VRAISDGLRQET-----DAIRVTLVSPGVVESELADHITDETARAAMRE 208
Cdd:COG3347  584 AQHLLRALAAEGgangiNANRVNPDAVLDGSAIWASAARAERAAAYGIG 632
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-205 4.28e-16

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 74.94  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLF-IGARRIEKLTALateLRATGGNVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:PRK12481   7 NGKVAIITGCNTGLGQGMAIGLAKAGADIVgVGVAEAPETQAQ---VEALGRKFHFITADLIQQKDIDSIVSQAVEVMGH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAV 165
Cdd:PRK12481  84 IDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASMLSFQGGIRVPSYTASKSAV 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVESELADHITDETARAA 205
Cdd:PRK12481 164 MGLTRALATElsQYNINVNAIAPGYMATDNTAALRADTARNE 205
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-225 5.77e-16

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 74.73  E-value: 5.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGAS--SGIGEATARHLSRKGHHLFI------------GARRIEKLTaLATELRATGGNVDAMAIDVTRPEDL 73
Cdd:PRK12748   4 MKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFtywspydktmpwGMHDKEPVL-LKEEIESYGVRCEHMEIDLSQPYAP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  74 QRIAARALEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLhgIAAVLPIMQEQGY--GHIINIASTGAYTV 151
Cdd:PRK12748  83 NRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATM--LLSSAFAKQYDGKagGRIINLTSGQSLGP 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 152 SPTAAVYCASKFAVRAISDGLRQET--DAIRVTLVSPGVVESelaDHITDETARAAMREF--RRIALPQEPvAQAIAY 225
Cdd:PRK12748 161 MPDELAYAATKGAIEAFTKSLAPELaeKGITVNAVNPGPTDT---GWITEELKHHLVPKFpqGRVGEPVDA-ARLIAF 234
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
10-123 6.83e-16

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 72.90  E-value: 6.83e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197    10 KVVILTGASSGIGEATARHLSRKG--HHLFIGARRI--EKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHG 85
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGarRLVLLSRSGPdaPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEG 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 738157197    86 RIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLH 123
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWN 118
PRK05717 PRK05717
SDR family oxidoreductase;
10-191 1.41e-15

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 73.77  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALAtelRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVA---KALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLDA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPL--SPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK05717  88 LVCNAAIADPhnTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSEPDTEAYAASKGGLLA 166
                        170       180
                 ....*....|....*....|....*
gi 738157197 168 ISDGLRQETDA-IRVTLVSPGVVES 191
Cdd:PRK05717 167 LTHALAISLGPeIRVNAVSPGWIDA 191
PRK07023 PRK07023
SDR family oxidoreductase;
13-226 2.07e-15

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 73.12  E-value: 2.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  13 ILTGASSGIGEATARHLSRKGHHLFIGARRieKLTALATelrATGGNVDAMAIDVTRPEDLQRIAA----RALEKHGRID 88
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLLQPGIAVLGVARS--RHPSLAA---AAGERLAEVELDLSDAAAAAAWLAgdllAAFVDGASRV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ALINNAG-VMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFA--- 164
Cdd:PRK07023  80 LLINNAGtVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAAldh 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197 165 -VRAISdglRQETDAIRVTLVSPGVVESELADHI-TDETARAAMRE-FRR------IALPQEPVAQAIAYA 226
Cdd:PRK07023 160 hARAVA---LDANRALRIVSLAPGVVDTGMQATIrATDEERFPMRErFRElkasgaLSTPEDAARRLIAYL 227
PRK07576 PRK07576
short chain dehydrogenase; Provisional
1-190 2.59e-15

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 73.07  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   1 MKTVVSETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARA 80
Cdd:PRK07576   1 MTTMFDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  81 LEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPTAAVYCA 160
Cdd:PRK07576  81 ADEFGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG-ASIIQISAPQAFVPMPMQAHVCA 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 738157197 161 SKFAVRAISDGLRQE--TDAIRVTLVSPGVVE 190
Cdd:PRK07576 160 AKAGVDMLTRTLALEwgPEGIRVNSIVPGPIA 191
PRK06196 PRK06196
oxidoreductase; Provisional
8-205 1.39e-14

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 71.64  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRatggNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK06196  25 SGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGID----GVEVVMLDLADLESVRAFAERFLDSGRRI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVM--PLSPLaalkVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTG------------------ 147
Cdd:PRK06196 101 DILINNAGVMacPETRV----GDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAGhrrspirwddphftrgyd 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197 148 ---AYTVSPTAAVYCASKFAVRAISDGlrqetdaIRVTLVSPGVVESELADHITDETARAA 205
Cdd:PRK06196 177 kwlAYGQSKTANALFAVHLDKLGKDQG-------VRAFSVHPGGILTPLQRHLPREEQVAL 230
PLN02780 PLN02780
ketoreductase/ oxidoreductase
13-207 1.98e-14

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 71.44  E-value: 1.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  13 ILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA--L 90
Cdd:PLN02780  57 LVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTVVVDFSGDIDEGVKRIKETIEGLDVgvL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  91 INNAGVMplSPLAAL--KVEE--WNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTV--SPTAAVYCASKFA 164
Cdd:PLN02780 137 INNVGVS--YPYARFfhEVDEelLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIpsDPLYAVYAATKAY 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 738157197 165 VRAISDGLRQE--TDAIRVTLVSPGVVESELAD--------HITDETARAAMR 207
Cdd:PLN02780 215 IDQFSRCLYVEykKSGIDVQCQVPLYVATKMASirrssflvPSSDGYARAALR 267
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-187 2.23e-14

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 70.29  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLfIGARRIEKLTALAtELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK08993   9 EGKVAVVTGCDTGLGQGMALGLAEAGCDI-VGINIVEPTETIE-QVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK08993  87 DILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNgGKIINIASMLSFQGGIRVPSYTASKSGVM 166
                        170       180
                 ....*....|....*....|...
gi 738157197 167 AISDGLRQE--TDAIRVTLVSPG 187
Cdd:PRK08993 167 GVTRLMANEwaKHNINVNAIAPG 189
PRK07102 PRK07102
SDR family oxidoreductase;
9-233 2.52e-14

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 69.95  E-value: 2.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILtGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRA-TGGNVDAMAIDVTrpeDLQRIAARALEKHGRI 87
Cdd:PRK07102   2 KKILII-GATSDIARACARRYAAAGARLYLAARDVERLERLADDLRArGAVAVSTHELDIL---DTASHAAFLDSLPALP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK07102  78 DIVLIAVGTLGDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESELadhiTDETARAAMrefrRIALPQEpVAQAIAYAIEQPAGV 233
Cdd:PRK07102 158 FLSGLRNRlfKSGVHVLTVKPGFVRTPM----TAGLKLPGP----LTAQPEE-VAKDIFRAIEKGKDV 216
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
10-144 4.33e-14

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: 69.40  E-value: 4.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIE---KL-----TAlATELRATGGNVDAMAIDVtRPEDLQRIA-ARA 80
Cdd:cd09762    4 KTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpKLpgtiyTA-AEEIEAAGGKALPCIVDI-RDEDQVRAAvEKA 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197  81 LEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIA 144
Cdd:cd09762   82 VEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLS 145
PRK06128 PRK06128
SDR family oxidoreductase;
13-189 4.47e-14

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 70.27  E-value: 4.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  13 ILTGASSGIGEATARHLSRKGHHLFIG-----ARRIEKLTALateLRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK06128  59 LITGADSGIGRATAIAFAREGADIALNylpeeEQDAAEVVQL---IQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAG-VMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGygHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK06128 136 DILVNIAGkQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGA--SIINTGSIQSYQPSPTLLDYASTKAAIV 213
                        170       180
                 ....*....|....*....|....*
gi 738157197 167 AISDGLRQET--DAIRVTLVSPGVV 189
Cdd:PRK06128 214 AFTKALAKQVaeKGIRVNAVAPGPV 238
PRK08703 PRK08703
SDR family oxidoreductase;
8-191 6.15e-14

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 68.80  E-value: 6.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGG-NVDAMAIDV--TRPEDLQRIAAR-ALEK 83
Cdd:PRK08703   5 SDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHpEPFAIRFDLmsAEEKEFEQFAATiAEAT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  84 HGRIDALINNAG-VMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:PRK08703  85 QGKLDGIVHCAGyFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFGASK 164
                        170       180       190
                 ....*....|....*....|....*....|..
gi 738157197 163 FAVRAISDGLRQETD---AIRVTLVSPGVVES 191
Cdd:PRK08703 165 AALNYLCKVAADEWErfgNLRANVLVPGPINS 196
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
10-197 7.27e-14

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 68.94  E-value: 7.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEK-LTALATElraTGGNVDAMAIDVTRPEDLQRIAARALEkhgRID 88
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKeLTKLAEQ---YNSNLTFHSLDLQDVHELETNFNEILS---SIQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 A-------LINNAG-VMPLSPLAALKVEEWNRMLDVNVrgvlhgIAAVLPI---MQE----QGYGHIINIASTGAYTVSP 153
Cdd:PRK06924  76 EdnvssihLINNAGmVAPIKPIEKAESEELITNVHLNL------LAPMILTstfMKHtkdwKVDKRVINISSGAAKNPYF 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 738157197 154 TAAVYCASKFAVRAISDGL----RQETDAIRVTLVSPGVVESELADHI 197
Cdd:PRK06924 150 GWSAYCSSKAGLDMFTQTVateqEEEEYPVKIVAFSPGVMDTNMQAQI 197
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
12-230 7.86e-14

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 67.99  E-value: 7.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLfIGARRIEkltalatelratggnvDAMAIDVTRPEDLqriaARALEKHGRIDALI 91
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEV-ITAGRSS----------------GDYQVDITDEASI----KALFEKVGHFDAIV 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGVMPLSPLAALKVEEWNRMLDVNVRG----VLHGiaavLPIMQEQgyGHIINIASTGAYTVSPTAAVYCASKFAVRA 167
Cdd:cd11731   60 STAGDAEFAPLAELTDADFQRGLNSKLLGqinlVRHG----LPYLNDG--GSITLTSGILAQRPIPGGAAAATVNGALEG 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197 168 ISDGLRQE-TDAIRVTLVSPGVVESELadhitdETARAAMREFRRIalPQEPVAQAIAYAIEQP 230
Cdd:cd11731  134 FVRAAAIElPRGIRINAVSPGVVEESL------EAYGDFFPGFEPV--PAEDVAKAYVRSVEGA 189
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
11-123 1.62e-13

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 66.43  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   11 VVILTGASSGIGEATARHLSRKG-HHLFIGARRI---EKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGaRHLVLLSRSAaprPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPP 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 738157197   87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLH 123
Cdd:pfam08659  82 IRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWN 118
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-187 2.16e-13

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 67.50  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGAS--SGIGEATARHLSRKGHHLFI------------GARRIEKLTaLATELRATGGNVDAMAIDVTRPEDLQR 75
Cdd:PRK12859   7 KVAVVTGVSrlDGIGAAICKELAEAGADIFFtywtaydkempwGVDQDEQIQ-LQEELLKNGVKVSSMELDLTQNDAPKE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  76 IAARALEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRG-VLHGIAAVLPIMQEQGyGHIINIASTGAYTVSPT 154
Cdd:PRK12859  86 LLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRAtTLLSSQFARGFDKKSG-GRIINMTSGQFQGPMVG 164
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 738157197 155 AAVYCASKFAVRAISDGLRQETDAIRVTL--VSPG 187
Cdd:PRK12859 165 ELAYAATKGAIDALTSSLAAEVAHLGITVnaINPG 199
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
12-230 3.38e-13

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 66.00  E-value: 3.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGH-HLFIGARRiekltalatelratggnvdamaidvtrpedlqriaaralekhgriDAL 90
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSpKVLVVSRR---------------------------------------------DVV 35
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  91 INNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAISD 170
Cdd:cd02266   36 VHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQ 115
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 171 GLRQE--TDAIRVTLVSPGVVESE-LADHITDETARAAMREFRRIALPQEPVAQAIAYAIEQP 230
Cdd:cd02266  116 QWASEgwGNGLPATAVACGTWAGSgMAKGPVAPEEILGNRRHGVRTMPPEEVARALLNALDRP 178
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
9-99 1.00e-12

Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 66.56  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:COG5748    6 KSTVIITGASSGVGLYAAKALADRGWHVIMACRDLEKAEAAAQELGIPPDSYTIIHIDLASLESVRRFVADFRALGRPLD 85
                         90
                 ....*....|..
gi 738157197  89 ALINNAGV-MPL 99
Cdd:COG5748   86 ALVCNAAVyYPL 97
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-192 1.92e-12

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 64.78  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATgGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK05786   6 KKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKY-GNIHYVVGDVSSTESARNVIEKAAKVLNAIDG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALKveEWNRMLDVNVRGVLHGIAAVLPIMQEqgyGHIINIAST--GAYTVSPTAAVYCASKFAVRA 167
Cdd:PRK05786  85 LVVTVGGYVEDTVEEFS--GLEEMLTNHIKIPLYAVNASLRFLKE---GSSIVLVSSmsGIYKASPDQLSYAVAKAGLAK 159
                        170       180
                 ....*....|....*....|....*..
gi 738157197 168 ISDGLRQE--TDAIRVTLVSPGVVESE 192
Cdd:PRK05786 160 AVEILASEllGRGIRVNGIAPTTISGD 186
PRK12742 PRK12742
SDR family oxidoreductase;
8-225 2.34e-12

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 64.39  E-value: 2.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHL-FIGARRIEKLTALATELRATGGNVDAMAIDvtrpEDLQRIAARalekhGR 86
Cdd:PRK12742   5 TGKKVLVLGGSRGIGAAIVRRFVTDGANVrFTYAGSKDAAERLAQETGATAVQTDSADRD----AVIDVVRKS-----GA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHgiAAVLPIMQEQGYGHIINIASTGAYTVS-PTAAVYCASKFAV 165
Cdd:PRK12742  76 LDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYH--ASVEAARQMPEGGRIIIIGSVNGDRMPvAGMAAYAASKSAL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197 166 RAISDGLRQE--TDAIRVTLVSPGVVESEL--ADHITDETARAAMrEFRRIALPQEpVAQAIAY 225
Cdd:PRK12742 154 QGMARGLARDfgPRGITINVVQPGPIDTDAnpANGPMKDMMHSFM-AIKRHGRPEE-VAGMVAW 215
PRK07806 PRK07806
SDR family oxidoreductase;
8-239 3.01e-12

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 64.36  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGAR-RIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:PRK07806   5 PGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRqKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNA-GVMP--LSPLAALKVeewNRMLDVNVrgvlhgIAAVLPIMQEQgyGHIINIASTGAYTVSPTAAV--YCAS 161
Cdd:PRK07806  85 LDALVLNAsGGMEsgMDEDYAMRL---NRDAQRNL------ARAALPLMPAG--SRVVFVTSHQAHFIPTVKTMpeYEPV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 162 KFAVRAISDGLRQETDA-----IRVTLVSPGVVESELADHITDETARAAMREFRRIALPQEPV---AQAIAYAIEQPAGV 233
Cdd:PRK07806 154 ARSKRAGEDALRALRPElaekgIGFVVVSGDMIEGTVTATLLNRLNPGAIEARREAAGKLYTVsefAAEVARAVTAPVPS 233

                 ....*.
gi 738157197 234 DISELI 239
Cdd:PRK07806 234 GHIEYV 239
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
10-164 3.13e-12

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: 64.41  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAT-GGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd05322    3 QVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEyGEKAYGFGADATNEQSVIALSKGVDEIFKRVD 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGY-GHIINIASTGAYTVSPTAAVYCASKFA 164
Cdd:cd05322   83 LLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIqGRIIQINSKSGKVGSKHNSGYSAAKFG 159
PRK09134 PRK09134
SDR family oxidoreductase;
1-231 6.04e-12

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 63.41  E-value: 6.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   1 MKTVVSETSKVVILTGASSGIGEATARHLSRKGHHLFIGARR-IEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAAR 79
Cdd:PRK09134   1 SPPMSMAAPRAALVTGAARRIGRAIALDLAAHGFDVAVHYNRsRDEAEALAAEIRALGRRAVALQADLADEAEVRALVAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  80 ALEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRG--VL-HGIAAVLPimqEQGYGHIINIASTGAYTVSPTAA 156
Cdd:PRK09134  81 ASAALGPITLLVNNASLFEYDSAASFTRASWDRHMATNLRApfVLaQAFARALP---ADARGLVVNMIDQRVWNLNPDFL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 157 VYCASKFAVRAISDGLRQE-TDAIRVTLVSPGvveseladhITDETARAAMREFR---------RIALPQEpVAQAIAYA 226
Cdd:PRK09134 158 SYTLSKAALWTATRTLAQAlAPRIRVNAIGPG---------PTLPSGRQSPEDFArqhaatplgRGSTPEE-IAAAVRYL 227

                 ....*
gi 738157197 227 IEQPA 231
Cdd:PRK09134 228 LDAPS 232
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
11-123 3.88e-11

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 62.38  E-value: 3.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  11 VVILTGASSGIGEATARHLSRKGhhlfiGAR-----------RIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAAR 79
Cdd:cd08953  207 VYLVTGGAGGIGRALARALARRY-----GARlvllgrsplppEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEK 281
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 738157197  80 ALEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLH 123
Cdd:cd08953  282 VRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLN 325
PRK08340 PRK08340
SDR family oxidoreductase;
12-95 4.32e-11

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 61.36  E-value: 4.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGnVDAMAIDVTRPEDLQRIAARALEKHGRIDALI 91
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGE-VYAVKADLSDKDDLKNLVKEAWELLGGIDALV 81

                 ....
gi 738157197  92 NNAG 95
Cdd:PRK08340  82 WNAG 85
PRK06101 PRK06101
SDR family oxidoreductase;
9-211 4.83e-11

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 60.65  E-value: 4.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLtalaTELRATGGNVDAMAIDVTRPEDLQriaaRALEKHGRI- 87
Cdd:PRK06101   1 MTAVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVL----DELHTQSANIFTLAFDVTDHPGTK----AALSQLPFIp 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEqgyGHIINIASTGAYTVS-PTAAVYCASKFAV- 165
Cdd:PRK06101  73 ELWIFNAGDCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSC---GHRVVIVGSIASELAlPRAEAYGASKAAVa 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738157197 166 ---RAISDGLRQEtdAIRVTLVSPGVVESELADHITDE-----TARAAMREFRR 211
Cdd:PRK06101 150 yfaRTLQLDLRPK--GIEVVTVFPGFVATPLTDKNTFAmpmiiTVEQASQEIRA 201
PRK06940 PRK06940
short chain dehydrogenase; Provisional
8-108 9.88e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 60.42  E-value: 9.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASsGIGEATARHLSrKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARAlEKHGRI 87
Cdd:PRK06940   1 MKEVVVVIGAG-GIGQAIARRVG-AGKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATA-QTLGPV 77
                         90       100
                 ....*....|....*....|...
gi 738157197  88 DALINNAGVMP--LSPLAALKVE 108
Cdd:PRK06940  78 TGLVHTAGVSPsqASPEAILKVD 100
PRK12744 PRK12744
SDR family oxidoreductase;
8-187 1.82e-10

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 59.37  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGhhlfigARRI--------EKLTALAT--ELRATGGNVDAMAIDVTRPEDLQRIA 77
Cdd:PRK12744   7 KGKVVLIAGGAKNLGGLIARDLAAQG------AKAVaihynsaaSKADAEETvaAVKAAGAKAVAFQADLTTAAAVEKLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  78 ARALEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRgvlhgiaAVLPIMQEQG-----YGHIINIAST--GAYT 150
Cdd:PRK12744  81 DDAKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSK-------SAFFFIKEAGrhlndNGKIVTLVTSllGAFT 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 738157197 151 vsPTAAVYCASKFAV----RAISD--GLRQetdaIRVTLVSPG 187
Cdd:PRK12744 154 --PFYSAYAGSKAPVehftRAASKefGARG----ISVTAVGPG 190
PRK12747 PRK12747
short chain dehydrogenase; Provisional
10-193 2.62e-10

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 58.93  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFI--GARRiEKLTALATELRATGGNVDAMAIDVTR---PEDLQRIAARALEKH 84
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIhyGNRK-EEAEETVYEIQSNGGSAFSIGANLESlhgVEALYSSLDNELQNR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  85 ---GRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQgyGHIINIASTGAYTVSPTAAVYCAS 161
Cdd:PRK12747  84 tgsTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDN--SRIINISSAATRISLPDFIAYSMT 161
                        170       180       190
                 ....*....|....*....|....*....|....
gi 738157197 162 KFAVRAISDGLRQETDA--IRVTLVSPGVVESEL 193
Cdd:PRK12747 162 KGAINTMTFTLAKQLGArgITVNAILPGFIKTDM 195
PRK07791 PRK07791
short chain dehydrogenase; Provisional
10-169 4.22e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 58.53  E-value: 4.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKG---------HHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARA 80
Cdd:PRK07791   7 RVVIVTGAGGGIGRAHALAFAAEGarvvvndigVGLDGSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLVDAA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  81 LEKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRG---VLHGIAAVLPIMQEQGY---GHIINIASTGAYTVSPT 154
Cdd:PRK07791  87 VETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGhfaTLRHAAAYWRAESKAGRavdARIINTSSGAGLQGSVG 166
                        170
                 ....*....|....*
gi 738157197 155 AAVYCASKFAVRAIS 169
Cdd:PRK07791 167 QGNYSAAKAGIAALT 181
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
12-149 7.83e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 57.68  E-value: 7.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRatggnVDAMAIDVTRPEDLQRIAAralekhgRIDALI 91
Cdd:COG0451    2 ILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPG-----VEFVRGDLRDPEALAAALA-------GVDAVV 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197  92 NNAGVmplsplAALKVEEWNRMLDVNVRGVLHgiaaVLPIMQEQGYGHIINIASTGAY 149
Cdd:COG0451   70 HLAAP------AGVGEEDPDETLEVNVEGTLN----LLEAARAAGVKRFVYASSSSVY 117
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
11-225 7.91e-10

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 57.50  E-value: 7.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  11 VVILTGASSGIGEATARHLSRKGHHLfigarriekltaLATELRAtgGNVDAmaiDVTRPEDLQRIAARALEK-HGRIDA 89
Cdd:cd05328    1 TIVITGAASGIGAATAELLEDAGHTV------------IGIDLRE--ADVIA---DLSTPEGRAAAIADVLARcSGVLDG 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLaalkveewNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAY-------------------- 149
Cdd:cd05328   64 LVNCAGVGGTTVA--------GLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAgwaqdklelakalaagtear 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 150 -------TVSPTAAVYCASKFAV-----RAISDGLRQEtdAIRVTLVSPGVVESEL-----ADHITDETARAAMREFRRI 212
Cdd:cd05328  136 avalaehAGQPGYLAYAGSKEALtvwtrRRAATWLYGA--GVRVNTVAPGPVETPIlqaflQDPRGGESVDAFVTPMGRR 213
                        250
                 ....*....|...
gi 738157197 213 ALPQEpVAQAIAY 225
Cdd:cd05328  214 AEPDE-IAPVIAF 225
PRK06953 PRK06953
SDR family oxidoreductase;
9-208 1.11e-09

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 56.62  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTAlateLRATGGnvDAMAIDVTRPEDlqrIAARALEKHG-RI 87
Cdd:PRK06953   1 MKTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAA----LQALGA--EALALDVADPAS---VAGLAWKLDGeAL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  88 DALINNAGVMPLSPLAALKV--EEWNRMLDVNVRGVLHGIAAVLPIMQEQG---------YGHIINIASTGAYTvsptaa 156
Cdd:PRK06953  72 DAAVYVAGVYGPRTEGVEPItrEDFDAVMHTNVLGPMQLLPILLPLVEAAGgvlavlssrMGSIGDATGTTGWL------ 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 157 vYCASKFAVR-AISDGLRQETDAIRVTLvSPGVVESEL---ADHITDETARAAMRE 208
Cdd:PRK06953 146 -YRASKAALNdALRAASLQARHATCIAL-HPGWVRTDMggaQAALDPAQSVAGMRR 199
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
11-211 3.23e-09

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: 55.69  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   11 VVILTGASSGIGEATARHLSR----KGHHLFIGARRIEKLTALATELRAT--GGNVDAMAIDVTRPEDLQRIaARALEKH 84
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEAGLEQL-LKALREL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   85 GRIDA-----LINNAGVmpLSPLAALKVE-----EWNRMLDVNVRGVLHGIAAVLPIMQE-QGYGH-IINIASTGAYTVS 152
Cdd:TIGR01500  81 PRPKGlqrllLINNAGT--LGDVSKGFVDlsdstQVQNYWALNLTSMLCLTSSVLKAFKDsPGLNRtVVNISSLCAIQPF 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197  153 PTAAVYCASKFA----VRAISdgLRQETDAIRVTLVSPGVVESELADHITDETARAAMREFRR 211
Cdd:TIGR01500 159 KGWALYCAGKAArdmlFQVLA--LEEKNPNVRVLNYAPGVLDTDMQQQVREESVDPDMRKGLQ 219
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
12-123 1.41e-08

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 54.31  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGH-HLFIGARRIEKL--TALATELRATGGNVDAMAIDVTRPEDLQRIAARaLEKHGRID 88
Cdd:cd05274  153 YLITGGLGGLGLLVARWLAARGArHLVLLSRRGPAPraAARAALLRAGGARVSVVRCDVTDPAALAALLAE-LAAGGPLA 231
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 738157197  89 ALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLH 123
Cdd:cd05274  232 GVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALN 266
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
12-118 1.54e-08

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 53.65  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALAtelRATGGNVDAMAIDVTRPEDLQRIaARALEKHGRIDALI 91
Cdd:cd08951   10 IFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAK---AACPGAAGVLIGDLSSLAETRKL-ADQVNAIGRFDAVI 85
                         90       100
                 ....*....|....*....|....*..
gi 738157197  92 NNAGVMpLSPLAALKVEEWNRMLDVNV 118
Cdd:cd08951   86 HNAGIL-SGPNRKTPDTGIPAMVAVNV 111
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
9-189 2.10e-08

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: 53.10  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHH-----LFIGARRIEKLTALATELRAtggnvdamaidvtrpEDLQRIAARALEK 83
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWvasidLAENEEADASIIVLDSDSFT---------------EQAKQVVASVARL 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  84 HGRIDALINNAGVMPL-SPLAALKVEEWNRMLDVNVRGVLhgIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:cd05334   66 SGKVDALICVAGGWAGgSAKSKSFVKNWDLMWKQNLWTSF--IASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYGAAK 143
                        170       180       190
                 ....*....|....*....|....*....|.
gi 738157197 163 FAVRAISDGLRQETD----AIRVTLVSPGVV 189
Cdd:cd05334  144 AAVHQLTQSLAAENSglpaGSTANAILPVTL 174
PRK07985 PRK07985
SDR family oxidoreductase;
13-193 2.32e-08

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 53.46  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  13 ILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTA--LATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDAL 90
Cdd:PRK07985  53 LVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDAqdVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALGGLDIM 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  91 INNAGVMPLSP-LAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGygHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK07985 133 ALVAGKQVAIPdIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGA--SIITTSSIQAYQPSPHLLDYAATKAAILNYS 210
                        170       180
                 ....*....|....*....|....*.
gi 738157197 170 DGLRQET--DAIRVTLVSPGVVESEL 193
Cdd:PRK07985 211 RGLAKQVaeKGIRVNIVAPGPIWTAL 236
PRK06720 PRK06720
hypothetical protein; Provisional
10-117 2.81e-08

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 51.90  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRIDA 89
Cdd:PRK06720  17 KVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVISITLNAFSRIDM 96
                         90       100
                 ....*....|....*....|....*...
gi 738157197  90 LINNAGVMPLSPLAALKVEEWNRMLDVN 117
Cdd:PRK06720  97 LFQNAGLYKIDSIFSRQQENDSNVLCIN 124
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
9-150 3.19e-08

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 52.98  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGNVDAMA--IDVTRPEDLQRIAARALEKHGR 86
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQNIFLhiVDMSDPKQVWEFVEEFKEEGKK 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197  87 IDALINNAGVMPLSplAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYT 150
Cdd:cd09808   81 LHVLINNAGCMVNK--RELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGGMLV 142
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-169 5.52e-08

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 52.48  E-value: 5.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   1 MKTVVSETSKVVILTGASSGIGEATARHLSRKGHHLFIG--ARRIEKLTALAtELRATGGNVDAMAIDVTrpedlQRIAA 78
Cdd:PRK07792   4 TTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNdvASALDASDVLD-EIRAAGAKAVAVAGDIS-----QRATA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  79 RAL----EKHGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRG---VLHGIAAVLPIMQEQG----YGHIINIASTG 147
Cdd:PRK07792  78 DELvataVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGhflLTRNAAAYWRAKAKAAggpvYGRIVNTSSEA 157
                        170       180
                 ....*....|....*....|..
gi 738157197 148 AYTVSPTAAVYCASKFAVRAIS 169
Cdd:PRK07792 158 GLVGPVGQANYGAAKAGITALT 179
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
10-101 6.26e-08

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 52.52  E-value: 6.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGH-HLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:cd09810    2 GTVVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRPLD 81
                         90
                 ....*....|....
gi 738157197  89 ALINNAGV-MPLSP 101
Cdd:cd09810   82 ALVCNAAVyLPTAK 95
PRK08339 PRK08339
short chain dehydrogenase; Provisional
8-203 2.76e-07

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 50.24  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   8 TSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGG-NVDAMAIDVTRPEDLQRIaARALEKHGR 86
Cdd:PRK08339   7 SGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNvDVSYIVADLTKREDLERT-VKELKNIGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVR 166
Cdd:PRK08339  86 PDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRISMA 165
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 738157197 167 AISDGLRQET--DAIRVTLVSPGVVESELADHITDETAR 203
Cdd:PRK08339 166 GLVRTLAKELgpKGITVNGIMPGIIRTDRVIQLAQDRAK 204
PRK12746 PRK12746
SDR family oxidoreductase;
10-200 4.04e-07

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 49.65  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIG-ARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEK----- 83
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNElqirv 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  84 -HGRIDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQgyGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:PRK12746  87 gTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAEVRLGFTGSIAYGLSK 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 738157197 163 FAVRAISDGLRQE--TDAIRVTLVSPGVVESELADHITDE 200
Cdd:PRK12746 165 GALNTMTLPLAKHlgERGITVNTIMPGYTKTDINAKLLDD 204
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
10-100 4.52e-07

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 49.52  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATEL--RATGGNVDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:cd09809    2 KVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRIleEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSPL 81
                         90
                 ....*....|...
gi 738157197  88 DALINNAGVMPLS 100
Cdd:cd09809   82 HVLVCNAAVFALP 94
PRK05854 PRK05854
SDR family oxidoreductase;
3-97 4.92e-07

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 49.68  E-value: 4.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   3 TVVSETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAT--GGNVDAMAIDVTrpeDLQRIAA-- 78
Cdd:PRK05854   8 TVPDLSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAvpDAKLSLRALDLS---SLASVAAlg 84
                         90       100
                 ....*....|....*....|
gi 738157197  79 RALEKHGR-IDALINNAGVM 97
Cdd:PRK05854  85 EQLRAEGRpIHLLINNAGVM 104
PRK09186 PRK09186
flagellin modification protein A; Provisional
10-145 6.04e-07

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 49.22  E-value: 6.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGN--VDAMAIDVTRPEDLQRIAARALEKHGRI 87
Cdd:PRK09186   5 KTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSkkLSLVELDITDQESLEEFLSKSAEKYGKI 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738157197  88 DALINNAgvMPLSplaalkvEEW-NRMLDVNVRGV-----LHGIAAVLpIMQE-------QGYGHIINIAS 145
Cdd:PRK09186  85 DGAVNCA--YPRN-------KDYgKKFFDVSLDDFnenlsLHLGSSFL-FSQQfakyfkkQGGGNLVNISS 145
PRK08416 PRK08416
enoyl-ACP reductase;
9-217 1.82e-06

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 47.84  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHL-FIGARRIEKLTALATELRATGG-NVDAMAIDVTRPEDLQRIAARALEKHGR 86
Cdd:PRK08416   8 GKTLVISGGTRGIGKAIVYEFAQSGVNIaFTYNSNVEEANKIAEDLEQKYGiKAKAYPLNILEPETYKELFKKIDEDFDR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  87 IDALINNA------GVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCA 160
Cdd:PRK08416  88 VDFFISNAiisgraVVGGYTKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISLSSTGNLVYIENYAGHGT 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197 161 SKFAVRAISDGLRQETDA--IRVTLVSPGVVESELADHITD-ETARAAMRE---FRRIALPQE 217
Cdd:PRK08416 168 SKAAVETMVKYAATELGEknIRVNAVSGGPIDTDALKAFTNyEEVKAKTEElspLNRMGQPED 230
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
12-123 2.43e-06

ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 47.94  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKG--HHLFIGAR--RIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAArALEKHGRI 87
Cdd:cd08952  233 VLVTGGTGALGAHVARWLARRGaeHLVLTSRRgpDAPGAAELVAELTALGARVTVAACDVADRDALAALLA-ALPAGHPL 311
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 738157197  88 DALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLH 123
Cdd:cd08952  312 TAVVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARH 347
PRK07578 PRK07578
short chain dehydrogenase; Provisional
12-228 2.82e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 46.73  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKghHLFIGARRiekltalatelraTGGNVdamAIDVTRPEDLQRIaaraLEKHGRIDALI 91
Cdd:PRK07578   3 ILVIGASGTIGRAVVAELSKR--HEVITAGR-------------SSGDV---QVDITDPASIRAL----FEKVGKVDAVV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGVMPLSPLAALKVEEWNRMLD------VN-VRGVLH------------GIAAVLPIMQeqgyghiiniaSTGAYTVS 152
Cdd:PRK07578  61 SAAGKVHFAPLAEMTDEDFNVGLQsklmgqVNlVLIGQHylndggsftltsGILSDEPIPG-----------GASAATVN 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738157197 153 ptAAVycaSKFAVRAISDGLRQetdaIRVTLVSPGVVEseladhitdETArAAMREFRR--IALPQEPVAQAIAYAIE 228
Cdd:PRK07578 130 --GAL---EGFVKAAALELPRG----IRINVVSPTVLT---------ESL-EKYGPFFPgfEPVPAARVALAYVRSVE 188
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
12-197 6.99e-06

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 45.09  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGnvdamaIDVTRPEDLQRIAAralekhgRIDALI 91
Cdd:cd05226    1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKRLSKEDQEPVAVVE------GDLRDLDSLSDAVQ-------GVDVVI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGvmplsplaalkveeWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRaisdg 171
Cdd:cd05226   68 HLAG--------------APRDTRDFCEVDVEGTRNVLEAAKEAGVKHFIFISSLGAYGDLHEETEPSPSSPYLA----- 128
                        170       180       190
                 ....*....|....*....|....*....|..
gi 738157197 172 LRQETDAI------RVTLVSPGVVESELADHI 197
Cdd:cd05226  129 VKAKTEAVlreaslPYTIVRPGVIYGDLARAI 160
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
10-187 8.44e-06

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


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 45.23  E-value: 8.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILtGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRATGGnvdamaiDVTRPEDLqriaARALEKHgriDA 89
Cdd:COG2910    1 KIAVI-GATGRVGSLIVREALARGHEVTALVRNPEKLPDEHPGLTVVVG-------DVLDPAAV----AEALAGA---DA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAALkveewnrmldvnvrgvLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCAS-KFAVRAI 168
Cdd:COG2910   66 VVSALGAGGGNPTTVL----------------SDGARALIDAMKAAGVKRLIVVGGAGSLDVAPGLGLDTPGfPAALKPA 129
                        170       180
                 ....*....|....*....|....
gi 738157197 169 SDGLRQETDAIR-----VTLVSPG 187
Cdd:COG2910  130 AAAKAAAEELLRasdldWTIVRPA 153
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
9-100 1.60e-05

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 45.07  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHL-----SRKGHHLFIGARRIEKLTALATELRAT----GGNVDAMAIDVTRPEDLQRIAAR 79
Cdd:cd08941    1 RKVVLVTGANSGLGLAICERLlaeddENPELTLILACRNLQRAEAACRALLAShpdaRVVFDYVLVDLSNMVSVFAAAKE 80
                         90       100
                 ....*....|....*....|.
gi 738157197  80 ALEKHGRIDALINNAGVMPLS 100
Cdd:cd08941   81 LKKRYPRLDYLYLNAGIMPNP 101
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
12-165 1.76e-05

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


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 44.45  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALAtelratGGNVDAMAIDVTRPEDLqriaARALEkhgRIDALI 91
Cdd:COG0702    2 ILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALA------AAGVEVVQGDLDDPESL----AAALA---GVDAVF 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738157197  92 NNAGVMPlsplaalkveewnrmlDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAavYCASKFAV 165
Cdd:COG0702   69 LLVPSGP----------------GGDFAVDVEGARNLADAAKAAGVKRIVYLSALGADRDSPSP--YLRAKAAV 124
PLN00015 PLN00015
protochlorophyllide reductase
13-96 5.85e-05

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 43.54  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  13 ILTGASSGIGEATARHLSRKG-HHLFIGARRIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARaLEKHGR-IDAL 90
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGkWHVVMACRDFLKAERAAKSAGMPKDSYTVMHLDLASLDSVRQFVDN-FRRSGRpLDVL 79

                 ....*.
gi 738157197  91 INNAGV 96
Cdd:PLN00015  80 VCNAAV 85
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
12-123 5.93e-05

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 43.79  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGH--HLFIGARR---IEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAARALEKHgR 86
Cdd:cd08956  196 VLITGGTGTLGALLARHLVTEHGvrHLLLVSRRgpdAPGAAELVAELAALGAEVTVAACDVADRAALAALLAAVPADH-P 274
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 738157197  87 IDALINNAGVMPLSPLAALKVEEWNRMLDVNVRGVLH 123
Cdd:cd08956  275 LTAVVHAAGVLDDGVLTSLTPERLDAVLRPKVDAAWH 311
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
11-192 7.88e-05

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: 42.56  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  11 VVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATeLRATGGNVDAMAidvtrPEDLQRIAARALEKHGRIDAL 90
Cdd:cd05361    3 IALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAERQA-FESENPGTKALS-----EQKPEELVDAVLQAGGAIDVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  91 INN-AGVMPLSPLAALKVEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTAAVYCASKFAVRAIS 169
Cdd:cd05361   77 VSNdYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALA 156
                        170       180
                 ....*....|....*....|....*
gi 738157197 170 DGLRQE--TDAIRVTLVSPGVVESE 192
Cdd:cd05361  157 ESLAKElsRDNILVYAIGPNFFNSP 181
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
9-164 1.12e-04

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 42.23  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   9 SKVVILTGASSGIGEATARHLSRKGHHLfIGARRIEKlTALAtELRATGgnVDAMAIDVTRPEDLQRIAARALEKHGRID 88
Cdd:PRK06483   2 PAPILITGAGQRIGLALAWHLLAQGQPV-IVSYRTHY-PAID-GLRQAG--AQCIQADFSTNAGIMAFIDELKQHTDGLR 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197  89 ALINNAGV-MPLSPLAALKvEEWNRMLDVNVRGVLHGIAAVLPIMQEQGYG--HIINIASTGAYTVSPTAAVYCASKFA 164
Cdd:PRK06483  77 AIIHNASDwLAEKPGAPLA-DVLARMMQIHVNAPYLLNLALEDLLRGHGHAasDIIHITDYVVEKGSDKHIAYAASKAA 154
PRK08303 PRK08303
short chain dehydrogenase; Provisional
10-224 1.56e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 41.91  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGAR----------RIEKLTALATELRATGGNVDAMAIDVTRPEDLQRIAAR 79
Cdd:PRK08303   9 KVALVAGATRGAGRGIAVELGAAGATVYVTGRstrarrseydRPETIEETAELVTAAGGRGIAVQVDHLVPEQVRALVER 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  80 ALEKHGRIDALINNA-GVMPLS----PLAALKVEEWNRMLDVNVRGvlHGIAA--VLPIMQEQGYGHIINIASTGA---- 148
Cdd:PRK08303  89 IDREQGRLDILVNDIwGGEKLFewgkPVWEHSLDKGLRMLRLAIDT--HLITShfALPLLIRRPGGLVVEITDGTAeyna 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 149 --YTVSPtaaVYCASKFAVRAISDGLRQETDAIRVTLVS--PGVVESELA-DH--ITDETARAAMREFRRIALPQEP--V 219
Cdd:PRK08303 167 thYRLSV---FYDLAKTSVNRLAFSLAHELAPHGATAVAltPGWLRSEMMlDAfgVTEENWRDALAKEPHFAISETPryV 243

                 ....*
gi 738157197 220 AQAIA 224
Cdd:PRK08303 244 GRAVA 248
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
6-95 6.74e-04

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


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 40.21  E-value: 6.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   6 SETSKVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELRAtgGNVDAMAIDVTRPEDLQRIAARAlekhg 85
Cdd:COG3268    2 TEREFDIVVYGATGYTGRLVAEYLARRGLRPALAGRNAAKLEAVAAELGA--ADLPLRVADLDDPASLAALLAGT----- 74
                         90
                 ....*....|
gi 738157197  86 riDALINNAG 95
Cdd:COG3268   75 --RVVLNTVG 82
PRK05884 PRK05884
SDR family oxidoreductase;
12-160 7.08e-04

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 39.79  E-value: 7.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALATELratggNVDAMAIDVTRPEDLQriAARALEKHgRIDALI 91
Cdd:PRK05884   3 VLVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKEL-----DVDAIVCDNTDPASLE--EARGLFPH-HLDTIV 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738157197  92 N------NAGVMPLSPLAALkVEEWNRMLDVNVrgvlhgIAAVLPIM----QEQGYGHIINIASTGAYTVSPTAAVYCA 160
Cdd:PRK05884  75 NvpapswDAGDPRTYSLADT-ANAWRNALDATV------LSAVLTVQsvgdHLRSGGSIISVVPENPPAGSAEAAIKAA 146
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
12-199 9.49e-04

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 39.69  E-value: 9.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEA-TARHLSRKGHHLFIGARRIEKLTALATE-LRATGGN-VDAMAIDVTRPEDLQRIAARALEkHGRID 88
Cdd:PRK07904  11 ILLLGGTSEIGLAiCERYLKNAPARVVLAALPDDPRRDAAVAqMKAAGASsVEVIDFDALDTDSHPKVIDAAFA-GGDVD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  89 ------ALINNAGVMPLSPLAALKVEEWNRMLDVNVrGVLHGIAavlpiMQEQGYGHIINIASTGAYTVSPTAAVYCASK 162
Cdd:PRK07904  90 vaivafGLLGDAEELWQNQRKAVQIAEINYTAAVSV-GVLLGEK-----MRAQGFGQIIAMSSVAGERVRRSNFVYGSTK 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 738157197 163 FAV----RAISDGLRQEtdAIRVTLVSPGVVESELADHITD 199
Cdd:PRK07904 164 AGLdgfyLGLGEALREY--GVRVLVVRPGQVRTRMSAHAKE 202
NAD_binding_10 pfam13460
NAD(P)H-binding;
16-230 1.10e-03

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 38.74  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   16 GASSGIGEATARHLSRKGHHLFIGARRIEKLTALATElratgGNVDAMAIDVTRPEDLqriaARALEKHgriDALINNAG 95
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALVRNPEKLADLEDH-----PGVEVVDGDVLDPDDL----AEALAGQ---DAVISALG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197   96 vmplsplaalkveewnrmldvNVRGVLHGIAAVLPIMQEQGYGHIINIASTGAYTVSPTaAVYCASKFAVRAISDGLRQE 175
Cdd:pfam13460  69 ---------------------GGGTDETGAKNIIDAAKAAGVKRFVLVSSLGVGDEVPG-PFGPWNKEMLGPYLAAKRAA 126
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738157197  176 TDAIRV-----TLVSPGvveseladHITDETARAAMR-----EFRRIALPQEPVAQAIAYAIEQP 230
Cdd:pfam13460 127 EELLRAsgldyTIVRPG--------WLTDGPTTGYRVtgkgePFKGGSISRADVADVLVALLDDP 183
PRK08177 PRK08177
SDR family oxidoreductase;
10-208 1.66e-03

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 38.47  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGASSGIGEATARHLSRKGHHLFIGARRIEKltalATELRATGGnVDAMAIDVTRPEDLQRIAARALEKhgRIDA 89
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQ----DTALQALPG-VHIEKLDMNDPASLDQLLQRLQGQ--RFDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVM-PL-SPLAALKVEEW------NRMLDVNVRGVLHGI----AAVLPIMQEQgyghiinIASTGAyTVSPTAAV 157
Cdd:PRK08177  75 LFVNAGISgPAhQSAADATAAEIgqlfltNAIAPIRLARRLLGQvrpgQGVLAFMSSQ-------LGSVEL-PDGGEMPL 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 738157197 158 YCASKFAVRAISDGLRQETDAIRVTLVS--PGVVESEL---ADHITDETARAAMRE 208
Cdd:PRK08177 147 YKASKAALNSMTRSFVAELGEPTLTVLSmhPGWVKTDMggdNAPLDVETSVKGLVE 202
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
12-189 2.11e-03

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 38.81  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRKGHHLFIGARRIEKLTALatelraTGGNVDAMAIDVTRPEDLqriaARALEKhgrIDALI 91
Cdd:cd05228    1 ILVTGATGFLGSNLVRALLAQGYRVRALVRSGSDAVLL------DGLPVEVVEGDLTDAASL----AAAMKG---CDRVF 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  92 NNAGVMPLSPlaalkvEEWNRMLDVNVRGVLHGIAAVLpimqEQGYGHIINIASTGAYTVSPTAAV-------------- 157
Cdd:cd05228   68 HLAAFTSLWA------KDRKELYRTNVEGTRNVLDAAL----EAGVRRVVHTSSIAALGGPPDGRIdettpwnerpfpnd 137
                        170       180       190
                 ....*....|....*....|....*....|...
gi 738157197 158 YCASKF-AVRAISDGLRQETDairVTLVSPGVV 189
Cdd:cd05228  138 YYRSKLlAELEVLEAAAEGLD---VVIVNPSAV 167
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
65-225 3.15e-03

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 37.67  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  65 IDVTRPEDLQRIAARAlekHGRIDALINNAGVMPLSPLAALkveewnrmLDVNVRGVLHGIAAVLPIMQEQgyGHIINIA 144
Cdd:PRK12428  30 ADLGDPASIDAAVAAL---PGRIDALFNIAGVPGTAPVELV--------ARVNFLGLRHLTEALLPRMAPG--GAIVNVA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 145 STGAY-------TVSPTAAV--------------------YCASKFAV-----RAISDGLRQEtdAIRVTLVSPGVVESE 192
Cdd:PRK12428  97 SLAGAewpqrleLHKALAATasfdegaawlaahpvalatgYQLSKEALilwtmRQAQPWFGAR--GIRVNCVAPGPVFTP 174
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 738157197 193 LADHIT----DETARAAMREFRRIALPQEpVAQAIAY 225
Cdd:PRK12428 175 ILGDFRsmlgQERVDSDAKRMGRPATADE-QAAVLVF 210
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
12-247 6.11e-03

UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 37.35  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  12 VILTGASSGIGEATARHLSRK--GHHLFIGARRIEKLTALATELratggnvdaMAIDVTRPEdlqriAARALEKHgRIDA 89
Cdd:cd05240    1 ILVTGAAGGLGRLLARRLAASprVIGVDGLDRRRPPGSPPKVEY---------VRLDIRDPA-----AADVFRER-EADA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  90 LINNAGVMPLSPLAAlkveewnRMLDVNVRGVLHgiaaVLPIMQEQGYGHIINIASTGAYTVSPTAAV------------ 157
Cdd:cd05240   66 VVHLAFILDPPRDGA-------ERHRINVDGTQN----VLDACAAAGVPRVVVTSSVAVYGAHPDNPApltedaplrgsp 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197 158 ---YCASKFAVRAISDGLRQETDAIRVTLVSPGVVeseLADHITDETARAamREFRRIALPQEP-----------VAQAI 223
Cdd:cd05240  135 efaYSRDKAEVEQLLAEFRRRHPELNVTVLRPATI---LGPGTRNTTRDF--LSPRRLPVPGGFdppfqflheddVARAL 209
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 738157197 224 AYAI-EQPAGV-------------DISELIVRPVASPH 247
Cdd:cd05240  210 VLAVrAGATGIfnvagdgpvplslVLALLGRRPVPLPS 247
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
10-136 8.58e-03

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 36.54  E-value: 8.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738157197  10 KVVILTGA--SSGIGEATARHLSRKGHHLFI---GARRIEKLTALATELratgGNVDAMAIDVTRPEDLQRIAARALEKH 84
Cdd:COG0623    6 KRGLITGVanDRSIAWGIAKALHEEGAELAFtyqGEALKKRVEPLAEEL----GSALVLPCDVTDDEQIDALFDEIKEKW 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738157197  85 GRIDALINNAGvmpLSPLAALKveewNRMLDVNVRGV----------LHGIA-AVLPIMQEQG 136
Cdd:COG0623   82 GKLDFLVHSIA---FAPKEELG----GRFLDTSREGFllamdisaysLVALAkAAEPLMNEGG 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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