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Conserved domains on  [gi|6320089|ref|NP_010169|]
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short-chain dehydrogenase/reductase [Saccharomyces cerevisiae S288C]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143197)

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

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  19011750|19011748|12604210|19027726|20423462

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 40-282 1.07e-88

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: 264.87  E-value: 1.07e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADIQsfPTFAQVEYNNI-------FYYQCDITSLDEIKNLKKAIERDHGNIN 112
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDIN--EKGAEETANNVrkaggkvHYYKCDVSKREEVYEAAKKIKKEVGDVT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  113 IIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGF 192
Cdd:cd05339  79 ILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGF 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  193 HKCMSRHFRSlsteCNKTGIKTLLVCPGKIKTNMFIDVPTPSKLLAPDIIPSQLALAIISAMEHNhLQTLNAPYYVNLVP 272
Cdd:cd05339 159 HESLRLELKA----YGKPGIKTTLVCPYFINTGMFQGVKTPRPLLAPILEPEYVAEKIVRAILTN-QQMLYLPFYAYFLP 233

                       250
                ....*....|
gi 6320089  273 FFKTLsWPYR 282
Cdd:cd05339 234 ILKRT-LPTP 242
 
Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 40-282 1.07e-88

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: 264.87  E-value: 1.07e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADIQsfPTFAQVEYNNI-------FYYQCDITSLDEIKNLKKAIERDHGNIN 112
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDIN--EKGAEETANNVrkaggkvHYYKCDVSKREEVYEAAKKIKKEVGDVT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  113 IIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGF 192
Cdd:cd05339  79 ILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGF 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  193 HKCMSRHFRSlsteCNKTGIKTLLVCPGKIKTNMFIDVPTPSKLLAPDIIPSQLALAIISAMEHNhLQTLNAPYYVNLVP 272
Cdd:cd05339 159 HESLRLELKA----YGKPGIKTTLVCPYFINTGMFQGVKTPRPLLAPILEPEYVAEKIVRAILTN-QQMLYLPFYAYFLP 233

                       250
                ....*....|
gi 6320089  273 FFKTLsWPYR 282
Cdd:cd05339 234 ILKRT-LPTP 242
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
37-284 1.32e-42

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 146.94  E-value: 1.32e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVAD-----IQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:COG0300   4 TGKTVLITGASSGIGRALARALAARGARVVLVArdaerLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:COG0300  84 DVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  192 FhkcmsrhFRSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTPSKllAPDIIPSQLALAIISAMEHNHLqtlnapyYVNLV 271
Cdd:COG0300 164 F-------SESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAG--RPLLSPEEVARAILRALERGRA-------EVYVG 227

                       250
                ....*....|...
gi 6320089  272 PFFKTLSWPYRHL 284
Cdd:COG0300 228 WDARLLARLLRLL 240
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 40-231 3.17e-40

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 138.90  E-value: 3.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089     40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFP---TFAQVEYNN--IFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKleaVAKELGALGgkALFIQGDVTDRAQVKALVEQAVERLGRLDIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFhk 194
Cdd:pfam00106  82 VNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGF-- 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 6320089    195 cmsrhFRSLSTECNKTGIKTLLVCPGKIKTNMFIDVP 231
Cdd:pfam00106 160 -----TRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 40-226 3.52e-30

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 114.17  E-value: 3.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVAD------IQSfpTFAQVEYNNI--FYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK05565   7 VAIVTGASGGIGRAIAELLAKEGAKVVIAYdineeaAQE--LLEEIKEEGGdaIAVKADVSSEEDVENLVEQIVEKFGKI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGeLTPARLTS-YGASKGAMI 190
Cdd:PRK05565  85 DILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWG-LIGASCEVlYSASKGAVN 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6320089   191 GFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK05565 164 AFTK-------ALAKELAPSGIRVNAVAPGAIDTEM 192
 
Name Accession Description Interval E-value
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 40-282 1.07e-88

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: 264.87  E-value: 1.07e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADIQsfPTFAQVEYNNI-------FYYQCDITSLDEIKNLKKAIERDHGNIN 112
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDIN--EKGAEETANNVrkaggkvHYYKCDVSKREEVYEAAKKIKKEVGDVT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  113 IIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGF 192
Cdd:cd05339  79 ILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGF 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  193 HKCMSRHFRSlsteCNKTGIKTLLVCPGKIKTNMFIDVPTPSKLLAPDIIPSQLALAIISAMEHNhLQTLNAPYYVNLVP 272
Cdd:cd05339 159 HESLRLELKA----YGKPGIKTTLVCPYFINTGMFQGVKTPRPLLAPILEPEYVAEKIVRAILTN-QQMLYLPFYAYFLP 233

                       250
                ....*....|
gi 6320089  273 FFKTLsWPYR 282
Cdd:cd05339 234 ILKRT-LPTP 242
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
37-284 1.32e-42

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 146.94  E-value: 1.32e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVAD-----IQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:COG0300   4 TGKTVLITGASSGIGRALARALAARGARVVLVArdaerLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:COG0300  84 DVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  192 FhkcmsrhFRSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTPSKllAPDIIPSQLALAIISAMEHNHLqtlnapyYVNLV 271
Cdd:COG0300 164 F-------SESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAG--RPLLSPEEVARAILRALERGRA-------EVYVG 227

                       250
                ....*....|...
gi 6320089  272 PFFKTLSWPYRHL 284
Cdd:COG0300 228 WDARLLARLLRLL 240
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 40-231 3.17e-40

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 138.90  E-value: 3.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089     40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFP---TFAQVEYNN--IFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKleaVAKELGALGgkALFIQGDVTDRAQVKALVEQAVERLGRLDIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFhk 194
Cdd:pfam00106  82 VNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGF-- 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 6320089    195 cmsrhFRSLSTECNKTGIKTLLVCPGKIKTNMFIDVP 231
Cdd:pfam00106 160 -----TRSLALELAPHGIRVNAVAPGGVDTDMTKELR 191
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 41-238 6.10e-38

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: 134.33  E-value: 6.10e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFP----TFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEAlaelAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  117 NAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHkcm 196
Cdd:cd05233  81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLT--- 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6320089  197 srhfRSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTPSKLLA 238
Cdd:cd05233 158 ----RSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKE 195
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 37-238 4.98e-35

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: 127.21  E-value: 4.98e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADI-----QSfpTFAQVEYN--NIFYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:COG1028   5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRdaealEA--AAAELRAAggRALAVAADVTDEAAVEALVAAAVAAFG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  110 NINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAM 189
Cdd:COG1028  83 RLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAV 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 6320089  190 IGFhkcmsrhFRSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTPSKLLA 238
Cdd:COG1028 163 VGL-------TRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVRE 204
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 40-226 9.01e-35

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: 126.12  E-value: 9.01e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYN-----NIFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:cd05333   2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIkalggNAAALEADVSDREAVEALVEKVEAEFGPVDIL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHK 194
Cdd:cd05333  82 VNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFTK 161

                       170       180       190
                ....*....|....*....|....*....|..
gi 6320089  195 cmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd05333 162 -------SLAKELASRGITVNAVAPGFIDTDM 186
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 36-233 1.57e-34

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: 125.68  E-value: 1.57e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   36 SKNATALITGGSSGLGFELAKELSRRINKVIVADI--QSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:COG4221   3 DKGKVALITGASSGIGAATARALAAAGARVVLAARraERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFH 193
Cdd:COG4221  83 LVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLS 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 6320089  194 KCMSRhfrslstECNKTGIKTLLVCPGKIKTNMFIDVPTP 233
Cdd:COG4221 163 ESLRA-------ELRPTGIRVTVIEPGAVDTEFLDSVFDG 195
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 40-226 3.52e-30

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 114.17  E-value: 3.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVAD------IQSfpTFAQVEYNNI--FYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK05565   7 VAIVTGASGGIGRAIAELLAKEGAKVVIAYdineeaAQE--LLEEIKEEGGdaIAVKADVSSEEDVENLVEQIVEKFGKI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGeLTPARLTS-YGASKGAMI 190
Cdd:PRK05565  85 DILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWG-LIGASCEVlYSASKGAVN 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6320089   191 GFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK05565 164 AFTK-------ALAKELAPSGIRVNAVAPGAIDTEM 192
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 37-226 1.45e-29

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


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 112.84  E-value: 1.45e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADI-QSFPTFAQVEYN----NIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:cd05347   4 KGKVALVTGASRGIGFGIASGLAEAGANIVINSRnEEKAEEAQQLIEkegvEATAFTCDVSDEEAIKAAVEAIEEDFGKI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:cd05347  84 DILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVAG 163

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6320089  192 FHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd05347 164 LTK-------ALATEWARHGIQVNAIAPGYFATEM 191
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 39-256 1.55e-28

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: 109.65  E-value: 1.55e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   39 ATALITGGSSGLGFELAKELSRRINKVIVAD---------IQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELVKEGANVIIVArseskleeaVEEIEAEANASGQKVSYISADLSDYEEVEQAFAQAVEKGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  110 NINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAM 189
Cdd:cd08939  82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFAL 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320089  190 IGFhkcmsrhFRSLSTECNKTGIKTLLVCPGKIKTNMF----IDVPTPSKLL---APDIIPSQLALAIISAMEH 256
Cdd:cd08939 162 RGL-------AESLRQELKPYNIRVSVVYPPDTDTPGFeeenKTKPEETKAIegsSGPITPEEAARIIVKGLDR 228
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 37-231 1.10e-27

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 107.59  E-value: 1.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQ-VEY-----NNIFYYQCDITSLDEIKNLKKAIERDHGN 110
Cdd:PRK05557   4 EGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEAlVAEigalgGKALAVQGDVSDAESVERAVDEAKAEFGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   111 INIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:PRK05557  84 VDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGVI 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6320089   191 GFHKCMSRHFRSlstecnkTGIKTLLVCPGKIKTNMFIDVP 231
Cdd:PRK05557 164 GFTKSLARELAS-------RGITVNAVAPGFIETDMTDALP 197
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 40-234 1.53e-27

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: 107.32  E-value: 1.53e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVI-----VADIQSfptfAQVEYN-NIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGYRVIatarnPDKLES----LGELLNdNLEVLELDVTDEESIKAAVKEVIERFGRIDV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFH 193
Cdd:cd05374  78 LVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALS 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6320089  194 KCMSRHFRSLstecnktGIKTLLVCPGKIKTNMFIDVPTPS 234
Cdd:cd05374 158 ESLRLELAPF-------GIKVTIIEPGPVRTGFADNAAGSA 191
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
37-243 2.44e-27

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 106.78  E-value: 2.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSfptfAQVE----------YNNIFYyQCDITSLDEIKNLKKAIER 106
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNE----EAAEalaaelraagGEARVL-VFDVSDEAAVRALIEAAVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   107 DHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASK 186
Cdd:PRK05653  79 AFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAK 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6320089   187 GAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTPSKLLAPDIIP 243
Cdd:PRK05653 159 AGVIGFTK-------ALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIP 208
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 41-255 7.05e-27

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 105.46  E-value: 7.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTF-----AQVEYNNIFYYQCDITSLDEIKNL-KKAIErDHGNINII 114
Cdd:cd05323   3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAaaelqAINPKVKATFVQCDVTSWEQLAAAfKKAIE-KFGRVDIL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  115 INNAGVA--HIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDN---REGFIINIASVLGeLTPARLTS-YGASKGA 188
Cdd:cd05323  82 INNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNkggKGGVIVNIGSVAG-LYPAPQFPvYSASKHG 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  189 MIGFhkcmSRHFRSLSTEcnKTGIKTLLVCPGKIKTNMFIDVPT-PSKLLAPDII--PSQLALAIISAME 255
Cdd:cd05323 161 VVGF----TRSLADLLEY--KTGVRVNAICPGFTNTPLLPDLVAkEAEMLPSAPTqsPEVVAKAIVYLIE 224
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 37-246 2.83e-24

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: 98.90  E-value: 2.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEY-NNIFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLgDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  116 NNAGVA------HIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDM------IDNREGFIINIASVLGELTPARLTSYG 183
Cdd:cd05371  81 NCAGIAvaaktyNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMgknepdQGGERGVIINTASVAAFEGQIGQAAYS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320089  184 ASKGAMIGFHKCMSRHFRSLstecnktGIKTLLVCPGKIKTNMFIDVPTPSK-LLAPDII-PSQL 246
Cdd:cd05371 161 ASKGGIVGMTLPIARDLAPQ-------GIRVVTIAPGLFDTPLLAGLPEKVRdFLAKQVPfPSRL 218
FabG-like PRK07231
SDR family oxidoreductase;
40-233 5.36e-24

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 97.98  E-value: 5.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQS---FPTFAQVEYN-NIFYYQCDITSLDEIKNL-KKAIERdHGNINII 114
Cdd:PRK07231   7 VAIVTGASSGIGEGIARRFAAEGARVVVTDRNEeaaERVAAEILAGgRAIAVAADVSDEADVEAAvAAALER-FGSVDIL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   115 INNAGVAHI-KKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFH 193
Cdd:PRK07231  86 VNNAGTTHRnGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLT 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 6320089   194 KcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM---FIDVPTP 233
Cdd:PRK07231 166 K-------ALAAELGPDKIRVNAVAPVVVETGLleaFMGEPTP 201
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 37-231 2.49e-23

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: 95.91  E-value: 2.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQS---FPTFAQVEYNNIFYYQcDITSLDEIKNLKKAIERDHGNINI 113
Cdd:cd05341   4 KGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDeegQAAAAELGDAARFFHL-DVTDEDGWTAVVDTAREAFGRLDV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFH 193
Cdd:cd05341  83 LVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGLT 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 6320089  194 KcmsrhfrSLSTECNKT--GIKTLLVCPGKIKTNMFIDVP 231
Cdd:cd05341 163 K-------SAALECATQgyGIRVNSVHPGYIYTPMTDELL 195
PRK12826 PRK12826
SDR family oxidoreductase;
40-226 2.89e-23

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 96.14  E-value: 2.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVE-----YNNIFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:PRK12826   8 VALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAElveaaGGKARARQVDVRDRAALKAAVAAGVEDFGRLDIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPAR-LTSYGASKGAMIGFh 193
Cdd:PRK12826  88 VANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVGYPgLAHYAASKAGLVGF- 166

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6320089   194 kcmsrhFRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK12826 167 ------TRALALELAARNITVNSVHPGGVDTPM 193
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 40-226 4.50e-23

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 95.32  E-value: 4.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIV------ADIQSfpTFAQVEYN--NIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK12825   8 VALVTGAARGLGRAIALRLARAGADVVVhyrsdeEAAEE--LVEAVEALgrRAQAVQADVTDKAALEAAVAAAVERFGRI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGEL-TPARlTSYGASKGAMI 190
Cdd:PRK12825  86 DILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPgWPGR-SNYAAAKAGLV 164

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6320089   191 GFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK12825 165 GLTK-------ALARELAEYGITVNMVAPGDIDTDM 193
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
40-226 9.42e-23

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 94.45  E-value: 9.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADiqsFPTF-AQVEYNNIFYYQ--------CDITSLDEIKNLKKAIERDHGN 110
Cdd:PRK12824   4 IALVTGAKRGIGSAIARELLNDGYRVIATY---FSGNdCAKDWFEEYGFTedqvrlkeLDVTDTEECAEALAEIEEEEGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   111 INIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:PRK12824  81 VDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGMI 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6320089   191 GFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK12824 161 GFTK-------ALASEGARYGITVNCIAPGYIATPM 189
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-233 1.53e-22

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 94.08  E-value: 1.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:PRK06463   6 KGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGVFTIKCDVGNRDQVKKSKEVVEKEFGRVDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   117 NAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTS-YGASKGAMIGFHkc 195
Cdd:PRK06463  86 NAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEGTTfYAITKAGIIILT-- 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6320089   196 msrhfRSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTP 233
Cdd:PRK06463 164 -----RRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQ 196
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 37-224 1.57e-22

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 94.36  E-value: 1.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADI-QSFPTFAQVEYN----NIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK07097   9 KGKIALITGASYGIGFAIAKAYAKAGATIVFNDInQELVDKGLAAYRelgiEAHGYVCDVTDEDGVQAMVSQIEKEVGVI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:PRK07097  89 DILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGGLKM 168

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6320089   192 FHKCMSRHFRSLSTECNKTGiktllvcPGKIKT 224
Cdd:PRK07097 169 LTKNIASEYGEANIQCNGIG-------PGYIAT 194
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 37-226 2.93e-22

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 93.16  E-value: 2.93e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEY----NNI--FYYQCDITSLDEIKNLKKAIERDHGN 110
Cdd:cd05352   7 KGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEElakkYGVktKAYKCDVSSQESVEKTFKQIQKDFGK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  111 INIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELT--PARLTSYGASKGA 188
Cdd:cd05352  87 IDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVnrPQPQAAYNASKAA 166

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6320089  189 MIgfHKCmsrhfRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd05352 167 VI--HLA-----KSLAVEWAKYFIRVNSISPGYIDTDL 197
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 37-257 3.45e-22

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: 93.03  E-value: 3.45e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIV-----ADIQSFPT-FAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGN 110
Cdd:cd05332   2 QGKVVIITGASSGIGEELAYHLARLGARLVLsarreERLEEVKSeCLELGAPSPHVVPLDMSDLEDAEQVVEEALKLFGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  111 INIIINNAGVaHIKKLEHMTNKEV-EQLIDINLIGaYRIISTFAED-MIDNREGFIINIASVLGELTPARLTSYGASKGA 188
Cdd:cd05332  82 LDILINNAGI-SMRSLFHDTSIDVdRKIMEVNYFG-PVALTKAALPhLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320089  189 MIGFhkcmsrhFRSLSTECNKTGIKTLLVCPGKIKTNMFIDVPT--------PSKLLAPDIIPSQLALAIISAMEHN 257
Cdd:cd05332 160 LQGF-------FDSLRAELSEPNISVTVVCPGLIDTNIAMNALSgdgsmsakMDDTTANGMSPEECALEILKAIALR 229
PRK06172 PRK06172
SDR family oxidoreductase;
41-227 4.59e-22

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 92.89  E-value: 4.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEY-----NNIFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:PRK06172  10 ALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALireagGEALFVACDVTRDAEVKALVEQTIAAYGRLDYAF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   116 NNAGVAHIK-KLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHK 194
Cdd:PRK06172  90 NNAGIEIEQgRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHAVIGLTK 169

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6320089   195 cmsrhfrSLSTECNKTGIKTLLVCPGKIKTNMF 227
Cdd:PRK06172 170 -------SAAIEYAKKGIRVNAVCPAVIDTDMF 195
PRK05650 PRK05650
SDR family oxidoreductase;
42-226 4.76e-21

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 90.48  E-value: 4.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    42 LITGGSSGLGFELAKELSRRINKVIVADIQSfPTFAQVEY------NNIFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNE-EGGEETLKllreagGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKc 195
Cdd:PRK05650  83 NNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSE- 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 6320089   196 msrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK05650 162 ------TLLVELADDEIGVHVVCPSFFQTNL 186
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 41-231 4.95e-21

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 90.06  E-value: 4.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVaDIQSFPTFAQVEYNNI-------FYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:PRK12935   9 AIVTGGAKGIGKAITVALAQEGAKVVI-NYNSSKEAAENLVNELgkeghdvYAVQADVSKVEDANRLVEEAVNHFGKVDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFH 193
Cdd:PRK12935  88 LVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGMLGFT 167

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6320089   194 KcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNMFIDVP 231
Cdd:PRK12935 168 K-------SLALELAKTNVTVNAICPGFIDTEMVAEVP 198
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 35-257 7.13e-21

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: 89.45  E-value: 7.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   35 LSKNaTALITGGSSGLGFELAKELSRRINKVIV-----ADIQSfptfAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:COG3967   3 LTGN-TILITGGTSGIGLALAKRLHARGNTVIItgrreEKLEE----AAAANPGLHTIVLDVADPASIAALAEQVTAEFP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  110 NINIIINNAGVAHIKKL--EHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGeLTPARLT-SYGASK 186
Cdd:COG3967  78 DLNVLINNAGIMRAEDLldEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLA-FVPLAVTpTYSATK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320089  187 GAMigfhkcmsrHF--RSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTPSKLLAPDiipsQLALAIISAMEHN 257
Cdd:COG3967 157 AAL---------HSytQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDPRAMPLD----EFADEVMAGLETG 216
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-248 1.42e-20

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 88.21  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRR-INKVIVADIQSFPTFAQVEYNN----IFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK07666   6 QGKNALITGAGRGIGRAVAIALAKEgVNVGLLARTEENLKAVAEEVEAygvkVVIATADVSDYEEVTAAIEQLKNELGSI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:PRK07666  86 DILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFGVLG 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320089   192 FHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNMFIDVP----TPSKLLAP----DIIPSQLAL 248
Cdd:PRK07666 166 LTE-------SLMQEVRKHNIRVTALTPSTVATDMAVDLGltdgNPDKVMQPedlaEFIVAQLKL 223
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 37-220 3.12e-20

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 88.14  E-value: 3.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSfptfAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:PRK06171   8 QGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHG----GDGQHENYQFVPTDVSSAEEVNHTVAEIIEKFGRIDGLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   117 NAGVaHIKKL---------EHMTNKEV-EQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASK 186
Cdd:PRK06171  84 NAGI-NIPRLlvdekdpagKYELNEAAfDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQSCYAATK 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6320089   187 GAMIGFHkcmsrhfRSLSTECNKTGIKTLLVCPG 220
Cdd:PRK06171 163 AALNSFT-------RSWAKELGKHNIRVVGVAPG 189
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 37-227 4.81e-20

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: 86.59  E-value: 4.81e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIV-----ADIQSfptfAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:cd05370   4 TGNTVLITGGTSGIGLALARKFLEAGNTVIItgrreERLAE----AKKELPNIHTIVLDVGDAESVEALAEALLSEYPNL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  112 NIIINNAGvahIKKLEHMTN-----KEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASK 186
Cdd:cd05370  80 DILINNAG---IQRPIDLRDpasdlDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATK 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 6320089  187 GAMigfhkcmsrHF--RSLSTECNKTGIKTLLVCPGKIKTNMF 227
Cdd:cd05370 157 AAL---------HSytLALRHQLKDTGVEVVEIVPPAVDTELH 190
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 41-226 6.83e-20

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: 86.75  E-value: 6.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVADIQsfPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINNAGV 120
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLP--FVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAGV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  121 AHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKCmsrhf 200
Cdd:cd05331  79 LRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKC----- 153

                       170       180
                ....*....|....*....|....*.
gi 6320089  201 rsLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd05331 154 --LGLELAPYGVRCNVVSPGSTDTAM 177
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 35-225 1.02e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 86.89  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    35 LSKNATALITGGSSGLGFELAKELSRRINKVIV-----ADIQSFPTFAQveyNNIFYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:PRK06180   1 MSSMKTWLITGVSSGFGRALAQAALAAGHRVVGtvrseAARADFEALHP---DRALARLLDVTDFDAIDAVVADAEATFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   110 NINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAM 189
Cdd:PRK06180  78 PIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFAL 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6320089   190 IGfhkcMSrhfRSLSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK06180 158 EG----IS---ESLAKEVAPFGIHVTAVEPGSFRTD 186
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 40-226 1.28e-19

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 85.37  E-value: 1.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKEL-----------SRRINKV--IVADIQSfptfaqvEYNNIFYYQCDITSLDEIKNLKKAIER 106
Cdd:cd05324   2 VALVTGANRGIGFEIVRQLaksgpgtviltARDVERGqaAVEKLRA-------EGLSVRFHQLDVTDDASIEAAADFVEE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  107 DHGNINIIINNAGVAHIKKLEHMTNKEV-EQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPArltsYGAS 185
Cdd:cd05324  75 KYGGLDILVNNAGIAFKGFDDSTPTREQaRETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTSA----YGVS 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6320089  186 KGAMIGFhkcmSRHfrsLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd05324 151 KAALNAL----TRI---LAKELKETGIKVNACCPGWVKTDM 184
PRK07326 PRK07326
SDR family oxidoreductase;
37-257 1.82e-19

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 85.45  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKV-IVADIQSFPTFAQVEYN---NIFYYQCDITSLDEIKNLKKAIERDHGNIN 112
Cdd:PRK07326   5 KGKVALITGGSKGIGFAIAEALLAEGYKVaITARDQKELEEAAAELNnkgNVLGLAADVRDEADVQRAVDAIVAAFGGLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   113 IIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTfAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGF 192
Cdd:PRK07326  85 VLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKA-AVPALKRGGGYIINISSLAGTNFFAGGAAYNASKFGLVGF 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320089   193 HKCMSRHFRslstecnKTGIKTLLVCPGKIKTNmFIDvPTPSKLLAPDIIPSQLALAIISAMEHN 257
Cdd:PRK07326 164 SEAAMLDLR-------QYGIKVSTIMPGSVATH-FNG-HTPSEKDAWKIQPEDIAQLVLDLLKMP 219
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 40-226 1.93e-19

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: 85.51  E-value: 1.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADIQ-------SFPTFAQVEYNNIFYyQCDITSLDEIKNL-KKAIERdHGNI 111
Cdd:cd05366   4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNleeaaksTIQEISEAGYNAVAV-GADVTDKDDVEALiDQAVEK-FGSF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMID-NREGFIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:cd05366  82 DVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKlGHGGKIINASSIAGVQGFPNLGAYSASKFAVR 161

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6320089  191 GFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd05366 162 GLTQ-------TAAQELAPKGITVNAYAPGIVKTEM 190
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 39-226 5.48e-19

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 84.72  E-value: 5.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    39 ATALITGGSSGLGFELAKELSRRINKVIVAD-----IQSFptFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:PRK12829  12 LRVLVTGGASGIGRAIAEAFAEAGARVHVCDvseaaLAAT--AARLPGAKVTATVADVADPAQVERVFDTAVERFGGLDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVA-HIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMID-NREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:PRK12829  90 LVNNAGIAgPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKAsGHGGVIIALSSVAGRLGYPGRTPYAASKWAVVG 169

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6320089   192 FhkcmsrhFRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK12829 170 L-------VKSLAIELGPLGIRVNAILPGIVRGPR 197
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 37-224 6.01e-19

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 84.17  E-value: 6.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADI-QSFPTFAQVEYNN----IFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK12429   3 KGKVALVTGAASGIGLEIALALAKEGAKVVIADLnDEAAAAAAEALQKaggkAIGVAMDVTDEEAINAGIDYAVETFGGV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:PRK12429  83 DILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIG 162

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6320089   192 FHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK12429 163 LTK-------VVALEGATHGVTVNAICPGYVDT 188
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 41-274 7.07e-19

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: 83.92  E-value: 7.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEY-----NNIFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAEllnpnPSVEVEILDVTDEERNQLVIAELEAELGGLDLVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKc 195
Cdd:cd05350  81 INAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAE- 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  196 msrhfrSLSTECNKTGIKTLLVCPGKIKT----NMFidvPTPskllaPDIIPSQLALAIISAMEHNH------LQTLNAP 265
Cdd:cd05350 160 ------SLRYDVKKRGIRVTVINPGFIDTpltaNMF---TMP-----FLMSVEQAAKRIYKAIKKGAaeptfpWRLAVPL 225


                ....*....
gi 6320089  266 YYVNLVPFF 274
Cdd:cd05350 226 RLLKLLPER 234
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 41-230 7.71e-19

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: 84.04  E-value: 7.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVADIQSfPTFAQVEYN----NIFYYQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:cd05326   7 AIITGGASGIGEATARLFAKHGARVVIADIDD-DAGQAVAAElgdpDISFVHCDVTVEADVRAAVDTAVARFGRLDIMFN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  117 NAGV--AHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHk 194
Cdd:cd05326  86 NAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKHAVLGLT- 164

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6320089  195 cmsrhfRSLSTECNKTGIKTLLVCPGKIKTNMFIDV 230
Cdd:cd05326 165 ------RSAATELGEHGIRVNCVSPYGVATPLLTAG 194
PRK06484 PRK06484
short chain dehydrogenase; Validated
 41-236 1.10e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 86.06  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSfptfAQVEYN------NIFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:PRK06484   8 VLVTGAAGGIGRAACQRFARAGDQVVVADRNV----ERARERadslgpDHHALAMDVSDEAQIREGFEQLHREFGRIDVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   115 INNAGVA--HIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGF-IINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:PRK06484  84 VNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAAVIS 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 6320089   192 FHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTPSKL 236
Cdd:PRK06484 164 LT-------RSLACEWAAKGIRVNAVLPGYVRTQMVAELERAGKL 201
PRK06398 PRK06398
aldose dehydrogenase; Validated
 37-228 1.20e-18

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 83.34  E-value: 1.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSfPTFAQVEYnnifyYQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:PRK06398   5 KDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKE-PSYNDVDY-----FKVDVSNKEQVIKGIDYVISKYGRIDILVN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   117 NAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKCM 196
Cdd:PRK06398  79 NAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVLGLTRSI 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 6320089   197 SRHFRSLstecnktgIKTLLVCPGKIKTNMFI 228
Cdd:PRK06398 159 AVDYAPT--------IRCVAVCPGSIRTPLLE 182
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 37-224 1.53e-18

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: 83.27  E-value: 1.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIV------ADIQSFPTFAQVEYN-NIFYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLngfgdaAEIEAVRAGLAAKHGvKVLYHGADLSKPAAIEDMVAYAQRQFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  110 NINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAM 189
Cdd:cd08940  81 GVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGV 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6320089  190 IGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:cd08940 161 VGLTK-------VVALETAGTGVTCNAICPGWVLT 188
PRK07454 PRK07454
SDR family oxidoreductase;
35-242 1.53e-18

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 82.70  E-value: 1.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    35 LSKNATALITGGSSGLGFELAKELSRR-INKVIVA----DIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:PRK07454   3 LNSMPRALITGASSGIGKATALAFAKAgWDLALVArsqdALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   110 NINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAM 189
Cdd:PRK07454  83 CPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAAL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6320089   190 IGFHKCMSRHFRSlstecnkTGIKTLLVCPGKIKTNMFiDVPT------PSKLLAPDII 242
Cdd:PRK07454 163 AAFTKCLAEEERS-------HGIRVCTITLGAVNTPLW-DTETvqadfdRSAMLSPEQV 213
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 37-233 2.69e-18

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: 82.32  E-value: 2.69e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIV--------ADiqsfPTFAQVEYNNI--FYYQCDITSLDEIKNLKKAIER 106
Cdd:cd05362   2 AGKVALVTGASRGIGRAIAKRLARDGASVVVnyasskaaAE----EVVAEIEAAGGkaIAVQADVSDPSQVARLFDAAEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  107 DHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNreGFIINIASVLGELTPARLTSYGASK 186
Cdd:cd05362  78 AFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG--GRIINISSSLTAAYTPNYGAYAGSK 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 6320089  187 GAMIGFHKCMSRhfrslstECNKTGIKTLLVCPGKIKTNMFIDVPTP 233
Cdd:cd05362 156 AAVEAFTRVLAK-------ELGGRGITVNAVAPGPVDTDMFYAGKTE 195
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 41-239 3.08e-18

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 82.07  E-value: 3.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYNN---------IFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK12827   9 VLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAagieaaggkALGLAFDVRDFAATRAALDAGVEEFGRL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMI-DNREGFIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:PRK12827  89 DILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIrARRGGRIVNIASVAGVRGNRGQVNYAASKAGLI 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 6320089   191 GFHKCMSRHFRSLstecnktGIKTLLVCPGKIKTNMFIDVPTPSKLLAP 239
Cdd:PRK12827 169 GLTKTLANELAPR-------GITVNAVAPGAINTPMADNAAPTEHLLNP 210
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 40-255 4.73e-18

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: 81.26  E-value: 4.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKV-IVADIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINNA 118
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDGYRVsLGLRNPEDLAALSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHNA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  119 GVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHkcmsr 198
Cdd:cd08932  82 GIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALA----- 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6320089  199 hfRSLSTECNKTGIKTLLVCPGKIKTNMFiDVPTPSKLLAPDII--PSQLALAIISAME 255
Cdd:cd08932 157 --HALRQEGWDHGVRVSAVCPGFVDTPMA-QGLTLVGAFPPEEMiqPKDIANLVRMVIE 212
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
40-226 1.42e-17

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 80.61  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQsfPTFAQVEYN------NIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:PRK08226   8 TALITGALQGIGEGIARVFARHGANLILLDIS--PEIEKLADElcgrghRCTAVVADVRDPASVAAAIKRAKEKEGRIDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTP-ARLTSYGASKGAMIGF 192
Cdd:PRK08226  86 LVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMVAdPGETAYALTKAAIVGL 165

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6320089   193 HKCMSRHFRslstecnKTGIKTLLVCPGKIKTNM 226
Cdd:PRK08226 166 TKSLAVEYA-------QSGIRVNAICPGYVRTPM 192
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 41-237 8.59e-17

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: 78.16  E-value: 8.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIV----ADIQSFPTFAQVEYN--NIFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVInyrkSKDAAAEVAAEIEELggKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFhk 194
Cdd:cd05359  81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEAL-- 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 6320089  195 cmsrhFRSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTPSKLL 237
Cdd:cd05359 159 -----VRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLL 196
PRK07201 PRK07201
SDR family oxidoreductase;
42-256 1.22e-16

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 80.00  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    42 LITGGSSGLGFELAKELSRRINKV-IVA----DIQSfpTFAQVEYN--NIFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:PRK07201 375 LITGASSGIGRATAIKVAEAGATVfLVArngeALDE--LVAEIRAKggTAHAYTCDLTDSAAVDHTVKDILAEHGHVDYL 452

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   115 INNAGVAHIKKLEHMTNK--EVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVlGELTPA-RLTSYGASKGAMIG 191
Cdd:PRK07201 453 VNNAGRSIRRSVENSTDRfhDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSI-GVQTNApRFSAYVASKAALDA 531

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320089   192 FHKCMSRHFrsLSTECNKTGIKTLLVcpgkiKTNMFidvpTPSKLL--APDIIPSQLALAIISAMEH 256
Cdd:PRK07201 532 FSDVAASET--LSDGITFTTIHMPLV-----RTPMI----APTKRYnnVPTISPEEAADMVVRAIVE 587
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 41-233 2.10e-16

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: 76.84  E-value: 2.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFA-----QVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAvaaaiQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  116 NNAGVAHIKKLE-HMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAmigfhk 194
Cdd:cd05365  82 NNAGGGGPKPFDmPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAA------ 155

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6320089  195 cMSRHFRSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTP 233
Cdd:cd05365 156 -VNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLTP 193
PRK09072 PRK09072
SDR family oxidoreductase;
37-226 2.32e-16

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 77.29  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVA--DIQSFPTFAQvEYNNIFYYQC---DITSLDEIKNLKKAIERdHGNI 111
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLVgrNAEKLEALAA-RLPYPGRHRWvvaDLTSEAGREAVLARARE-MGGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:PRK09072  82 NVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRG 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6320089   192 FHKCMSRhfrslstECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK09072 162 FSEALRR-------ELADTGVRVLYLAPRATRTAM 189
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 41-255 2.38e-16

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 76.39  E-value: 2.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKV-IVA-DIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINNA 118
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVgICArDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  119 GVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKcmsr 198
Cdd:cd08929  83 GVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSE---- 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6320089  199 hfrSLSTECNKTGIKTLLVCPGKIKTNmFIDVPTP-SKLLAPDIIpsqlALAIISAME 255
Cdd:cd08929 159 ---AAMLDLREANIRVVNVMPGSVDTG-FAGSPEGqAWKLAPEDV----AQAVLFALE 208
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 41-234 2.58e-16

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: 76.49  E-value: 2.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRR-INKVIVAD--------IQSFPTFAQVEYNnifYYQCDITSLDEI-KNLKKAIE-RDHG 109
Cdd:cd05356   4 AVVTGATDGIGKAYAEELAKRgFNVILISRtqekldavAKEIEEKYGVETK---TIAADFSAGDDIyERIEKELEgLDIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  110 NINIIinnAGVAH--IKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKG 187
Cdd:cd05356  81 ILVNN---VGISHsiPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKA 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 6320089  188 AMIGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKTNM------FIDVPTPS 234
Cdd:cd05356 158 FLDFFS-------RALYEEYKSQGIDVQSLLPYLVATKMskirksSLFVPSPE 203
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 37-254 2.81e-16

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: 76.78  E-value: 2.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKEL----------SRRINKV--IVADIQSfptfaqVEYNNIFYYQCDITSLDEIKNLKKAI 104
Cdd:cd05343   5 RGRVALVTGASVGIGAAVARALvqhgmkvvgcARRVDKIeaLAAECQS------AGYPTLFPYQCDLSNEEQILSMFSAI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  105 ERDHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIgAYRIISTFA-EDMIDNR--EGFIINIASVLGE-LTPARLT 180
Cdd:cd05343  79 RTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVL-ALSICTREAyQSMKERNvdDGHIININSMSGHrVPPVSVF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  181 S-YGASKGAMIGFHKCMSRHFRSLstecnKTGIKTLLVCPGKIKTN----MFIDVPTPSKLL---APDIIPSQLALAIIS 252
Cdd:cd05343 158 HfYAATKHAVTALTEGLRQELREA-----KTHIRATSISPGLVETEfafkLHDNDPEKAAATyesIPCLKPEDVANAVLY 232


                ..
gi 6320089  253 AM 254
Cdd:cd05343 233 VL 234
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 37-227 3.07e-16

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 76.61  E-value: 3.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQS-----FPTFAQVEYN--NIFYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSekaanVAQEINAEYGegMAYGFGADATSEQSVLALSRGVDEIFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   110 NINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMI-DNREGFIINIASVLGELTPARLTSYGASKGA 188
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIrDGIQGRIIQINSKSGKVGSKHNSGYSAAKFG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6320089   189 MIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGK-IKTNMF 227
Cdd:PRK12384 161 GVGLTQ-------SLALDLAEYGITVHSLMLGNlLKSPMF 193
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 37-251 5.16e-16

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: 76.34  E-value: 5.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADIqsfpTFAQV-----EYNN----IFYYQCDITSLDEIKNLKKAIERD 107
Cdd:cd08935   4 KNKVAVITGGTGVLGGAMARALAQAGAKVAALGR----NQEKGdkvakEITAlggrAIALAADVLDRASLERAREEIVAQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  108 HGNINIIINNAGVAH--------------IKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGE 173
Cdd:cd08935  80 FGTVDILINGAGGNHpdattdpehyepetEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAF 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320089  174 LTPARLTSYGASKGAMIGFHKCMSRHFrslstecNKTGIKTLLVCPGKIKTNMFIDVptpskLLAPDIIPSQLALAII 251
Cdd:cd08935 160 SPLTKVPAYSAAKAAVSNFTQWLAVEF-------ATTGVRVNAIAPGFFVTPQNRKL-----LINPDGSYTDRSNKIL 225
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 40-196 5.99e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 75.85  E-value: 5.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQsfPTFAQV----EYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:PRK06841  17 VAVVTGGASGIGHAIAELFAAKGARVALLDRS--EDVAEVaaqlLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKC 195
Cdd:PRK06841  95 NSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGVVGMTKV 174


                 .
gi 6320089   196 M 196
Cdd:PRK06841 175 L 175
PRK07775 PRK07775
SDR family oxidoreductase;
40-231 6.01e-16

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 76.33  E-value: 6.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELS----------RRINKV--IVADIQSfptfaqvEYNNIFYYQCDITSLDEIKNLKKAIERD 107
Cdd:PRK07775  12 PALVAGASSGIGAATAIELAaagfpvalgaRRVEKCeeLVDKIRA-------DGGEAVAFPLDVTDPDSVKSFVAQAEEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   108 HGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKG 187
Cdd:PRK07775  85 LGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKA 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 6320089   188 AMIGfhkcMSRHFRslsTECNKTGIKTLLVCPGKIKTNMFIDVP 231
Cdd:PRK07775 165 GLEA----MVTNLQ---MELEGTGVRASIVHPGPTLTGMGWSLP 201
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 40-226 6.71e-16

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: 75.58  E-value: 6.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERdhgnINIIINNAG 119
Cdd:cd05368   4 VALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEEGR----IDVLFNCAG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  120 VAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGEL--TPARlTSYGASKGAMIGFHKcms 197
Cdd:cd05368  80 FVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIkgVPNR-FVYSTTKAAVIGLTK--- 155

                       170       180
                ....*....|....*....|....*....
gi 6320089  198 rhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd05368 156 ----SVAADFAQQGIRCNAICPGTVDTPS 180
PRK05866 PRK05866
SDR family oxidoreductase;
42-256 7.12e-16

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 76.32  E-value: 7.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    42 LITGGSSGLGFELAKELSRRINKVIV--------ADIQSFPTFAQVEYNNIfyyQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:PRK05866  44 LLTGASSGIGEAAAEQFARRGATVVAvarredllDAVADRITRAGGDAMAV---PCDLSDLDAVDALVADVEKRIGGVDI 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKKLEHMTNK--EVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIAS--VLGELTPaRLTSYGASKGAM 189
Cdd:PRK05866 121 LINNAGRSIRRPLAESLDRwhDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATwgVLSEASP-LFSVYNASKAAL 199

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320089   190 IGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKTNMFidVPTPSKLLAPDIIPSQLALAIISAMEH 256
Cdd:PRK05866 200 SAVS-------RVIETEWGDRGVHSTTLYYPLVATPMI--APTKAYDGLPALTADEAAEWMVTAART 257
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-226 9.91e-16

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 75.00  E-value: 9.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAqveyNNIFYYQCDITS-LDEIKNLKKAIErdhgninIII 115
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLS----GNFHFLQLDLSDdLEPLFDWVPSVD-------ILC 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   116 NNAGVAH-IKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHK 194
Cdd:PRK06550  73 NTAGILDdYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGFTK 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 6320089   195 cmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK06550 153 -------QLALDYAKDGIQVFGIAPGAVKTPM 177
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 41-226 1.00e-15

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: 75.02  E-value: 1.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVADIQSfPTFAQ------VEYNNIFYYQCDITslDEIKNLKKAIERDHGNIN-- 112
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCRD-PSAATelaalgASHSRLHILELDVT--DEIAESAEAVAERLGDAGld 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  113 IIINNAGVAHI-KKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLG---ELTPARLTSYGASKGA 188
Cdd:cd05325  78 VLINNAGILHSyGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsigDNTSGGWYSYRASKAA 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6320089  189 MigfhkCMSrhFRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd05325 158 L-----NML--TKSLAVELKRDGITVVSLHPGWVRTDM 188
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 41-226 1.13e-15

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 74.95  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRinKVIVA----DIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:PRK12936   9 ALVTGASGGIGEEIARLLHAQ--GAIVGlhgtRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEGVDILVN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   117 NAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKcm 196
Cdd:PRK12936  87 NAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFSK-- 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 6320089   197 srhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK12936 165 -----SLAQEIATRNVTVNCVAPGFIESAM 189
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
37-225 1.48e-15

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 74.77  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVadiqsfPTF----------AQVEYNNIFYYQCDITSLDEIKNLKKAIER 106
Cdd:PRK06935  14 DGKVAIVTGGNTGLGQGYAVALAKAGADIII------TTHgtnwdetrrlIEKEGRKVTFVQVDLTKPESAEKVVKEALE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   107 DHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVL----GELTPArltsY 182
Cdd:PRK06935  88 EFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLsfqgGKFVPA----Y 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 6320089   183 GASKGAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK06935 164 TASKHGVAGLTK-------AFANELAAYNIQVNAIAPGYIKTA 199
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 40-233 1.61e-15

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 74.62  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEY-----NNIFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:PRK12939   9 RALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAAleaagGRAHAIAADLADPASVQRFFDAAAAALGGLDGL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHK 194
Cdd:PRK12939  89 VNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIGMTR 168

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6320089   195 CMSRHFRSlstecnkTGIKTLLVCPGKIKTNMFIDVPTP 233
Cdd:PRK12939 169 SLARELGG-------RGITVNAIAPGLTATEATAYVPAD 200
PRK06484 PRK06484
short chain dehydrogenase; Validated
 40-224 1.86e-15

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 76.43  E-value: 1.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEY--NNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINN 117
Cdd:PRK06484 271 VVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEAlgDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVNN 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   118 AGVAHI-KKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMidNREGFIINIASVLGELTPARLTSYGASKGAMigfhKCM 196
Cdd:PRK06484 351 AGIAEVfKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAV----TML 424

                        170       180
                 ....*....|....*....|....*...
gi 6320089   197 SrhfRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK06484 425 S---RSLACEWAPAGIRVNTVAPGYIET 449
PRK07074 PRK07074
SDR family oxidoreductase;
37-224 2.11e-15

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 74.42  E-value: 2.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFP---TFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAAlaaFADALGDARFVPVACDLTDAASLAAALANAAAERGPVDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKKLeHMTNKEVEQL-IDINLIGAYRIISTFAEDMIDNREGFIINIASV-----LGEltPArltsYGASKG 187
Cdd:PRK07074  81 LVANAGAARAASL-HDTTPASWRAdNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVngmaaLGH--PA----YSAAKA 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6320089   188 AMIGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK07074 154 GLIHYT-------KLLAVEYGRFGIRANAVAPGTVKT 183
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 40-247 2.33e-15

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: 73.86  E-value: 2.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADI-----QSFPTFAQVEYN-NIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPSVVVLLarseePLQELKEELRPGlRVTTVKADLSDAAGVEQLLEAIRKLDGERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  114 IINNAGV-AHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNR-EGFIINIASvLGELTPARLTS-YGASKGAMI 190
Cdd:cd05367  81 LINNAGSlGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSS-GAAVNPFKGWGlYCSSKAARD 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320089  191 GFhkcmsrhFRSLSTEcnKTGIKTLLVCPGKIKTNM----------------FIDVPTPSKLLAPDIIPSQLA 247
Cdd:cd05367 160 MF-------FRVLAAE--EPDVRVLSYAPGVVDTDMqreiretsadpetrsrFRSLKEKGELLDPEQSAEKLA 223
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 37-225 2.33e-15

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: 74.29  E-value: 2.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADI------QSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGN 110
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADInapaleQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  111 INIIINNAGVAHIKKLEHMTNKEVEQL---IDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTP-------ARLT 180
Cdd:cd08930  81 IDILINNAYPSPKVWGSRFEEFPYEQWnevLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIAPdfriyenTQMY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6320089  181 S---YGASKGAMIGFHKCMSRHFRslstecnKTGIKTLLVCPGKIKTN 225
Cdd:cd08930 161 SpveYSVIKAGIIHLTKYLAKYYA-------DTGIRVNAISPGGILNN 201
PRK06181 PRK06181
SDR family oxidoreductase;
38-225 3.17e-15

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 73.86  E-value: 3.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    38 NATALITGGSSGLGFELAKELSRRINKVIVAD-----IQSFPTFAQVEYNNIFYYQCDITSLDEIKNL-KKAIERdHGNI 111
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAArnetrLASLAQELADHGGEALVVPTDVSDAEACERLiEAAVAR-FGGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEV-EQLIDINLIGAYRIIStFAEDMIDNREGFIINIASVLGeLT--PARlTSYGASKGA 188
Cdd:PRK06181  80 DILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTH-AALPHLKASRGQIVVVSSLAG-LTgvPTR-SGYAASKHA 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6320089   189 MIGFhkcmsrhFRSLSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK06181 157 LHGF-------FDSLRIELADDGVAVTVVCPGFVATD 186
PLN02253 PLN02253
xanthoxin dehydrogenase
 28-226 3.54e-15

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 74.09  E-value: 3.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    28 PSYNPSILSKnaTALITGGSSGLGFELAKELSRRINKVIVADIQS------FPTFAQVEynNIFYYQCDITSLDEIKNLK 101
Cdd:PLN02253  10 SLPSQRLLGK--VALVTGGATGIGESIVRLFHKHGAKVCIVDLQDdlgqnvCDSLGGEP--NVCFFHCDVTVEDDVSRAV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   102 KAIERDHGNINIIINNAGV--AHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFII---NIASVLGELTP 176
Cdd:PLN02253  86 DFTVDKFGTLDIMVNNAGLtgPPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVslcSVASAIGGLGP 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 6320089   177 ArltSYGASKGAMIGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PLN02253 166 H---AYTGSKHAVLGLT-------RSVAAELGKHGIRVNCVSPYAVPTAL 205
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 48-238 3.85e-15

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: 73.23  E-value: 3.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089     48 SGLGFELAKELSRRINKVIVADIQ--SFPTFAQV--EYNNIFYyQCDITSLDEIKNLKKAIERDHGNINIIINNAGVA-- 121
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNeaLAKRVEELaeELGAAVL-PCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFApk 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    122 HIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMidNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKCMSRHFR 201
Cdd:pfam13561  85 LKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELG 162

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 6320089    202 slstecnKTGIKTLLVCPGKIKTNMFIDVPTPSKLLA 238
Cdd:pfam13561 163 -------PRGIRVNAISPGPIKTLAASGIPGFDELLA 192
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 41-226 4.11e-15

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 73.84  E-value: 4.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSfPTFAQV------EYNNIFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:PRK05876   9 AVITGGASGIGLATGTEFARRGARVVLGDVDK-PGLRQAvnhlraEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNRE-GFIINIASVLGELTPARLTSYGASKGAMIGFH 193
Cdd:PRK05876  88 FSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTgGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLA 167

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6320089   194 KCMSRhfrslstECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK05876 168 ETLAR-------EVTADGIGVSVLCPMVVETNL 193
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 37-224 5.67e-15

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


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 73.19  E-value: 5.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVaDIQSFP-----TFAQVEYNNIF--YYQCDITSLDEIKNLKKAIERDHG 109
Cdd:cd05358   2 KGKVALVTGASSGIGKAIAIRLATAGANVVV-NYRSKEdaaeeVVEEIKAVGGKaiAVQADVSKEEDVVALFQSAIKEFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  110 NINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNR-EGFIINIASVLGELTPARLTSYGASKGA 188
Cdd:cd05358  81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKiKGKIINMSSVHEKIPWPGHVNYAASKGG 160

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6320089  189 MIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:cd05358 161 VKMMTK-------TLAQEYAPKGIRVNAIAPGAINT 189
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 36-256 6.31e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 73.40  E-value: 6.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    36 SKNATALITGGSSGLGFELAKELSRRINKVI--VADIQSFPTFAQVEYnnifyYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:PRK06179   2 SNSKVALVTGASSGIGRATAEKLARAGYRVFgtSRNPARAAPIPGVEL-----LELDVTDDASVQAAVDEVIARAGRIDV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGeLTPARLTS-YGASKGAMIGF 192
Cdd:PRK06179  77 LVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLG-FLPAPYMAlYAASKHAVEGY 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320089   193 HKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTP-SKLLAPDIIPSQLALAIISAMEH 256
Cdd:PRK06179 156 SE-------SLDHEVRQFGIRVSLVEPAYTKTNFDANAPEPdSPLAEYDRERAVVSKAVAKAVKK 213
PRK07832 PRK07832
SDR family oxidoreductase;
41-281 8.41e-15

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 72.77  E-value: 8.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFP---TFAQVEYNN---IFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGlaqTVADARALGgtvPEHRALDISDYDAVAAFAADIHAAHGSMDVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMID-NREGFIINIASVLGELTPARLTSYGASKGAMIGfh 193
Cdd:PRK07832  83 MNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAaGRGGHLVNVSSAAGLVALPWHAAYSASKFGLRG-- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   194 kcMSRHFRslsTECNKTGIKTLLVCPGKIKTNMF-------IDVPTPS------KLLAPDIIPSQLALAIISAMEHNHlq 260
Cdd:PRK07832 161 --LSEVLR---FDLARHGIGVSVVVPGAVKTPLVntveiagVDREDPRvqkwvdRFRGHAVTPEKAAEKILAGVEKNR-- 233

                        250       260
                 ....*....|....*....|....*...
gi 6320089   261 tlnapYYVNLVP------FFK-TLSWPY 281
Cdd:PRK07832 234 -----YLVYTSPdiralyWFKrKAWWPY 256
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 40-226 1.16e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 72.29  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELA---KELSRRInkVIVADIQSFPTFAQVEYNNI----FYYQCDITSLDEIKNLKKAIERDHGNIN 112
Cdd:PRK08213  14 TALVTGGSRGLGLQIAealGEAGARV--VLSARKAEELEEAAAHLEALgidaLWIAADVADEADIERLAEETLERFGHVD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   113 IIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFA-EDMIDNREGFIINIASV--LGELTPARLTS--YGASKG 187
Cdd:PRK08213  92 ILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAkRSMIPRGYGRIINVASVagLGGNPPEVMDTiaYNTSKG 171

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6320089   188 AMIGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK08213 172 AVINFT-------RALAAEWGPHGIRVNAIAPGFFPTKM 203
PRK06949 PRK06949
SDR family oxidoreductase;
41-226 1.79e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 71.72  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKEL----------SRRINKV--IVADIQSFPTFAQVeynnifyYQCDITSLDEIKNLKKAIERDH 108
Cdd:PRK06949  12 ALVTGASSGLGARFAQVLaqagakvvlaSRRVERLkeLRAEIEAEGGAAHV-------VSLDVTDYQSIKAAVAHAETEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   109 GNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGF--------IINIASVLGELTPARLT 180
Cdd:PRK06949  85 GTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIASVAGLRVLPQIG 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6320089   181 SYGASKGAMIGFHKCMsrhfrslSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK06949 165 LYCMSKAAVVHMTRAM-------ALEWGRHGINVNAICPGYIDTEI 203
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 37-224 1.80e-14

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 71.85  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEY-----NNIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK13394   6 NGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEinkagGKAIGVAMDVTNEDAVNAGIDKVAERFGSV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMI-DNREGFIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:PRK13394  86 DILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLL 165

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6320089   191 GFHKCmsrhfrsLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK13394 166 GLARV-------LAKEGAKHNVRSHVVCPGFVRT 192
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 40-230 1.96e-14

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 71.72  E-value: 1.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADI----QSFPTFAQVEY--NNIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINDLpdddQATEVVAEVLAagRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  114 IINNAGVAHIKK--LEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGF------IINIASVLGELTPARLTSYGAS 185
Cdd:cd05337  83 LVNNAGIAVRPRgdLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRFdgphrsIIFVTSINAYLVSPNRGEYCIS 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6320089  186 KGAmigfhkcMSRHFRSLSTECNKTGIKTLLVCPGKIKTNMFIDV 230
Cdd:cd05337 163 KAG-------LSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPV 200
PRK07577 PRK07577
SDR family oxidoreductase;
37-227 2.51e-14

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 70.91  E-value: 2.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIV---ADIQSFPTFaqveynnifYYQCDITSLDEIKNLKKAIeRDHGNINI 113
Cdd:PRK07577   2 SSRTVLVTGATKGIGLALSLRLANLGHQVIGiarSAIDDFPGE---------LFACDLADIEQTAATLAQI-NEIHPVDA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARlTSYGASKGAMIGfh 193
Cdd:PRK07577  72 IVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRAIFGALDR-TSYSAAKSALVG-- 148

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6320089   194 kCMsrhfRSLSTECNKTGIKTLLVCPGKIKTNMF 227
Cdd:PRK07577 149 -CT----RTWALELAEYGITVNAVAPGPIETELF 177
PRK06114 PRK06114
SDR family oxidoreductase;
41-226 3.99e-14

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 70.58  E-value: 3.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVeYNNI-------FYYQCDITSLdeiKNLKKAIER---DHGN 110
Cdd:PRK06114  11 AFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAET-AEHIeaagrraIQIAADVTSK---ADLRAAVARteaELGA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   111 INIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTS--YGASKGA 188
Cdd:PRK06114  87 LTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGLLQahYNASKAG 166

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6320089   189 MIgfHkcMSrhfRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK06114 167 VI--H--LS---KSLAMEWVGRGIRVNSISPGYTATPM 197
PRK06182 PRK06182
short chain dehydrogenase; Validated
 36-225 4.25e-14

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 70.76  E-value: 4.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    36 SKNATALITGGSSGLGFELAKELS----------RRINKviVADIQSFptfaqveynNIFYYQCDITSLDEIKNLKKAIE 105
Cdd:PRK06182   1 MQKKVALVTGASSGIGKATARRLAaqgytvygaaRRVDK--MEDLASL---------GVHPLSLDVTDEASIKAAVDTII 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   106 RDHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGAS 185
Cdd:PRK06182  70 AEEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHAT 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6320089   186 KGAMIGFHKCmsrhfrsLSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK06182 150 KFALEGFSDA-------LRLEVAPFGIDVVVIEPGGIKTE 182
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 39-256 5.08e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 70.74  E-value: 5.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    39 ATALITGGSSGLGFELAKELSRRINKVIVADI-QSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINN 117
Cdd:PRK07825   6 KVVAITGGARGIGLATARALAALGARVAIGDLdEALAKETAAELGLVVGGPLDVTDPASFAAFLDAVEADLGPIDVLVNN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   118 AGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKCMS 197
Cdd:PRK07825  86 AGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVGFTDAAR 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6320089   198 RHFRSlstecnkTGIKTLLVCPGKIKTNMfiDVPTPSKLLAPDIIPSQLALAIISAMEH 256
Cdd:PRK07825 166 LELRG-------TGVHVSVVLPSFVNTEL--IAGTGGAKGFKNVEPEDVAAAIVGTVAK 215
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 37-220 5.79e-14

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 70.70  E-value: 5.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADI-----QSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK08277   9 KGKVAVITGGGGVLGGAMAKELARAGAKVAILDRnqekaEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGPC 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIK----KLEHMTNKE-----------VEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGeLTP 176
Cdd:PRK08277  89 DILINGAGGNHPKattdNEFHELIEPtktffdldeegFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNA-FTP 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 6320089   177 -ARLTSYGASKGAMIGFHKCMSRHFrslstecNKTGIKTLLVCPG 220
Cdd:PRK08277 168 lTKVPAYSAAKAAISNFTQWLAVHF-------AKVGIRVNAIAPG 205
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 41-224 7.60e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 69.80  E-value: 7.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIV---------ADIQSFPTFAQVEYNNIFyyqcDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK07523  13 ALVTGSSQGIGYALAEGLAQAGAEVILngrdpaklaAAAESLKGQGLSAHALAF----DVTDHDAVRAAIDAFEAEIGPI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:PRK07523  89 DILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAVGN 168

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6320089   192 FHKCMsrhfrslSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK07523 169 LTKGM-------ATDWAKHGLQCNAIAPGYFDT 194
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 40-224 9.17e-14

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: 69.41  E-value: 9.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYN---NIFYYQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:cd05349   2 VVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEageRAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  117 NAGVAHI------KKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:cd05349  82 NALIDFPfdpdqrKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAKAALL 161

                       170       180       190
                ....*....|....*....|....*....|....
gi 6320089  191 GFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:cd05349 162 GFT-------RNMAKELGPYGITVNMVSGGLLKV 188
PRK06124 PRK06124
SDR family oxidoreductase;
32-224 9.34e-14

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 69.74  E-value: 9.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    32 PSILSK----NATALITGGSSGLGFELAKELSRRINKVIV-----ADIQsfPTFAQVEYNN------IFyyqcDITSLDE 96
Cdd:PRK06124   1 MSILQRfslaGQVALVTGSARGLGFEIARALAGAGAHVLVngrnaATLE--AAVAALRAAGgaaealAF----DIADEEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    97 IKNLKKAIERDHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTP 176
Cdd:PRK06124  75 VAAAFARIDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVAR 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6320089   177 ARLTSYGASKGAMIGFhkcmsrhFRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK06124 155 AGDAVYPAAKQGLTGL-------MRALAAEFGPHGITSNAIAPGYFAT 195
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
41-255 1.10e-13

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 69.33  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKEL----------SRRINKVIVAdiqsfptFAQVEYNNIFYYQCDITSLDEIKNLKKA----IER 106
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLlekgthvisiSRTENKELTK-------LAEQYNSNLTFHSLDLQDVHELETNFNEilssIQE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   107 DHGNINIIINNAG-VAHIKKLEHMTNKEVEQLIDINLIGAYRIISTF---AEDMidNREGFIINIASVLGELTPARLTSY 182
Cdd:PRK06924  77 DNVSSIHLINNAGmVAPIKPIEKAESEELITNVHLNLLAPMILTSTFmkhTKDW--KVDKRVINISSGAAKNPYFGWSAY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   183 GASKGAMIGFHKCMsrHFRSLSTEcnkTGIKTLLVCPGKIKTNM-----------------FIDVPTPSKLLAPDIIpsq 245
Cdd:PRK06924 155 CSSKAGLDMFTQTV--ATEQEEEE---YPVKIVAFSPGVMDTNMqaqirssskedftnldrFITLKEEGKLLSPEYV--- 226

                        250
                 ....*....|
gi 6320089   246 lALAIISAME 255
Cdd:PRK06924 227 -AKALRNLLE 235
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 37-227 2.07e-13

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: 68.65  E-value: 2.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYNNIFY------YQCDITSLDEIKNLKKAIERDHGN 110
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYgekaygFGADATNEQSVIALSKGVDEIFKR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  111 INIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMI-DNREGFIINIASVLGELTPARLTSYGASKGAM 189
Cdd:cd05322  81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIrDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGG 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6320089  190 IGFHKcmsrhfrSLSTECNKTGIKTLLVCPGK-IKTNMF 227
Cdd:cd05322 161 VGLTQ-------SLALDLAEHGITVNSLMLGNlLKSPMF 192
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 37-226 3.26e-13

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: 67.90  E-value: 3.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYNNIFYYQC--DITSLDEIKNLKKAIERDHGNINII 114
Cdd:cd08944   2 EGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALrvDVTDEQQVAALFERAVEEFGGLDLL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  115 INNAGVAHIKKLEHMTNKEV-EQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFH 193
Cdd:cd08944  82 VNNAGAMHLTPAIIDTDLAVwDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLT 161

                       170       180       190
                ....*....|....*....|....*....|...
gi 6320089  194 kcmsrhfRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd08944 162 -------RTLAAELRHAGIRCNALAPGLIDTPL 187
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 40-240 4.41e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 67.83  E-value: 4.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINNAG 119
Cdd:PRK06057   9 VAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGGLFVPTDVTDEDAVNALFDTAAETYGSVDIAFNNAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   120 VAHIKKlEHMTNKEVE---QLIDINLIGAYRIISTFAEDMIDNREGFIINIAS---VLGELTPArlTSYGASKGAMIGfh 193
Cdd:PRK06057  89 ISPPED-DSILNTGLDawqRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASfvaVMGSATSQ--ISYTASKGGVLA-- 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6320089   194 kcMSRHfrsLSTECNKTGIKTLLVCPGKIKTnmfidvPTPSKLLAPD 240
Cdd:PRK06057 164 --MSRE---LGVQFARQGIRVNALCPGPVNT------PLLQELFAKD 199
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 37-226 4.46e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 67.86  E-value: 4.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADI------QSFPTFAQVEYNnIFYYQCDITSLDEIKNLKKAIERDHGN 110
Cdd:PRK08085   8 AGKNILITGSAQGIGFLLATGLAEYGAEIIINDItaeraeLAVAKLRQEGIK-AHAAPFNVTHKQEVEAAIEHIEKDIGP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   111 INIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMi 190
Cdd:PRK08085  87 IDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGAV- 165

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6320089   191 gfhKCMSrhfRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK08085 166 ---KMLT---RGMCVELARHNIQVNGIAPGYFKTEM 195
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 38-190 1.11e-12

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: 66.45  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   38 NATALITGGSSGLGFELAKELSRRINKVIVADI--QSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIdeERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLV 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320089  116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNReGFIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:cd09761  81 NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAASKGGLV 154
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 38-224 1.38e-12

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: 66.14  E-value: 1.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   38 NATALITGGSSGLGFELAKEL----------SRRINKVIVADIQSFPTFAQVeynniFYYQCDITSLDEIKNLKKAIERD 107
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALaregarvaicARNRENLERAASELRAGGAGV-----LAVVADLTDPEDIDRLVEKAGDA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  108 HGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLG-ELTPARLTSyGASK 186
Cdd:cd05344  76 FGRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVkEPEPNLVLS-NVAR 154

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6320089  187 GAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:cd05344 155 AGLIGLVK-------TLSRELAPDGVTVNSVLPGYIDT 185
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 41-231 1.42e-12

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 65.23  E-value: 1.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRR-INKVIVadiqsfptfaqveynnifyyqcdITSLDEIKNLkkaierdhgniniiinnAG 119
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRgSPKVLV-----------------------VSRRDVVVHN-----------------AA 40

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  120 VAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFhkcmsrh 199
Cdd:cd02266  41 ILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGL------- 113

                       170       180       190
                ....*....|....*....|....*....|..
gi 6320089  200 FRSLSTECNKTGIKTLLVCPGKIKTNMFIDVP 231
Cdd:cd02266 114 AQQWASEGWGNGLPATAVACGTWAGSGMAKGP 145
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-226 1.43e-12

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 66.14  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQS---FPTFAQVEYNNI--FYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK08217   4 KDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQeklEEAVAECGALGTevRGYAANVTDEEDVEATFAQIAEDFGQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAH----IKKLEH-----MTNKEVEQLIDINLIGAYRIISTFAEDMIDN-REGFIINIASVlgeltpARL-- 179
Cdd:PRK08217  84 NGLINNAGILRdgllVKAKDGkvtskMSLEQFQSVIDVNLTGVFLCGREAAAKMIESgSKGVIINISSI------ARAgn 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6320089   180 ---TSYGASKG---AM-IGFHKCMSRHfrslstecnktGIKTLLVCPGKIKTNM 226
Cdd:PRK08217 158 mgqTNYSASKAgvaAMtVTWAKELARY-----------GIRVAAIAPGVIETEM 200
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 40-226 1.82e-12

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 66.06  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQsfptFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINNAG 119
Cdd:PRK08220  10 TVWVTGAAQGIGYAVALAFVEAGAKVIGFDQA----FLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLDVLVNAAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   120 VAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKCMSRH 199
Cdd:PRK08220  86 ILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSLAKCVGLE 165

                        170       180
                 ....*....|....*....|....*..
gi 6320089   200 FRSLSTECNktgiktlLVCPGKIKTNM 226
Cdd:PRK08220 166 LAPYGVRCN-------VVSPGSTDTDM 185
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 38-233 1.85e-12

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 66.02  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    38 NATALITGGSSGLGFELAKELSRRINKVIVADIQSfPTFAQVEYN------NIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK06113  11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINA-DAANHVVDEiqqlggQAFACRCDITSEQELSALADFALSKLGKV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEhMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAmig 191
Cdd:PRK06113  90 DILVNNAGGGGPKPFD-MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAA--- 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6320089   192 fhkcMSRHFRSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTP 233
Cdd:PRK06113 166 ----ASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITP 203
PRK06914 PRK06914
SDR family oxidoreductase;
37-225 2.43e-12

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 65.82  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIV--------ADIQSFPTFAQVeYNNIFYYQCDITSLDEIKNLKKAIERdH 108
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIAtmrnpekqENLLSQATQLNL-QQNIKVQQLDVTDQNSIHNFQLVLKE-I 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   109 GNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGA 188
Cdd:PRK06914  80 GRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYA 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6320089   189 MIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK06914 160 LEGFSE-------SLRLELKPFGIDVALIEPGSYNTN 189
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 40-231 2.90e-12

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: 65.56  E-value: 2.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKV--IVADIQSFPTFAQVEYNNIFYY-------QCDITSLDEIKNLKKAIERDHgn 110
Cdd:cd09806   2 VVLITGCSSGIGLHLAVRLASDPSKRfkVYATMRDLKKKGRLWEAAGALAggtletlQLDVCDSKSVAAAVERVTERH-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  111 INIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:cd09806  80 VDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALE 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 6320089  191 GFhkcmsrhFRSLSTECNKTGIKTLLVCPGKIKT----NMFIDVP 231
Cdd:cd09806 160 GL-------CESLAVQLLPFNVHLSLIECGPVHTafmeKVLGSPE 197
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 40-240 3.66e-12

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: 65.10  E-value: 3.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADIQSfptfAQVEY------NNIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:cd05345   7 VAIVTGAGSGFGEGIARRFAQEGARVVIADINA----DGAERvaadigEAAIAIQADVTKRADVEAMVEAALSKFGRLDI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  114 IINNAGVAHIKK-LEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGF 192
Cdd:cd05345  83 LVNNAGITHRNKpMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVTA 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 6320089  193 HKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNMFidvptpSKLLAPD 240
Cdd:cd05345 163 TK-------AMAVELAPRNIRVNCLCPVAGETPLL------SMFMGED 197
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 36-226 3.85e-12

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: 65.25  E-value: 3.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   36 SKNATALITGGSSGLGFELAKELSRRINKVIV---------ADIQSFptfaQVEYNNIFYYQCDITSLDEIKNLKKAIER 106
Cdd:cd08945   1 QDSEVALVTGATSGIGLAIARRLGKEGLRVFVcargeeglaTTVKEL----REAGVEADGRTCDVRSVPEIEALVAAAVA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  107 DHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAED--MIDNREGFIINIASVLGELTPARLTSYGA 184
Cdd:cd08945  77 RYGPIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSA 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 6320089  185 SKGAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd08945 157 SKHGVVGFTK-------ALGLELARTGITVNAVCPGFVETPM 191
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 37-224 5.37e-12

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 64.53  E-value: 5.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKEL----------SRRINKV--IVADIQSFpTFAQVEYnnifyYQCDITSLDEIKNLKKAI 104
Cdd:cd05369   2 KGKVAFITGGGTGIGKAIAKAFaelgasvaiaGRKPEVLeaAAEEISSA-TGGRAHP-----IQCDVRDPEAVEAAVDET 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  105 ERDHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNR-EGFIINIASVLGELTPARLTSYG 183
Cdd:cd05369  76 LKEFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKhGGSILNISATYAYTGSPFQVHSA 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6320089  184 ASKGAMIGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:cd05369 156 AAKAGVDALT-------RSLAVEWGPYGIRVNAIAPGPIPT 189
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 41-250 6.69e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 64.05  E-value: 6.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEY---NNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINN 117
Cdd:PRK12828  10 VAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGvpaDALRIGGIDLVDPQAARRAVDEVNRQFGRLDALVNI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   118 AGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFhkcms 197
Cdd:PRK12828  90 AGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVARL----- 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6320089   198 rhFRSLSTECNKTGIKTLLVCPGKIKTNMfIDVPTPSKLLAPDIIPSQLALAI 250
Cdd:PRK12828 165 --TEALAAELLDRGITVNAVLPSIIDTPP-NRADMPDADFSRWVTPEQIAAVI 214
PRK05867 PRK05867
SDR family oxidoreductase;
41-226 6.74e-12

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 64.29  E-value: 6.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVA--DIQSFPTFAQ---VEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:PRK05867  12 ALITGASTGIGKRVALAYVEAGAQVAIAarHLDALEKLADeigTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDIAV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDN-REGFIINIASVLGEL--TPARLTSYGASKGAMIGF 192
Cdd:PRK05867  92 CNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIinVPQQVSHYCASKAAVIHL 171

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6320089   193 HKCMSRHFRSLSTECNKtgiktllVCPGKIKTNM 226
Cdd:PRK05867 172 TKAMAVELAPHKIRVNS-------VSPGYILTEL 198
PRK06138 PRK06138
SDR family oxidoreductase;
37-227 8.50e-12

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 64.02  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADI----QSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNIN 112
Cdd:PRK06138   4 AGRVAIVTGAGSGIGRATAKLFAREGARVVVADRdaeaAERVAAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWGRLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   113 IIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGF 192
Cdd:PRK06138  84 VLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIASL 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6320089   193 HKCMSRHFRslstecnKTGIKTLLVCPGKIKTNMF 227
Cdd:PRK06138 164 TRAMALDHA-------TDGIRVNAVAPGTIDTPYF 191
PRK08589 PRK08589
SDR family oxidoreductase;
38-224 1.55e-11

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 63.64  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    38 NATALITGGSSGLGFELAKELSRRINKVIVADI--QSFPTFAQVEYN--NIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:PRK08589   6 NKVAVITGASTGIGQASAIALAQEGAYVLAVDIaeAVSETVDKIKSNggKAKAYHVDISDEQQVKDFASEIKEQFGRVDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKKLEHMTNKEV-EQLIDINLIGAYrIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGF 192
Cdd:PRK08589  86 LFNNAGVDNAAGRIHEYPVDVfDKIMAVDMRGTF-LMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYNAAKGAVINF 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 6320089   193 HkcmsrhfRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK08589 165 T-------KSIAIEYGRDGIRANAIAPGTIET 189
PRK08017 PRK08017
SDR family oxidoreductase;
40-224 1.65e-11

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 63.18  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQSfptfAQVEYNNIFYYQCDITSLDEIKNLKKA----IERDHGNINIII 115
Cdd:PRK08017   4 SVLITGCSSGIGLEAALELKRRGYRVLAACRKP----DDVARMNSLGFTGILLDLDDPESVERAadevIALTDNRLYGLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGEL-TPARlTSYGASKGAMIGFHK 194
Cdd:PRK08017  80 NNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLIsTPGR-GAYAASKYALEAWSD 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 6320089   195 cmsrhfrSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK08017 159 -------ALRMELRHSGIKVSLIEPGPIRT 181
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 41-229 1.89e-11

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: 62.79  E-value: 1.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVADIQS--FPTFAQVEYNNIFY--YQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:cd08943   4 ALVTGGASGIGLAIAKRLAAEGAAVVVADIDPeiAEKVAEAAQGGPRAlgVQCDVTSEAQVQSAFEQAVLEFGGLDIVVS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  117 NAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMI-DNREGFIINIASVLGELTPARLTSYGASKGAMIgfHKC 195
Cdd:cd08943  84 NAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKsQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEA--HLA 161

                       170       180       190
                ....*....|....*....|....*....|....
gi 6320089  196 msrhfRSLSTECNKTGIKTLLVCPGKIKTNMFID 229
Cdd:cd08943 162 -----RCLALEGGEDGIRVNTVNPDAVFRGSKIW 190
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 39-224 3.13e-11

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: 62.30  E-value: 3.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   39 ATALITGGSSGLGFELAKELSRRINKVI--------VADIQSfpTFAQVEYNNIFYYQCDITSLDEIK----NLKKAIER 106
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLIltgrraerLQELAD--ELGAKFPVKVLPLQLDVSDRESIEaaleNLPEEFRD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  107 DHGNINIIINNAGVAHIKKLEHmtnKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASK 186
Cdd:cd05346  79 IDILVNNAGLALGLDPAQEADL---EDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATK 155

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6320089  187 GAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:cd05346 156 AAVRQFSL-------NLRKDLIGTGIRVTNIEPGLVET 186
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
37-190 3.37e-11

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 62.35  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADI--QSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:PRK07067   5 QGKVALLTGAASGIGEAVAERYLAEGARVVIADIkpARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDIL 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6320089   115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREG-FIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:PRK07067  85 FNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGgKIINMASQAGRRGEALVSHYCATKAAVI 161
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 42-239 3.67e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 62.36  E-value: 3.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    42 LITGGSSGLGFELAKELSRRINKVIVA--DIQSFPTFAQVEYNNIFYYQCDITSLDEI-KNLKKAIERdHGNINIIINNA 118
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATarDTATLADLAEKYGDRLLPLALDVTDRAAVfAAVETAVEH-FGRLDIVVNNA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   119 GVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKcmsr 198
Cdd:PRK08263  86 GYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSE---- 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 6320089   199 hfrSLSTECNKTGIKTLLVCPGKIKTNMF---IDVPTPSKLLAP 239
Cdd:PRK08263 162 ---ALAQEVAEFGIKVTLVEPGGYSTDWAgtsAKRATPLDAYDT 202
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 40-224 4.54e-11

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: 62.08  E-value: 4.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVA--DIQSFPTFAQVEYNNIFYY---QCDITSLDEIKNLKKAIE-RDHGNINI 113
Cdd:cd05329   8 TALVTGGTKGIGYAIVEELAGLGAEVYTCarNQKELDECLTEWREKGFKVegsVCDVSSRSERQELMDTVAsHFGGKLNI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGeLTPARLTS-YGASKGAmigf 192
Cdd:cd05329  88 LVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAG-VIAVPSGApYGATKGA---- 162

                       170       180       190
                ....*....|....*....|....*....|..
gi 6320089  193 hkcMSRHFRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:cd05329 163 ---LNQLTRSLACEWAKDNIRVNAVAPWVIAT 191
PRK06482 PRK06482
SDR family oxidoreductase;
40-225 4.84e-11

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 62.06  E-value: 4.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVI--VADIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINN 117
Cdd:PRK06482   4 TWFITGASSGFGRGMTERLLARGDRVAatVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDVVVSN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   118 AGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFhkcms 197
Cdd:PRK06482  84 AGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGF----- 158

                        170       180
                 ....*....|....*....|....*...
gi 6320089   198 rhFRSLSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK06482 159 --VEAVAQEVAPFGIEFTIVEPGPARTN 184
PRK07024 PRK07024
SDR family oxidoreductase;
43-226 4.99e-11

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 61.87  E-value: 4.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    43 ITGGSSGLGFELAKE----------LSRRiNKVIVADIQSFPTFAQVEynnifYYQCDITSLDEIKNLKKAIERDHGNIN 112
Cdd:PRK07024   7 ITGASSGIGQALAREyarqgatlglVARR-TDALQAFAARLPKAARVS-----VYAADVRDADALAAAAADFIAAHGLPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   113 IIINNAGVAHIKKLEHMTNKEV-EQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLG--ELTPArlTSYGASKGAM 189
Cdd:PRK07024  81 VVIANAGISVGTLTEEREDLAVfREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGvrGLPGA--GAYSASKAAA 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6320089   190 IGFhkcmsrhFRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK07024 159 IKY-------LESLRVELRPAGVRVVTIAPGYIRTPM 188
PRK05855 PRK05855
SDR family oxidoreductase;
41-225 7.77e-11

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 62.69  E-value: 7.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFP---TFAQVEYNN--IFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:PRK05855 318 VVVTGAGSGIGRETALAFAREGAEVVASDIDEAAaerTAELIRAAGavAHAYRVDVSDADAMEAFAEWVRAEHGVPDIVV 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNRE-GFIINIASvLGELTPAR-LTSYGASKGAMIGFH 193
Cdd:PRK05855 398 NNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTgGHIVNVAS-AAAYAPSRsLPAYATSKAAVLMLS 476

                        170       180       190
                 ....*....|....*....|....*....|..
gi 6320089   194 KCmsrhfrsLSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK05855 477 EC-------LRAELAAAGIGVTAICPGFVDTN 501
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 43-256 7.95e-11

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: 60.86  E-value: 7.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   43 ITGGSSGLGFELAKELSRRINKVIVA------------DIQSFPTFAQVeynnifyYQCDITSLDEIKNLKKAIERDHGN 110
Cdd:cd05360   5 ITGASSGIGRATALAFAERGAKVVLAarsaealhelarEVRELGGEAIA-------VVADVADAAQVERAADTAVERFGR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  111 INIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAyrIISTFA--EDMIDNREGFIINIASVLGELTPARLTSYGASKGA 188
Cdd:cd05360  78 IDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGH--VYGTLAalPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHA 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320089  189 MIGFhkcmsrhFRSLSTECNKTG--IKTLLVCPGKIKTNMF----IDVPTPSKLLAPDIIPSQLALAIISAMEH 256
Cdd:cd05360 156 VRGF-------TESLRAELAHDGapISVTLVQPTAMNTPFFgharSYMGKKPKPPPPIYQPERVAEAIVRAAEH 222
PRK06500 PRK06500
SDR family oxidoreductase;
37-227 1.03e-10

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 60.74  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVA--DIQSFPTfAQVEY-NNIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:PRK06500   5 QGKTALITGGTSGIGLETARQFLAEGARVAITgrDPASLEA-ARAELgESALVIRADAGDVAAQKALAQALAEAFGRLDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEdmIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFH 193
Cdd:PRK06500  84 VFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLP--LLANPASIVLNGSINAHIGMPNSSVYAASKAALLSLA 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6320089   194 KcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNMF 227
Cdd:PRK06500 162 K-------TLSGELLPRGIRVNAVSPGPVQTPLY 188
PRK08264 PRK08264
SDR family oxidoreductase;
37-255 1.19e-10

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 60.29  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKE-LSRRINKVIVA--DIQSFPTFAqveyNNIFYYQCDITSLDEIKNLKKAIerdhGNINI 113
Cdd:PRK08264   5 KGKVVLVTGANRGIGRAFVEQlLARGAAKVYAAarDPESVTDLG----PRVVPLQLDVTDPASVAAAAEAA----SDVTI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKK-LEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGF 192
Cdd:PRK08264  77 LVNNAGIFRTGSlLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWSL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320089   193 HKCMsRHfrSLSTEcnktGIKTLLVCPGKIKTNMfidvptPSKLLAPDIIPSQLALAIISAME 255
Cdd:PRK08264 157 TQAL-RA--ELAPQ----GTRVLGVHPGPIDTDM------AAGLDAPKASPADVARQILDALE 206
PRK07063 PRK07063
SDR family oxidoreductase;
37-229 1.30e-10

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 60.83  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQsFPTFAQVEYN--------NIFYYQCDITSLDEIKNLKKAIERDH 108
Cdd:PRK07063   6 AGKVALVTGAAQGIGAAIARAFAREGAAVALADLD-AALAERAAAAiardvagaRVLAVPADVTDAASVAAAVAAAEEAF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   109 GNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLG-ELTPARLtSYGASKG 187
Cdd:PRK07063  85 GPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAfKIIPGCF-PYPVAKH 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6320089   188 AMIGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKTNMFID 229
Cdd:PRK07063 164 GLLGLT-------RALGIEYAARNVRVNAIAPGYIETQLTED 198
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 40-230 1.82e-10

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 60.36  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYN------NIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:PRK12745   4 VALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQElralgvEVIFFPADVADLSAHEAMLDAAQAAWGRIDC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKK---LEhMTNKEVEQLIDINLIGAYRIISTFAEDMIDNRE------GFIINIASVLGELT-PARLtSYG 183
Cdd:PRK12745  84 LVNNAGVGVKVRgdlLD-LTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVsPNRG-EYC 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6320089   184 ASKGAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNMFIDV 230
Cdd:PRK12745 162 ISKAGLSMAAQ-------LFAARLAEEGIGVYEVRPGLIKTDMTAPV 201
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 40-253 1.97e-10

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: 60.10  E-value: 1.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVA-------DIQSFPTFAQVEYNNI----------FYYQCDITSLDEIKNLKK 102
Cdd:cd05338   5 VAFVTGASRGIGRAIALRLAKAGATVVVAaktasegDNGSAKSLPGTIEETAeeieaaggqaLPIVVDVRDEDQVRALVE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  103 AIERDHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGeLTPARL-TS 181
Cdd:cd05338  85 ATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLS-LRPARGdVA 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320089  182 YGASKGAMIGFHKCMSRHFRSLSTECNKTGIKTLLVCPGkikTNMFIDVPTPSKLLAPDIIpSQLALAIISA 253
Cdd:cd05338 164 YAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPA---ATELSGGSDPARARSPEIL-SDAVLAILSR 231
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 37-227 2.19e-10

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: 59.86  E-value: 2.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFA-QVEYNNI-----FYYQCDITSLDEIKNLKKAIERDHGN 110
Cdd:cd08933   8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQAlESELNRAgpgscKFVPCDVTKEEDIKTLISVTVERFGR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  111 INIIINNAGVaHI--KKLEHMTNKEVEQLIDINLIGAYrIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGA 188
Cdd:cd08933  88 IDCLVNNAGW-HPphQTTDETSAQEFRDLLNLNLISYF-LASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATKGA 165

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 6320089  189 MIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNMF 227
Cdd:cd08933 166 ITAMTK-------ALAVDESRYGVRVNCISPGNIWTPLW 197
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 42-226 2.26e-10

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


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 59.98  E-value: 2.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   42 LITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQ----VEYNNIFYYQCDITSLDEIKnlkKAIE--RDHGNIN--- 112
Cdd:cd09805   4 LITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNGPGAKelrrVCSDRLRTLQLDVTKPEQIK---RAAQwvKEHVGEKglw 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  113 IIINNAGVAHIKKLEHMTNKEV-EQLIDINLIGAYRIISTFAEdMIDNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:cd09805  81 GLVNNAGILGFGGDEELLPMDDyRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEA 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6320089  192 FHKCMSRhfrslstECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd09805 160 FSDSLRR-------ELQPWGVKVSIIEPGNFKTGI 187
PRK06194 PRK06194
hypothetical protein; Provisional
 37-225 2.31e-10

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 60.03  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFP---TFAQVEYNNI--FYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK06194   5 AGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDAldrAVAELRAQGAevLGVRTDVSDAAQVEALADAALERFGAV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDN------REGFIINIASVLGELTPARLTSYGAS 185
Cdd:PRK06194  85 HLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpaYEGHIVNTASMAGLLAPPAMGIYNVS 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6320089   186 KGAMIGFHKCMSRHFRSLSTEcnktgIKTLLVCPGKIKTN 225
Cdd:PRK06194 165 KHAVVSLTETLYQDLSLVTDQ-----VGASVLCPYFVPTG 199
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 39-226 3.10e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 59.34  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    39 ATALITGGSSGLGFELAKELSRRINKVIVADI-QSFPTFAQVEYNnifyyqCDITSLDEIKNLK-KAIERDHGNINIIIN 116
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARnAAALDRLAGETG------CEPLRLDVGDDAAiRAALAAAGAFDGLVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   117 NAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMI-DNREGFIINIASVLGEL-TPARLtSYGASKGAMIGFHk 194
Cdd:PRK07060  84 CAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIaAGRGGSIVNVSSQAALVgLPDHL-AYCASKAALDAIT- 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 6320089   195 cmsrhfRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK07060 162 ------RVLCVELGPHGIRVNSVNPTVTLTPM 187
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 37-254 3.97e-10

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: 58.96  E-value: 3.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKE-LSRRINKVIVA--DIQSFPTFAQVEYNNIFYYQCDITSLDEIKNL-KKAIERDhgnin 112
Cdd:cd05354   2 KDKTVLVTGANRGIGKAFVESlLAHGAKKVYAAvrDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAaAQAKDVD----- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  113 IIINNAGVAHIKK-LEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:cd05354  77 VVINNAGVLKPATlLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYS 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320089  192 FHKCmsrhfrsLSTECNKTGIKTLLVCPGKIKTNMF--IDVPTPSkllapdiiPSQLALAIISAM 254
Cdd:cd05354 157 LTQG-------LRAELAAQGTLVLSVHPGPIDTRMAagAGGPKES--------PETVAEAVLKAL 206
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 37-224 4.05e-10

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 59.35  E-value: 4.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVaDIQSFPTFAQVEYNNI-------FYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:PRK08936   6 EGKVVVITGGSTGLGRAMAVRFGKEKAKVVI-NYRSDEEEANDVAEEIkkaggeaIAVKGDVTVESDVVNLIQTAVKEFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   110 NINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAY----RIISTFAEdmiDNREGFIINIASVLGELTPARLTSYGAS 185
Cdd:PRK08936  85 TLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFlgsrEAIKYFVE---HDIKGNIINMSSVHEQIPWPLFVHYAAS 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6320089   186 KGAMigfhKCMSrhfRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK08936 162 KGGV----KLMT---ETLAMEYAPKGIRVNNIGPGAINT 193
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 41-224 1.78e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 57.22  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLG---FELAKELSRRInkVIVADIQSFPTFAQVEYnnifyYQCDITSLDEIKNLKKAIERDHGNINIIINN 117
Cdd:PRK06523  12 ALVTGGTKGIGaatVARLLEAGARV--VTTARSRPDDLPEGVEF-----VAADLTTAEGCAAVARAVLERLGGVDILVHV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   118 AG--VAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELT-PARLTSYGASKGAMIGFHK 194
Cdd:PRK06523  85 LGgsSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPlPESTTAYAAAKAALSTYSK 164

                        170       180       190
                 ....*....|....*....|....*....|
gi 6320089   195 cmsrhfrSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK06523 165 -------SLSKEVAPKGVRVNTVSPGWIET 187
PRK09730 PRK09730
SDR family oxidoreductase;
39-236 2.02e-09

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 57.17  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    39 ATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVeYNNI-------FYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEV-VNLItqaggkaFVLQADISDENQVVAMFTAIDQHDEPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIK-KLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDN---REGFIINIASVLGEL-TPARLTSYGASK 186
Cdd:PRK09730  81 AALVNNAGILFTQcTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLgAPGEYVDYAASK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 6320089   187 GAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNMFIDVPTPSKL 236
Cdd:PRK09730 161 GAIDTLTT-------GLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGRV 203
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 40-188 2.07e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 57.29  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQSfPTFAQVEY-----NNIFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:PRK05872  11 VVVVTGAARGIGAELARRLHARGAKLALVDLEE-AELAALAAelggdDRVLTVVADVTDLAAMQAAAEEAVERFGGIDVV 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320089   115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNReGFIINIASvLGELTPA-RLTSYGASKGA 188
Cdd:PRK05872  90 VANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSS-LAAFAAApGMAAYCASKAG 162
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
37-230 2.45e-09

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 57.04  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVAD--IQSFPTFAQ---VEYNNIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDynEETAQAAADklsKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAY----RIISTFAEdmiDNREGFIINIASVLGELTPARLTSYGASKG 187
Cdd:PRK08643  81 NVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIwgiqAAQEAFKK---LGHGGKIINATSQAGVVGNPELAVYSSTKF 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 6320089   188 AMIGFHKCMSRHFRSLstecnktGIKTLLVCPGKIKTNMFIDV 230
Cdd:PRK08643 158 AVRGLTQTAARDLASE-------GITVNAYAPGIVKTPMMFDI 193
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 37-226 2.46e-09

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: 56.76  E-value: 2.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQS---FPTFAQVEYNN----IFYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:cd05330   2 KDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEeglEAAKAALLEIApdaeVLLIKADVSDEAQVEAYVDATVEQFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  110 NINIIINNAGVAHIKKL-EHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGA 188
Cdd:cd05330  82 RIDGFFNNAGIEGKQNLtEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHG 161

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6320089  189 MIGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd05330 162 VVGLT-------RNSAVEYGQYGIRINAIAPGAILTPM 192
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 40-227 3.41e-09

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: 56.47  E-value: 3.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADI--QSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINN 117
Cdd:cd05363   5 TALITGSARGIGRAFAQAYVREGARVAIADInlEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDILVNN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  118 AGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMI-DNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKcm 196
Cdd:cd05363  85 AALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIaQGRGGKIINMASQAGRRGEALVGVYCATKAAVISLTQ-- 162

                       170       180       190
                ....*....|....*....|....*....|.
gi 6320089  197 srhfrSLSTECNKTGIKTLLVCPGKIKTNMF 227
Cdd:cd05363 163 -----SAGLNLIRHGINVNAIAPGVVDGEHW 188
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 40-231 6.30e-09

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: 55.69  E-value: 6.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVA------------DIqsfptFAQVEYNNIFYYQCDITSLDEIKNLKKAIERD 107
Cdd:cd05327   3 VVVITGANSGIGKETARELAKRGAHVIIAcrneekgeeaaaEI-----KKETGNAKVEVIQLDLSSLASVRQFAEEFLAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  108 HGNINIIINNAGVAHIKklEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTP----------- 176
Cdd:cd05327  78 FPRLDILINNAGIMAPP--RRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPidfndldlenn 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6320089  177 ---ARLTSYGASKGAMIGFHKCMSRHFrslstecNKTGIKTLLVCPGKIKTNMFIDVP 231
Cdd:cd05327 156 keySPYKAYGQSKLANILFTRELARRL-------EGTGVTVNALHPGVVRTELLRRNG 206
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
41-242 1.51e-08

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 54.63  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFA-----QVEYNNIFY-YQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:PRK12938   6 AYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVkwledQKALGFDFIaSEGNVGDWDSTKAAFDKVKAEVGEIDVL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   115 INNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHk 194
Cdd:PRK12938  86 VNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIHGFT- 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6320089   195 cmsrhfRSLSTECNKTGIKTLLVCPGKIKTNMFidvptpsKLLAPDII 242
Cdd:PRK12938 165 ------MSLAQEVATKGVTVNTVSPGYIGTDMV-------KAIRPDVL 199
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 38-229 1.68e-08

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 54.36  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    38 NATALITGGSSGLGFELAKELSRRINKVIV------ADIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVnyagsaAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMidNREGFIINIA-SVLGELTPArLTSYGASKGAMI 190
Cdd:PRK12937  85 DVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLStSVIALPLPG-YGPYAASKAAVE 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6320089   191 GFHKCMSRHFRSlstecnkTGIKTLLVCPGKIKTNMFID 229
Cdd:PRK12937 162 GLVHVLANELRG-------RGITVNAVAPGPVATELFFN 193
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
41-225 1.75e-08

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 54.14  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFP-TFAQVE-YNNIFYY-QCDITSLDEIKNLKKAIERDHGNINIIINN 117
Cdd:PRK12481  11 AIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPeTQAQVEaLGRKFHFiTADLIQQKDIDSIVSQAVEVMGHIDILINN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   118 AGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREG-FIINIASVLGELTPARLTSYGASKGAMIGFHkcm 196
Cdd:PRK12481  91 AGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNGgKIINIASMLSFQGGIRVPSYTASKSAVMGLT--- 167

                        170       180
                 ....*....|....*....|....*....
gi 6320089   197 srhfRSLSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK12481 168 ----RALATELSQYNINVNAIAPGYMATD 192
PRK07069 PRK07069
short chain dehydrogenase; Validated
 41-231 2.04e-08

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 53.95  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQV--EYNNI------FYYQCDITSLDEIKNLKKAIERDHGNIN 112
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFaaEINAAhgegvaFAAVQDVTDEAQWQALLAQAADAMGGLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   113 IIINNAGVAHIKKLEHMTNKEVEQLIDIN----LIGAYRIISTfaedMIDNREGFIINIASVLGELTPARLTSYGASKGA 188
Cdd:PRK07069  82 VLVNNAGVGSFGAIEQIELDEWRRVMAINvesiFLGCKHALPY----LRASQPASIVNISSVAAFKAEPDYTAYNASKAA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6320089   189 MIGFHKcmsrhfrSLSTECNKTGIktllvcpgKIKTN----MFIDVP 231
Cdd:PRK07069 158 VASLTK-------SIALDCARRGL--------DVRCNsihpTFIRTG 189
PRK08267 PRK08267
SDR family oxidoreductase;
42-258 2.75e-08

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 53.79  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    42 LITGGSSGLGFELAKELSRR--------INKVIVADIQsfptfAQVEYNNIFYYQCDITSLDEIKN-LKKAIERDHGNIN 112
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEgwrvgaydINEAGLAALA-----AELGAGNAWTGALDVTDRAAWDAaLADFAAATGGRLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   113 IIINNAGVAHIKKLEHMTNKEVEQLIDINLIGA---------YRIISTFAEdmidnregfIINIASVLGELTPARLTSYG 183
Cdd:PRK08267  80 VLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVlngahaalpYLKATPGAR---------VINTSSASAIYGQPGLAVYS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   184 ASKGAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM------FIDVPTPSKLLApDIIPSQLALAIISAMEHN 257
Cdd:PRK08267 151 ATKFAVRGLTE-------ALDLEWRRHGIRVADVMPLFVDTAMldgtsnEVDAGSTKRLGV-RLTPEDVAEAVWAAVQHP 222


                 .
gi 6320089   258 H 258
Cdd:PRK08267 223 T 223
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 40-226 4.18e-08

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 54.07  E-value: 4.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADI-QSFPTFAQVEyNNI--FYYQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:PRK08261 212 VALVTGAARGIGAAIAEVLARDGAHVVCLDVpAAGEALAAVA-NRVggTALALDITAPDAPARIAEHLAERHGGLDIVVH 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   117 NAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASV------LGEltparlTSYGASKGAMI 190
Cdd:PRK08261 291 NAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSIsgiagnRGQ------TNYAASKAGVI 364

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6320089   191 GFHKCMSRHFRslstecnKTGIKTLLVCPGKIKTNM 226
Cdd:PRK08261 365 GLVQALAPLLA-------ERGITINAVAPGFIETQM 393
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 41-197 4.58e-08

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: 52.86  E-value: 4.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIV-----ADIQSFPTfaqvEYNNIFYYQCDITSLDEIKnlkKAIERdHGNINIII 115
Cdd:cd05351  10 ALVTGAGKGIGRATVKALAKAGARVVAvsrtqADLDSLVR----ECPGIEPVCVDLSDWDATE---EALGS-VGPVDLLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNR-EGFIINIASVLGELTPARLTSYGASKGAMIGFHK 194
Cdd:cd05351  82 NNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTVYCSTKAALDMLTK 161


                ...
gi 6320089  195 CMS 197
Cdd:cd05351 162 VMA 164
PRK09242 PRK09242
SDR family oxidoreductase;
38-224 7.23e-08

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 52.44  E-value: 7.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    38 NATALITGGSSGLGFELAKELSRRINKVIV-----ADIQSFPTFAQVEYNN--IFYYQCDITSLDEIKNLKKAIERDHGN 110
Cdd:PRK09242   9 GQTALITGASKGIGLAIAREFLGLGADVLIvardaDALAQARDELAEEFPEreVHGLAADVSDDEDRRAILDWVEDHWDG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   111 INIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRiISTFAEDMIDNRE-GFIINIASVLGeLTPARL-TSYGASKGA 188
Cdd:PRK09242  89 LHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFE-LSRYAHPLLKQHAsSAIVNIGSVSG-LTHVRSgAPYGMTKAA 166

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6320089   189 MIgfhkcmsRHFRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK09242 167 LL-------QMTRNLAVEWAEDGIRVNAVAPWYIRT 195
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 37-242 9.14e-08

(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: 51.94  E-value: 9.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   37 KNATALITGGSSGLGFELAKELSRRINKVIVADI---------QSFPTFAQVE------------YNnifyyqcDITSLD 95
Cdd:cd05353   4 DGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggdrkgsgkSSSAADKVVDeikaaggkavanYD-------SVEDGE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   96 EIknLKKAIERdHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELT 175
Cdd:cd05353  77 KI--VKTAIDA-FGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYG 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6320089  176 PARLTSYGASKGAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKiKTNMFIDV--PTPSKLLAPDII 242
Cdd:cd05353 154 NFGQANYSAAKLGLLGLSN-------TLAIEGAKYNITCNTIAPAA-GSRMTETVmpEDLFDALKPEYV 214
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 43-258 1.07e-07

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: 51.68  E-value: 1.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   43 ITGGSSGLGFELAKELSRR--------INKVIVADIQsfptfAQVEYNNIFYYQCDITSLDEIKN-LKKAIERDHGNINI 113
Cdd:cd08931   5 ITGAASGIGRETALLFARNgwfvglydIDEDGLAALA-----AELGAENVVAGALDVTDRAAWAAaLADFAAATGGRLDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFH 193
Cdd:cd08931  80 LFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLT 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320089  194 KCMSRHFRSLstecnktGIKTLLVCPGKIKT---NMFIDVPTPSKLLAPDIIPSQLALAIISAMEHNH 258
Cdd:cd08931 160 EALDVEWARH-------GIRVADVWPWFVDTpilTKGETGAAPKKGLGRVLPVSDVAKVVWAAAHGVP 220
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 15-226 1.55e-07

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: 51.52  E-value: 1.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   15 KHLKDFPSVILSLPSYNPSILSKNATALITGGSSGLGFELAKELSRRINKVIVA-------DIQSFPTFAQVEYNNIFYY 87
Cdd:cd05355   3 IEAKMDPLPDFGEKSYKGSGKLKGKKALITGGDSGIGRAVAIAFAREGADVAINylpeeedDAEETKKLIEEEGRKCLLI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   88 QCDITSLDEIKNLKKAIERDHGNINIIINNAGVAH-IKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMidNREGFIIN 166
Cdd:cd05355  83 PGDLGDESFCRDLVKEVVKEFGKLDILVNNAAYQHpQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIIN 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  167 IASVLGELTPARLTSYGASKGAMIGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd05355 161 TTSVTAYKGSPHLLDYAATKGAIVAFT-------RGLSLQLAEKGIRVNAVAPGPIWTPL 213
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 40-220 1.55e-07

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 51.55  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADI--QSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINN 117
Cdd:PRK08265   8 VAIVTGGATLIGAAVARALVAAGARVAIVDIdaDNGAAVAASLGERARFIATDITDDAAIERAVATVVARFGRVDILVNL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   118 A------GVAHikklehmTNKEVEQLIDINLIGAYRIISTFAEDMIdNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:PRK08265  88 ActylddGLAS-------SRADWLAALDVNLVSAAMLAQAAHPHLA-RGGGAIVNFTSISAKFAQTGRWLYPASKAAIRQ 159

                        170       180
                 ....*....|....*....|....*....
gi 6320089   192 FHkcmsrhfRSLSTECNKTGIKTLLVCPG 220
Cdd:PRK08265 160 LT-------RSMAMDLAPDGIRVNSVSPG 181
PRK07035 PRK07035
SDR family oxidoreductase;
41-224 2.16e-07

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 51.17  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKEL----------SRRINKV------IVADIQSFPTFAqveynnifyyqCDITSLDEIKNLKKAI 104
Cdd:PRK07035  11 ALVTGASRGIGEAIAKLLaqqgahvivsSRKLDGCqavadaIVAAGGKAEALA-----------CHIGEMEQIDALFAHI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   105 ERDHGNINIIINNAgvAHIKKLEHMTNKEV---EQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGeLTPARLTS 181
Cdd:PRK07035  80 RERHGRLDILVNNA--AANPYFGHILDTDLgafQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNG-VSPGDFQG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 6320089   182 -YGASKGAMIGfhkcMSRHFrslSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK07035 157 iYSITKAAVIS----MTKAF---AKECAPFGIRVNALLPGLTDT 193
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-226 4.29e-07

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 50.10  E-value: 4.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIV------ADIQSfpTFAQVEYN--NIFYYQCDITSLDEIKNLKKAIERDH 108
Cdd:PRK06077   5 KDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVnakkraEEMNE--TLKMVKENggEGIGVLADVSTREGCETLAKATIDRY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   109 GNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNreGFIINIASVLGELTPARLTSYGASKGA 188
Cdd:PRK06077  83 GVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREG--GAIVNIASVAGIRPAYGLSIYGAMKAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6320089   189 MIGFHKCMSRHFrslstecnKTGIKTLLVCPGKIKTNM 226
Cdd:PRK06077 161 VINLTKYLALEL--------APKIRVNAIAPGFVKTKL 190
PRK12743 PRK12743
SDR family oxidoreductase;
38-226 5.27e-07

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 50.03  E-value: 5.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    38 NATALITGGSSGLGFELAKELSRRINKVIV-------------ADIQSFPTFAQVEynnifyyQCDITSLDEIKNLKKAI 104
Cdd:PRK12743   2 AQVAIVTASDSGIGKACALLLAQQGFDIGItwhsdeegaketaEEVRSHGVRAEIR-------QLDLSDLPEGAQALDKL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   105 ERDHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMID-NREGFIINIASVlGELTPARLTS-Y 182
Cdd:PRK12743  75 IQRLGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKqGQGGRIINITSV-HEHTPLPGASaY 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 6320089   183 GASKGAMIGFHKCMsrhfrslSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK12743 154 TAAKHALGGLTKAM-------ALELVEHGILVNAVAPGAIATPM 190
PRK07831 PRK07831
SDR family oxidoreductase;
28-195 1.10e-06

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 48.88  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    28 PSYNP-SILSKNATALITGGS-SGLGFELAKELSRRINKVIVADI------QSFPTFA-QVEYNNIFYYQCDITSLDEIK 98
Cdd:PRK07831   6 PKYVPgHGLLAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIherrlgETADELAaELGLGRVEAVVCDVTSEAQVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    99 NLKKAIERDHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNRE-GFIINIASVLGELTPA 177
Cdd:PRK07831  86 ALIDAAVERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHgGVIVNNASVLGWRAQH 165

                        170
                 ....*....|....*...
gi 6320089   178 RLTSYGASKGAMIGFHKC 195
Cdd:PRK07831 166 GQAHYAAAKAGVMALTRC 183
PRK08177 PRK08177
SDR family oxidoreductase;
40-235 1.15e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 48.49  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVI--VADIQSFPTFAQVEYNNIfyYQCDITSLDEIKNLKKAI-ERDHGNINIIIN 116
Cdd:PRK08177   3 TALIIGASRGLGLGLVDRLLERGWQVTatVRGPQQDTALQALPGVHI--EKLDMNDPASLDQLLQRLqGQRFDLLFVNAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   117 NAGVAHiKKLEHMTNKEVEQLIDINLIGAYRIISTFAEdMIDNREGFIINIASVLGELT---PARLTSYGASKGA---MI 190
Cdd:PRK08177  81 ISGPAH-QSAADATAAEIGQLFLTNAIAPIRLARRLLG-QVRPGQGVLAFMSSQLGSVElpdGGEMPLYKASKAAlnsMT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 6320089   191 gfhkcmsrhfRSLSTECNKTGIKTLLVCPGKIKTNMF-----IDVPTPSK 235
Cdd:PRK08177 159 ----------RSFVAELGEPTLTVLSMHPGWVKTDMGgdnapLDVETSVK 198
PRK06947 PRK06947
SDR family oxidoreductase;
40-226 1.52e-06

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 48.65  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRR-----INkvIVADIQSFP-TFAQVEY--NNIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK06947   4 VVLITGASRGIGRATAVLAAARgwsvgIN--YARDAAAAEeTADAVRAagGRACVVAGDVANEADVIAMFDAVQSAFGRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAG-VAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNR---EGFIINIASVLGEL-TPARLTSYGASK 186
Cdd:PRK06947  82 DALVNNAGiVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrGGAIVNVSSIASRLgSPNEYVDYAGSK 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 6320089   187 GAM----IGFHKCMSRHfrslstecnktGIKTLLVCPGKIKTNM 226
Cdd:PRK06947 162 GAVdtltLGLAKELGPH-----------GVRVNAVRPGLIETEI 194
PRK06123 PRK06123
SDR family oxidoreductase;
41-226 1.68e-06

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 48.24  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQV------EYNNIFYYQCDITSLDEIKNLKKAIERDHGNINII 114
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVvqairrQGGEALAVAADVADEADVLRLFEAVDRELGRLDAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   115 INNAGVAHIK-KLEHMTNKEVEQLIDINLIGAY-------RIISTfaedMIDNREGFIINIASVLGEL-TPARLTSYGAS 185
Cdd:PRK06123  85 VNNAGILEAQmRLEQMDAARLTRIFATNVVGSFlcareavKRMST----RHGGRGGAIVNVSSMAARLgSPGEYIDYAAS 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 6320089   186 KGAM----IGfhkcmsrhfrsLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK06123 161 KGAIdtmtIG-----------LAKEVAAEGIRVNAVRPGVIYTEI 194
PRK09291 PRK09291
SDR family oxidoreductase;
40-224 1.97e-06

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 48.07  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIvADIQSFPtfaQVEYNNIFYYQCDiTSLDEIK-NLKKAIERDHGNINII---I 115
Cdd:PRK09291   4 TILITGAGSGFGREVALRLARKGHNVI-AGVQIAP---QVTALRAEAARRG-LALRVEKlDLTDAIDRAQAAEWDVdvlL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKc 195
Cdd:PRK09291  79 NNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEAIAE- 157

                        170       180
                 ....*....|....*....|....*....
gi 6320089   196 msrhfrSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK09291 158 ------AMHAELKPFGIQVATVNPGPYLT 180
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 40-224 3.35e-06

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 47.39  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQSfPTFAQV---EYN-NIFYYQCDITSLDEIKNL-KKAIERDHGNINII 114
Cdd:PRK08642   7 TVLVTGGSRGLGAAIARAFAREGARVVVNYHQS-EDAAEAladELGdRAIALQADVTDREQVQAMfATATEHFGKPITTV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   115 INNA-------GVAHiKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKG 187
Cdd:PRK08642  86 VNNAladfsfdGDAR-KKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHDYTTAKA 164

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6320089   188 AMIGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK08642 165 ALLGLT-------RNLAAELGPYGITVNMVSGGLLRT 194
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 41-224 4.56e-06

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: 47.15  E-value: 4.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVAD-----IQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:cd08934   6 ALVTGASSGIGEATARALAAEGAAVAIAArrvdrLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLDILV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFHKc 195
Cdd:cd08934  86 NNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSE- 164

                       170       180
                ....*....|....*....|....*....
gi 6320089  196 msrhfrSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:cd08934 165 ------GLRQEVTERGVRVVVIEPGTVDT 187
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
41-219 6.50e-06

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 47.53  E-value: 6.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADI-QSFPTFAQVEYNNIFYY---QCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:PRK08324 425 ALVTGAAGGIGKATAKRLAAEGACVVLADLdEEAAEAAAAELGGPDRAlgvACDVTDEAAVQAAFEEAALAFGGVDIVVS 504

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   117 NAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMID-NREGFIINIASVLGELTPARLTSYGASKGAMIgfHKC 195
Cdd:PRK08324 505 NAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAqGLGGSIVFIASKNAVNPGPNFGAYGAAKAAEL--HLV 582

                        170       180
                 ....*....|....*....|....
gi 6320089   196 msrhfRSLSTECNKTGIKTLLVCP 219
Cdd:PRK08324 583 -----RQLALELGPDGIRVNGVNP 601
PRK12742 PRK12742
SDR family oxidoreductase;
133-226 6.55e-06

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 46.29  E-value: 6.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   133 EVEQLIDINLIGAYRIISTFAEDMIDNreGFIINIASVLGELTP-ARLTSYGASKGAMIGFHKCMSRHFrslstecNKTG 211
Cdd:PRK12742  98 DIDRLFKINIHAPYHASVEAARQMPEG--GRIIIIGSVNGDRMPvAGMAAYAASKSALQGMARGLARDF-------GPRG 168

                         90
                 ....*....|....*
gi 6320089   212 IKTLLVCPGKIKTNM 226
Cdd:PRK12742 169 ITINVVQPGPIDTDA 183
PRK12744 PRK12744
SDR family oxidoreductase;
37-227 7.10e-06

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 46.66  E-value: 7.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYN---------NIFYYQCDITSLDEIKNLKKAIERD 107
Cdd:PRK12744   7 KGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEETvaavkaagaKAVAFQADLTTAAAVEKLFDDAKAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   108 HGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNreGFIINIA-SVLGELTPArLTSYGASK 186
Cdd:PRK12744  87 FGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDN--GKIVTLVtSLLGAFTPF-YSAYAGSK 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6320089   187 GAMigfhkcmsRHF-RSLSTECNKTGIKTLLVCPGKIKTNMF 227
Cdd:PRK12744 164 APV--------EHFtRAASKEFGARGISVTAVGPGPMDTPFF 197
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 39-222 9.36e-06

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: 46.12  E-value: 9.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   39 ATALITGGSSGLGFELAKELSRRINKVIV------ADIQsfPTFAQVE--YNNIFYYQCDITSLDEIKNLKKAIERDHGN 110
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVVhynrseAEAQ--RLKDELNalRNSAVLVQADLSDFAACADLVAAAFRAFGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  111 INIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:cd05357  79 CDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALE 158

                       170       180       190
                ....*....|....*....|....*....|..
gi 6320089  191 GFHkcmsrhfRSLSTECNKTgIKTLLVCPGKI 222
Cdd:cd05357 159 GLT-------RSAALELAPN-IRVNGIAPGLI 182
PRK06101 PRK06101
SDR family oxidoreductase;
38-224 9.80e-06

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 46.02  E-value: 9.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    38 NATALITGGSSGLGFELAKELSRRINKVIV-ADIQSFPTFAQVEYNNIFYYQCDITSLDEIknlKKAIERDHGNINIIIN 116
Cdd:PRK06101   1 MTAVLITGATSGIGKQLALDYAKQGWQVIAcGRNQSVLDELHTQSANIFTLAFDVTDHPGT---KAALSQLPFIPELWIF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   117 NAGvahikKLEHMTNKEVE-----QLIDINLIGAYRIISTFAEDMidNREGFIINIASVLGELTPARLTSYGASKGAMIG 191
Cdd:PRK06101  78 NAG-----DCEYMDDGKVDatlmaRVFNVNVLGVANCIEGIQPHL--SCGHRVVIVGSIASELALPRAEAYGASKAAVAY 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6320089   192 FHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK06101 151 FA-------RTLQLDLRPKGIEVVTVFPGFVAT 176
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
41-225 1.03e-05

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 46.02  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIVADI-QSFPTFAQVEY--NNIFYYQCDITSLDEIKNLKKAIERDHGNINIIINN 117
Cdd:PRK08993  13 AVVTGCDTGLGQGMALGLAEAGCDIVGINIvEPTETIEQVTAlgRRFLSLTADLRKIDGIPALLERAVAEFGHIDILVNN 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   118 AGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREG-FIINIASVLGELTPARLTSYGASKGAMIGFHkcm 196
Cdd:PRK08993  93 AGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGgKIINIASMLSFQGGIRVPSYTASKSGVMGVT--- 169

                        170       180
                 ....*....|....*....|....*....
gi 6320089   197 srhfRSLSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK08993 170 ----RLMANEWAKHNINVNAIAPGYMATN 194
PRK09186 PRK09186
flagellin modification protein A; Provisional
 37-225 1.33e-05

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 45.75  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADI-----QSFPTFAQVEYNN--IFYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:PRK09186   3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADIdkealNELLESLGKEFKSkkLSLVELDITDQESLEEFLSKSAEKYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   110 NINIIINNA---GVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPA-------RL 179
Cdd:PRK09186  83 KIDGAVNCAyprNKDYGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVAPKfeiyegtSM 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 6320089   180 TS---YGASKGAMIGFHKCMSRHFrslstecNKTGIKTLLVCPGKIKTN 225
Cdd:PRK09186 163 TSpveYAAIKAGIIHLTKYLAKYF-------KDSNIRVNCVSPGGILDN 204
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 41-224 1.53e-05

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: 45.60  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVAD----IQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:cd08937   7 VVVTGAAQGIGRGVAERLAGEGARVLLVDrselVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDVLIN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  117 NAGVAHIKK-LEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVL---GELTParltsYGASKGAMIGF 192
Cdd:cd08937  87 NVGGTIWAKpYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIAtrgIYRIP-----YSAAKGGVNAL 161

                       170       180       190
                ....*....|....*....|....*....|..
gi 6320089  193 HKCMSRhfrslstECNKTGIKTLLVCPGKIKT 224
Cdd:cd08937 162 TASLAF-------EHARDGIRVNAVAPGGTEA 186
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 41-194 2.50e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 45.00  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRRINKVIV-------------ADIQSFPTFAQveynnifYYQCDITSLDEIKNLKKAIERD 107
Cdd:PRK06198   9 ALVTGGTQGLGAAIARAFAERGAAGLVicgrnaekgeaqaAELEALGAKAV-------FVQADLSDVEDCRRVVAAADEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   108 HGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMI-DNREGFIINIASVLGELTPARLTSYGASK 186
Cdd:PRK06198  82 FGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRrRKAEGTIVNIGSMSAHGGQPFLAAYCASK 161


                 ....*...
gi 6320089   187 GAMIGFHK 194
Cdd:PRK06198 162 GALATLTR 169
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 21-224 3.08e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 44.64  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    21 PSVILSLPSYNPSILSKNATALITGGSSGLGFELAKELSRR-INKVIV-----ADIQSfpTFAQVEYNNIfyyQCDITSL 94
Cdd:PRK06701  29 PLPQFEAPNYKGSGKLKGKVALITGGDSGIGRAVAVLFAKEgADIAIVyldehEDANE--TKQRVEKEGV---KCLLIPG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    95 D--EIKNLKKAIER---DHGNINIIINNAGVA-HIKKLEHMTNKEVEQLIDINLIGAYRiistFAEDMIDN--REGFIIN 166
Cdd:PRK06701 104 DvsDEAFCKDAVEEtvrELGRLDILVNNAAFQyPQQSLEDITAEQLDKTFKTNIYSYFH----MTKAALPHlkQGSAIIN 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6320089   167 IASVLGELTPARLTSYGASKGAMIGFHkcmsrhfRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK06701 180 TGSITGYEGNETLIDYSATKGAIHAFT-------RSLAQSLVQKGIRVNAVAPGPIWT 230
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 41-226 4.36e-05

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 44.47  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRR-INKVIVA-----------DIQSfpTFAQVEYNNIFY-YQCDItslDE-IKNLKKAIE- 105
Cdd:PLN02780  56 ALVTGPTDGIGKGFAFQLARKgLNLVLVArnpdklkdvsdSIQS--KYSKTQIKTVVVdFSGDI---DEgVKRIKETIEg 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   106 RDHGninIIINNAGVAH-IKKLEHMTNKE-VEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPAR--LTS 181
Cdd:PLN02780 131 LDVG---VLINNVGVSYpYARFFHEVDEElLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSDplYAV 207

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 6320089   182 YGASKGAMIGFHKCmsrhfrsLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PLN02780 208 YAATKAYIDQFSRC-------LYVEYKKSGIDVQCQVPLYVATKM 245
PRK07102 PRK07102
SDR family oxidoreductase;
136-256 5.21e-05

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 43.76  E-value: 5.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   136 QLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFhkcmsrhfrsLSTECN---KTGI 212
Cdd:PRK07102 102 REFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKAALTAF----------LSGLRNrlfKSGV 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 6320089   213 KTLLVCPGKIKTNMFIDVPTPSKLLAPdiiPSQLALAIISAMEH 256
Cdd:PRK07102 172 HVLTVKPGFVRTPMTAGLKLPGPLTAQ---PEEVAKDIFRAIEK 212
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 40-239 5.29e-05

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: 43.99  E-value: 5.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVA--DIQSFPTFA-----QVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNIN 112
Cdd:cd09807   3 TVIITGANTGIGKETARELARRGARVIMAcrDMAKCEEAAaeirrDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDRLD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  113 IIINNAGVAhikKLEHMTNKE-VEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVL---GELTPARLTS------- 181
Cdd:cd09807  83 VLINNAGVM---RCPYSKTEDgFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAhkaGKINFDDLNSeksyntg 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  182 --YGASKGAMIGFHKCMSRHFRSlstecnkTGIKTLLVCPGKIKTNMFIDVPTPSKLLAP 239
Cdd:cd09807 160 faYCQSKLANVLFTRELARRLQG-------TGVTVNALHPGVVRTELGRHTGIHHLFLST 212
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
40-189 5.92e-05

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 43.81  E-value: 5.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYNNIFYYQCDITSLDEiknLKKAIER-D---Hgniniii 115
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFVRGDLRDPEA---LAAALAGvDavvH------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  116 nNAGVAHIkklehmTNKEVEQLIDINLIGAYRIIstfaEDMIDNREGFIINI--ASVLG-------ELTPAR-LTSYGAS 185
Cdd:COG0451  71 -LAAPAGV------GEEDPDETLEVNVEGTLNLL----EAARAAGVKRFVYAssSSVYGdgegpidEDTPLRpVSPYGAS 139


                ....
gi 6320089  186 KGAM 189
Cdd:COG0451 140 KLAA 143
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 40-200 6.89e-05

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: 43.53  E-value: 6.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELS----------RRINK---VIVADIQSFPTFAQveynnifYYQCDITSLDEIKNLKKAIER 106
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAaegfsvalaaRREAKleaLLVDIIRDAGGSAK-------AVPTDARDEDEVIALFDLIEE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  107 DHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFII---NIASVLGEltpARLTSYG 183
Cdd:cd05373  74 EIGPLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIftgATASLRGR---AGFAAFA 150

                       170
                ....*....|....*..
gi 6320089  184 ASKGAMIGFHKCMSRHF 200
Cdd:cd05373 151 GAKFALRALAQSMAREL 167
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 35-208 7.29e-05

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 43.90  E-value: 7.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   35 LSKNATALITGGSSGLGFELAKELSRRINKVIV--------ADIQS-FPTFAQVEYN--NIFYYQCDITSLDEIKNLKKA 103
Cdd:cd08953 202 LKPGGVYLVTGGAGGIGRALARALARRYGARLVllgrsplpPEEEWkAQTLAALEALgaRVLYISADVTDAAAVRRLLEK 281

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  104 IERDHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDnregFIINIASVLGELTPARLTSYG 183
Cdd:cd08953 282 VRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLD----FFVLFSSVSAFFGGAGQADYA 357

                       170       180
                ....*....|....*....|....*
gi 6320089  184 ASKGAMIGFhkcmSRHFRSLSTECN 208
Cdd:cd08953 358 AANAFLDAF----AAYLRQRGPQGR 378
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 40-226 1.05e-04

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: 42.85  E-value: 1.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIV----ADIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINIII 115
Cdd:cd08942   8 IVLVTGGSRGIGRMIAQGFLEAGARVIIsarkAEACADAAEELSAYGECIAIPADLSSEEGIEALVARVAERSDRLDVLV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  116 NNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDM----IDNREGFIINIASVLGELTPARLT-SYGASKGAMi 190
Cdd:cd08942  88 NNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLraaaTAENPARVINIGSIAGIVVSGLENySYGASKAAV- 166

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6320089  191 gfHKCMsrhfRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:cd08942 167 --HQLT----RKLAKELAGEHITVNAIAPGRFPSKM 196
PRK05693 PRK05693
SDR family oxidoreductase;
40-225 1.14e-04

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 42.86  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVA--DIQSFPTFAQVEYNNIfyyQCDITSLDEIKNLKKAIERDHGNINIIINN 117
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATarKAEDVEALAAAGFTAV---QLDVNDGAALARLAEELEAEHGGLDVLINN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   118 AGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNReGFIINIASVLGELTPARLTSYGASKGAMigfhkcms 197
Cdd:PRK05693  80 AGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSR-GLVVNIGSVSGVLVTPFAGAYCASKAAV-------- 150

                        170       180       190
                 ....*....|....*....|....*....|
gi 6320089   198 rHFRS--LSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK05693 151 -HALSdaLRLELAPFGVQVMEVQPGAIASQ 179
PRK06139 PRK06139
SDR family oxidoreductase;
36-192 1.15e-04

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 43.17  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    36 SKNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEynnifyyQC------------DITSLDEIKNLKKA 103
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAE-------ECralgaevlvvptDVTDADQVKALATQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   104 IERDHGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIG----AYRIISTFaedmIDNREGFIINIASVLGELTPARL 179
Cdd:PRK06139  78 AASFGGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGymrdAHAALPIF----KKQGHGIFINMISLGGFAAQPYA 153

                        170
                 ....*....|...
gi 6320089   180 TSYGASKGAMIGF 192
Cdd:PRK06139 154 AAYSASKFGLRGF 166
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 40-256 1.19e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 42.99  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIV------------ADIQSFPTFAqveynniFYYQCDITSLDEIKNLKKAIERD 107
Cdd:PRK07109  10 VVVITGASAGVGRATARAFARRGAKVVLlargeeglealaAEIRAAGGEA-------LAVVADVADAEAVQAAADRAEEE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   108 HGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAyrIISTFA--EDMIDNREGFIINIASVLGELTPARLTSYGAS 185
Cdd:PRK07109  83 LGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGV--VHGTLAalRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320089   186 KGAMIGFHKcmsrhfrSLSTEC--NKTGIKTLLVCPGKIKTnMFID-----VPTPSKLLAPDIIPSQLALAIISAMEH 256
Cdd:PRK07109 161 KHAIRGFTD-------SLRCELlhDGSPVSVTMVQPPAVNT-PQFDwarsrLPVEPQPVPPIYQPEVVADAILYAAEH 230
PRK05993 PRK05993
SDR family oxidoreductase;
35-225 1.36e-04

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 42.71  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    35 LSKNATALITGGSSGLGFELAKELSRRINKVIvADIQSFPTFAQVEYNNIFYYQCDITSLDEIKNL-KKAIERDHGNINI 113
Cdd:PRK05993   1 MDMKRSILITGCSSGIGAYCARALQSDGWRVF-ATCRKEEDVAALEAEGLEAFQLDYAEPESIAALvAQVLELSGGRLDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   114 IINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGeLTPARLT-SYGASKGAMIGF 192
Cdd:PRK05993  80 LFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILG-LVPMKYRgAYNASKFAIEGL 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6320089   193 HKCmsrhfrsLSTECNKTGIKTLLVCPGKIKTN 225
Cdd:PRK05993 159 SLT-------LRMELQGSGIHVSLIEPGPIETR 184
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 39-138 1.52e-04

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 41.78  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089     39 ATALITGGSSGLGFELAKELSRRINKVIV---------ADIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:pfam08659   1 GTYLITGGLGGLGRELARWLAERGARHLVllsrsaaprPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGP 80

                          90       100
                  ....*....|....*....|....*....
gi 6320089    110 NINIIINNAGVAHIKKLEHMTNKEVEQLI 138
Cdd:pfam08659  81 PIRGVIHAAGVLRDALLENMTDEDWRRVL 109
PRK07856 PRK07856
SDR family oxidoreductase;
37-196 1.54e-04

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 42.23  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVEYnniFYYQCDITSLDEIKNLKKAIERDHGNINIIIN 116
Cdd:PRK07856   5 TGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVDGRPA---EFHAADVRDPDQVAALVDAIVERHGRLDVLVN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   117 NAGVAHIKKLEHMTNKEVEQLIDINLIGAYrIISTFAEDMIDNRE--GFIINIASVLGeLTPARLTS-YGASKGAMIGFH 193
Cdd:PRK07856  82 NAGGSPYALAAEASPRFHEKIVELNLLAPL-LVAQAANAVMQQQPggGSIVNIGSVSG-RRPSPGTAaYGAAKAGLLNLT 159


                 ...
gi 6320089   194 KCM 196
Cdd:PRK07856 160 RSL 162
PRK12746 PRK12746
SDR family oxidoreductase;
41-226 2.10e-04

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 41.94  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    41 ALITGGSSGLGFELAKELSRriNKVIVA------DIQSFPTFAQVEYN--NIFYYQCDITSLDEIKNLKKAIERD----- 107
Cdd:PRK12746   9 ALVTGASRGIGRAIAMRLAN--DGALVAihygrnKQAADETIREIESNggKAFLIEADLNSIDGVKKLVEQLKNElqirv 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   108 -HGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMidNREGFIINIASVLGELTPARLTSYGASK 186
Cdd:PRK12746  87 gTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSIAYGLSK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6320089   187 GAMIGFHKCMSRHFrslstecNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK12746 165 GALNTMTLPLAKHL-------GERGITVNTIMPGYTKTDI 197
PRK09009 PRK09009
SDR family oxidoreductase;
42-105 2.33e-04

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 41.59  E-value: 2.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320089    42 LITGGSSGLGFELAKELSRRInkvivADIQSFPTF----AQVEYNNIFYYQCDITSLDEIKNLKKAIE 105
Cdd:PRK09009   4 LIVGGSGGIGKAMVKQLLERY-----PDATVHATYrhhkPDFQHDNVQWHALDVTDEAEIKQLSEQFT 66
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
136-230 2.35e-04

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 42.00  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   136 QLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMIGFhkcmsrhFRSLSTECNKTGIKTL 215
Cdd:PRK07904 113 QIAEINYTAAVSVGVLLGEKMRAQGFGQIIAMSSVAGERVRRSNFVYGSTKAGLDGF-------YLGLGEALREYGVRVL 185

                         90
                 ....*....|....*
gi 6320089   216 LVCPGKIKTNMFIDV 230
Cdd:PRK07904 186 VVRPGQVRTRMSAHA 200
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 40-192 2.72e-04

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: 42.12  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQ------VEYNNIFYYQCDITSLDEIKNLKKAIERDHGNINI 113
Cdd:cd09810   3 TVVITGASSGLGLAAAKALARRGEWHVVMACRDFLKAEQaaqevgMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  114 IINNAGVAHIK-KLEHMTNKEVEQLIDINLIGAYRIISTFAEDM--IDNREGFIINIASVLGEL-TPARLTSYGASKGAM 189
Cdd:cd09810  83 LVCNAAVYLPTaKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLqrSENASPRIVIVGSITHNPnTLAGNVPPRATLGDL 162


                ...
gi 6320089  190 IGF 192
Cdd:cd09810 163 EGL 165
PRK08219 PRK08219
SDR family oxidoreductase;
39-250 2.74e-04

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 41.46  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    39 ATALITGGSSGLGFELAKELSRRiNKVIVA--DIQSFPTFAQvEYNNIFYYQCDITSLDEIKNLKKAIER-D---Hgnin 112
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAPT-HTLLLGgrPAERLDELAA-ELPGATPFPVDLTDPEAIAAAVEQLGRlDvlvH---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   113 iiinNAGVAHIKKLEHMTNKEVEQLIDINLIGAyriistfAE------DMIDNREGFIINIASVLGELTPARLTSYGASK 186
Cdd:PRK08219  78 ----NAGVADLGPVAESTVDEWRATLEVNVVAP-------AEltrlllPALRAAHGHVVFINSGAGLRANPGWGSYAASK 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320089   187 GAMIGFHKcmsrhfrSLSTEcNKTGIKTLLVCPGKIKTNMFIDVPT-------PSKLLAPDIIPSQLALAI 250
Cdd:PRK08219 147 FALRALAD-------ALREE-EPGNVRVTSVHPGRTDTDMQRGLVAqeggeydPERYLRPETVAKAVRFAV 209
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 41-226 2.77e-04

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: 41.03  E-value: 2.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPtfaqveynnifyYQCDITSLDEIKNLKKAIER-DHgniniIINNAG 119
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGD------------YQVDITDEASIKALFEKVGHfDA-----IVSTAG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  120 VAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNreGFIINIASVLGELTPARLTSYGASKGAMIGFHKCMsrh 199
Cdd:cd11731  64 DAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLNDG--GSITLTSGILAQRPIPGGAAAATVNGALEGFVRAA--- 138

                       170       180
                ....*....|....*....|....*..
gi 6320089  200 frslSTECNKtGIKTLLVCPGKIKTNM 226
Cdd:cd11731 139 ----AIELPR-GIRINAVSPGVVEESL 160
PRK08628 PRK08628
SDR family oxidoreductase;
37-192 3.53e-04

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 41.48  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLG----FELAKElsRRINKVIVADIQSFPTFAQVEYNNI--FYYQCDITSLDEIKNLKKAIERDHGN 110
Cdd:PRK08628   6 KDKVVIVTGGASGIGaaisLRLAEE--GAIPVIFGRSAPDDEFAEELRALQPraEFVQVDLTDDAQCRDAVEQTVAKFGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   111 INIIINNAGVAHIKKLEHmTNKEVEQLIDINLIgAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMI 190
Cdd:PRK08628  84 IDGLVNNAGVNDGVGLEA-GREAFVASLERNLI-HYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSGYAAAKGAQL 161


                 ..
gi 6320089   191 GF 192
Cdd:PRK08628 162 AL 163
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 35-222 4.31e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 41.10  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    35 LSKNATALITGGSSGLGFELAKELSRR-INKVIVADIQSFPTFAQVEYNNI----FYYQCDITSLDEIKNL-KKAIERDH 108
Cdd:PRK07890   2 LLKGKVVVVSGVGPGLGRTLAVRAARAgADVVLAARTAERLDEVAAEIDDLgrraLAVPTDITDEDQCANLvALALERFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   109 GNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNReGFIINIASVLGELTPARLTSYGASKGA 188
Cdd:PRK07890  82 RVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHSQPKYGAYKMAKGA 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 6320089   189 MigfhKCMSrhfRSLSTECNKTGIKTLLVCPGKI 222
Cdd:PRK07890 161 L----LAAS---QSLATELGPQGIRVNSVAPGYI 187
PRK08340 PRK08340
SDR family oxidoreductase;
42-102 4.67e-04

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 40.94  E-value: 4.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320089    42 LITGGSSGLGFELAKELSRRINKVIVA--DIQSFPTFAQ--VEYNNIFYYQCDITSLDEIKNLKK 102
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISsrNEENLEKALKelKEYGEVYAVKADLSDKDDLKNLVK 68
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 37-226 5.07e-04

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 40.83  E-value: 5.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIV------ADIQSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERD--- 107
Cdd:PRK12747   3 KGKVALVTGASRGIGRAIAKRLANDGALVAIhygnrkEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNElqn 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   108 ---HGNINIIINNAGVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREgfIINIASVLGELTPARLTSYGA 184
Cdd:PRK12747  83 rtgSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSR--IINISSAATRISLPDFIAYSM 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6320089   185 SKGAmigfhkcMSRHFRSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK12747 161 TKGA-------INTMTFTLAKQLGARGITVNAILPGFIKTDM 195
PRK07774 PRK07774
SDR family oxidoreductase;
37-224 1.51e-03

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 39.34  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    37 KNATALITGGSSGLGFELAKELSRRINKVIVADI---QSFPTFAQV--EYNNIFYYQCDITSLDEIKNLKKAIERDHGNI 111
Cdd:PRK07774   5 DDKVAIVTGAAGGIGQAYAEALAREGASVVVADInaeGAERVAKQIvaDGGTAIAVQVDVSDPDSAKAMADATVSAFGGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   112 NIIINNAGVAHIKKLEHMTNKEV---EQLIDINLIGAYRIISTFAEDMIDNREGFIINIASvlgelTPARLTS--YGASK 186
Cdd:PRK07774  85 DYLVNNAAIYGGMKLDLLITVPWdyyKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSS-----TAAWLYSnfYGLAK 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6320089   187 GAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:PRK07774 160 VGLNGLTQ-------QLARELGGMNIRVNAIAPGPIDT 190
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 41-224 3.52e-03

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 38.20  E-value: 3.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQV------EYNNIFYYQCDITSLDEIKNLKKAIERD-HGNINI 113
Cdd:cd09763   6 ALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTaeeieaRGGKCIPVRCDHSDDDEVEALFERVAREqQGRLDI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  114 IINNAGVAHIKKLEHMTNK--EVEQLI--DINLIG--AYRIISTFAED-MIDNREGFIINIAS---VLGELTPArltsYG 183
Cdd:cd09763  86 LVNNAYAAVQLILVGVAKPfwEEPPTIwdDINNVGlrAHYACSVYAAPlMVKAGKGLIVIISStggLEYLFNVA----YG 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6320089  184 ASKGAmigfhkcMSRHFRSLSTECNKTGIKTLLVCPGKIKT 224
Cdd:cd09763 162 VGKAA-------IDRMAADMAHELKPHGVAVVSLWPGFVRT 195
PRK05717 PRK05717
SDR family oxidoreductase;
31-191 4.06e-03

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 37.95  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    31 NPSILSKNATALITGGSSGLGFELAKELSRRINKVIVADI--QSFPTFAQVEYNNIFYYQCDITSLDEIKNLKKAIERDH 108
Cdd:PRK05717   3 EPNPGHNGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLdrERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   109 GNINIIINNAGVA--HIKKLEHMTNKEVEQLIDINLIGAYrIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASK 186
Cdd:PRK05717  83 GRLDALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPM-LLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYAASK 161


                 ....*
gi 6320089   187 GAMIG 191
Cdd:PRK05717 162 GGLLA 166
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
40-68 5.76e-03

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


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 38.05  E-value: 5.76e-03
                        10        20
                ....*....|....*....|....*....
gi 6320089   40 TALITGGSSGLGFELAKELSRRINKVIVA 68
Cdd:COG5748   8 TVIITGASSGVGLYAAKALADRGWHVIMA 36
PRK08251 PRK08251
SDR family oxidoreductase;
42-226 6.80e-03

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 37.22  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    42 LITGGSSGLGFELAKEL----------SRRINKvivadIQSFPTFAQVEYNNI--FYYQCDITSLDEIKNLKKAIERDHG 109
Cdd:PRK08251   6 LITGASSGLGAGMAREFaakgrdlalcARRTDR-----LEELKAELLARYPGIkvAVAALDVNDHDQVFEVFAEFRDELG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   110 NINIIINNAGV---AHIKKLEHMTNKeveQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGEL-TPARLTSYGAS 185
Cdd:PRK08251  81 GLDRVIVNAGIgkgARLGTGKFWANK---ATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRgLPGVKAAYAAS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6320089   186 KGAMIGFHKcmsrhfrSLSTECNKTGIKTLLVCPGKIKTNM 226
Cdd:PRK08251 158 KAGVASLGE-------GLRAELAKTPIKVSTIEPGYIRSEM 191
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 40-234 8.90e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 37.09  E-value: 8.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089    40 TALITGGSSGLGFELAKELSRRINKVIVADIQSFPTFAQVE-------YNNIFYYQCDITSLDEIKNLKKAIERDHGNIN 112
Cdd:PRK05875   9 TYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEeiealkgAGAVRYEPADVTDEDQVARAVDAATAWHGRLH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   113 IIINNAGVAH-IKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASVLGELTPARLTSYGASKGAMig 191
Cdd:PRK05875  89 GVVHCAGGSEtIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKSAV-- 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6320089   192 fhkcmsRHFRSLST-ECNKTGIKTLLVCPGKIKTNM---FIDVPTPS 234
Cdd:PRK05875 167 ------DHLMKLAAdELGPSWVRVNSIRPGLIRTDLvapITESPELS 207
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 41-253 9.55e-03

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: 36.73  E-value: 9.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089   41 ALITGGSSGLGFELAKELSRRINKVIVA--DIQSFPTFAQVEYNNIFyyQCDITSLDEIknlkKAIERDHGNINIIINNA 118
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSgrDAGALAGLAAEVGALAR--PADVAAELEV----WALAQELGPLDLLVYAA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320089  119 GVAHIKKLEHMTNKEVEQLIDINLIGAYRIISTFAEDMIDNREGFIINIASvlgELTPAR-LTSYGASKGAMIGFHKCMS 197
Cdd:cd11730  75 GAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYP---ELVMLPgLSAYAAAKAALEAYVEVAR 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6320089  198 RHFRslstecnktGIKTLLVCPGKIKTNMFIDVPTPSK-LLAPDiipsQLALAIISA 253
Cdd:cd11730 152 KEVR---------GLRLTLVRPPAVDTGLWAPPGRLPKgALSPE----DVAAAILEA 195
 
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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