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Conserved domains on  [gi|15239681|ref|NP_197421|]
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NAD(P)-binding Rossmann-fold superfamily protein [Arabidopsis thaliana]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10172393)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to 3-ketodihydrosphingosine reductase (KDSR) that catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS); classical SDRs have an TGXXX[AG]XG 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
SCOP:  4000029

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
38-271 2.14e-99

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: 293.00  E-value: 2.14e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQ---LATGVEVATFSADVRDYDAVSKAIDES----G 110
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEaeaNASGQKVSYISADLSDYEEVEQAFAQAvekgG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 111 PIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRgpaSISLVSSQAGQAGIYGYTAYSASK 190
Cdd:cd08939  82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPG---HIVFVSSQAALVGIYGYSAYCPSK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 191 FGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSIIAASSGSMKTNEVAKICFDGIKAGKFTVTCHFI 270
Cdd:cd08939 159 FALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENKTKPEETKAIEGSSGPITPEEAARIIVKGLDRGYDDVFTDFI 238

                .
gi 15239681 271 G 271
Cdd:cd08939 239 G 239
 
Name Accession Description Interval E-value
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
38-271 2.14e-99

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: 293.00  E-value: 2.14e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQ---LATGVEVATFSADVRDYDAVSKAIDES----G 110
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEaeaNASGQKVSYISADLSDYEEVEQAFAQAvekgG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 111 PIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRgpaSISLVSSQAGQAGIYGYTAYSASK 190
Cdd:cd08939  82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPG---HIVFVSSQAALVGIYGYSAYCPSK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 191 FGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSIIAASSGSMKTNEVAKICFDGIKAGKFTVTCHFI 270
Cdd:cd08939 159 FALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENKTKPEETKAIEGSSGPITPEEAARIIVKGLDRGYDDVFTDFI 238

                .
gi 15239681 271 G 271
Cdd:cd08939 239 G 239
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
35-296 1.74e-62

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 198.94  E-value: 1.74e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAIDE----SG 110
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELR-AAGARVEVVALDVTDPDAVAALAEAvlarFG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 111 PIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASK 190
Cdd:COG0300  82 PIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRAR-GRG--RIVNVSSVAGLRGLPGMAAYAASK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 191 FGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQelkkrpeltSIIAASSGSMKTNEVAKICFDGIKAGKFTVtchFI 270
Cdd:COG0300 159 AALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTAR---------AGAPAGRPLLSPEEVARAILRALERGRAEV---YV 226
                       250       260
                ....*....|....*....|....*.
gi 15239681 271 GFLLSIASTGMSPQGSFWLALTEVMF 296
Cdd:COG0300 227 GWDARLLARLLRLLPRLFDRLLRRAL 252
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
38-222 7.10e-53

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 172.41  E-value: 7.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681    38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYD----AVSKAIDESGPID 113
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELG-ALGGKALFIQGDVTDRAqvkaLVEQAVERLGRLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:pfam00106  80 ILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSG---GRIVNISSVAGLVPYPGGSAYSASKAAV 156
                         170       180
                  ....*....|....*....|....*....
gi 15239681   194 QGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTD 185
PRK07326 PRK07326
SDR family oxidoreductase;
40-233 6.58e-45

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 153.24  E-value: 6.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiQLATGVEVATFSADVRDYDAVSKAID----ESGPIDVL 115
Cdd:PRK07326   9 ALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAA--ELNNKGNVLGLAADVRDEADVQRAVDaivaAFGGLDVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpaSISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK07326  87 IANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGG----YIINISSLAGTNFFAGGAAYNASKFGLVG 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15239681  196 LAQALQQEVISDGIHVTLLFPPDTDT------PGFEQELKKRPE 233
Cdd:PRK07326 163 FSEAAMLDLRQYGIKVSTIMPGSVAThfnghtPSEKDAWKIQPE 206
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
40-188 4.21e-09

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 55.18  E-value: 4.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681     40 VFITGGSSGIGLALAHRAVSEGA-KVSILARSTEKLAEAKRSIQL--ATGVEVATFSADVRDYDAVSKAIDE----SGPI 112
Cdd:smart00822   3 YLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAEleAAGARVTVVACDVADRDALAAVLAAipavEGPL 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239681    113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALpamkareGRGPASISLVSSQAGQAGIYGYTAYSA 188
Cdd:smart00822  83 TGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTA-------DLPLDFFVLFSSIAGVLGSPGQANYAA 151
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
42-268 7.49e-05

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 43.75  E-value: 7.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681    42 ITGGSSGIGLA----LAHRAVSEGAKVSILARSTEKLAEAKRSIQLAT-GVEVATFSADV---RDYDAVSKAIDESGPID 113
Cdd:TIGR01500   5 VTGASRGFGRTiaqeLAKCLKSPGSVLVLSARNDEALRQLKAEIGAERsGLRVVRVSLDLgaeAGLEQLLKALRELPRPK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   114 -----VLIVNQGVF--IGK-ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRgPASISLVSSQAGQAGIYGYTA 185
Cdd:TIGR01500  85 glqrlLLINNAGTLgdVSKgFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGL-NRTVVNISSLCAIQPFKGWAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   186 YSASKFGLQGLAQALQQEVISDGIHVtLLFPP---DTDTPGFEQELKKRPELTSIIAA--SSGSMKT-NEVAKICFDGIK 259
Cdd:TIGR01500 164 YCAGKAARDMLFQVLALEEKNPNVRV-LNYAPgvlDTDMQQQVREESVDPDMRKGLQElkAKGKLVDpKVSAQKLLSLLE 242

                  ....*....
gi 15239681   260 AGKFTVTCH 268
Cdd:TIGR01500 243 KDKFKSGAH 251
 
Name Accession Description Interval E-value
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
38-271 2.14e-99

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: 293.00  E-value: 2.14e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQ---LATGVEVATFSADVRDYDAVSKAIDES----G 110
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEaeaNASGQKVSYISADLSDYEEVEQAFAQAvekgG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 111 PIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRgpaSISLVSSQAGQAGIYGYTAYSASK 190
Cdd:cd08939  82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPG---HIVFVSSQAALVGIYGYSAYCPSK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 191 FGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSIIAASSGSMKTNEVAKICFDGIKAGKFTVTCHFI 270
Cdd:cd08939 159 FALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENKTKPEETKAIEGSSGPITPEEAARIIVKGLDRGYDDVFTDFI 238

                .
gi 15239681 271 G 271
Cdd:cd08939 239 G 239
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
35-296 1.74e-62

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 198.94  E-value: 1.74e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAIDE----SG 110
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELR-AAGARVEVVALDVTDPDAVAALAEAvlarFG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 111 PIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASK 190
Cdd:COG0300  82 PIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRAR-GRG--RIVNVSSVAGLRGLPGMAAYAASK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 191 FGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQelkkrpeltSIIAASSGSMKTNEVAKICFDGIKAGKFTVtchFI 270
Cdd:COG0300 159 AALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTAR---------AGAPAGRPLLSPEEVARAILRALERGRAEV---YV 226
                       250       260
                ....*....|....*....|....*.
gi 15239681 271 GFLLSIASTGMSPQGSFWLALTEVMF 296
Cdd:COG0300 227 GWDARLLARLLRLLPRLFDRLLRRAL 252
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
38-253 7.90e-58

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: 186.54  E-value: 7.90e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqlatGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:COG4221   6 KVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL----GGRALAVPLDVTDEAAVEAAVAaavaEFGRLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:COG4221  82 VLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRAR-GSG--HIVNISSIAGLRPYPGGAVYAATKAAV 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSIIAASSGSMKTNEVAKI 253
Cdd:COG4221 159 RGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPLTPEDVAEA 218
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
38-226 1.34e-53

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: 176.13  E-value: 1.34e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:COG1028   7 KVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELR-AAGGRALAVAADVTDEAAVEALVAaavaAFGRLD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:COG1028  86 ILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGG---GRIVNISSIAGLRGSPGQAAYAASKAAV 162
                       170       180       190
                ....*....|....*....|....*....|...
gi 15239681 194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQ 226
Cdd:COG1028 163 VGLTRSLALELAPRGIRVNAVAPGPIDTPMTRA 195
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
38-222 7.10e-53

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 172.41  E-value: 7.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681    38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYD----AVSKAIDESGPID 113
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELG-ALGGKALFIQGDVTDRAqvkaLVEQAVERLGRLD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:pfam00106  80 ILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSG---GRIVNISSVAGLVPYPGGSAYSASKAAV 156
                         170       180
                  ....*....|....*....|....*....
gi 15239681   194 QGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTD 185
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
40-284 2.27e-52

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: 172.47  E-value: 2.27e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLatGVEVATFSADVRDYDAVSKAIDE----SGPIDVL 115
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEAL--GGNAVAVQADVSDEEDVEALVEEaleeFGRLDIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd05233  79 VNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGG---GRIVNISSVAGLRPLPGQAAYAASKAALEG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 196 LAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSIIAASSGSMKT-NEVAkicfdgikagkftvtcHFIGFLL 274
Cdd:cd05233 156 LTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGRLGTpEEVA----------------EAVVFLA 219
                       250
                ....*....|
gi 15239681 275 SIASTGMSPQ 284
Cdd:cd05233 220 SDEASYITGQ 229
PRK07326 PRK07326
SDR family oxidoreductase;
40-233 6.58e-45

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 153.24  E-value: 6.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiQLATGVEVATFSADVRDYDAVSKAID----ESGPIDVL 115
Cdd:PRK07326   9 ALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAA--ELNNKGNVLGLAADVRDEADVQRAVDaivaAFGGLDVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpaSISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK07326  87 IANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGG----YIINISSLAGTNFFAGGAAYNASKFGLVG 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15239681  196 LAQALQQEVISDGIHVTLLFPPDTDT------PGFEQELKKRPE 233
Cdd:PRK07326 163 FSEAAMLDLRQYGIKVSTIMPGSVAThfnghtPSEKDAWKIQPE 206
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
38-211 2.83e-44

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 151.85  E-value: 2.83e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:PRK05653   6 KTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELR-AAGGEARVLVFDVSDEAAVRALIEaaveAFGALD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK05653  85 ILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKA-RYG--RIVNISSVSGVTGNPGQTNYSAAKAGV 161
                        170
                 ....*....|....*...
gi 15239681  194 QGLAQALQQEVISDGIHV 211
Cdd:PRK05653 162 IGFTKALALELASRGITV 179
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
38-237 3.24e-43

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 149.25  E-value: 3.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARST-EKLAEAKRSIQlATGVEVATFSADVRD----YDAVSKAIDESGPI 112
Cdd:PRK12825   7 RVALVTGAARGLGRAIALRLARAGADVVVHYRSDeEAAEELVEAVE-ALGRRAQAVQADVTDkaalEAAVAAAVERFGRI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAM-KAREGRgpasISLVSSQAGQAGIYGYTAYSASKF 191
Cdd:PRK12825  86 DILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMrKQRGGR----IVNISSVAGLPGWPGRSNYAAAKA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15239681  192 GLQGLAQALQQEVISDGIHVTLLFPPDTDTP----GFEQELKKRPELTSI 237
Cdd:PRK12825 162 GLVGLTKALARELAEYGITVNMVAPGDIDTDmkeaTIEEAREAKDAETPL 211
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
40-225 4.49e-41

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: 143.29  E-value: 4.49e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSK----AIDESGPIDVL 115
Cdd:cd05360   3 VVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVR-ELGGEAIAVVADVADAAQVERaadtAVERFGRIDTW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd05360  82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRR---RGGGALINVGSLLGYRSAPLQAAYSASKHAVRG 158
                       170       180       190
                ....*....|....*....|....*....|..
gi 15239681 196 LAQALQQEVISDG--IHVTLLFPPDTDTPGFE 225
Cdd:cd05360 159 FTESLRAELAHDGapISVTLVQPTAMNTPFFG 190
PRK07109 PRK07109
short chain dehydrogenase; Provisional
34-225 1.30e-40

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 144.68  E-value: 1.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   34 PIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAV----SKAIDES 109
Cdd:PRK07109   5 PIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIR-AAGGEALAVVADVADAEAVqaaaDRAEEEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  110 GPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSAS 189
Cdd:PRK07109  84 GPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPR-DRG--AIIQVGSALAYRSIPLQSAYCAA 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15239681  190 KFGLQGLAQALQQEVISDG--IHVTLLFPPDTDTPGFE 225
Cdd:PRK07109 161 KHAIRGFTDSLRCELLHDGspVSVTMVQPPAVNTPQFD 198
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
40-211 1.93e-39

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 139.17  E-value: 1.93e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK05557   8 ALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAkaefGGVDIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAM-KAREGRgpasISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:PRK05557  88 VNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMmKQRSGR----IINISSVVGLMGNPGQANYAASKAGVI 163
                        170
                 ....*....|....*..
gi 15239681  195 GLAQALQQEVISDGIHV 211
Cdd:PRK05557 164 GFTKSLARELASRGITV 180
PRK12826 PRK12826
SDR family oxidoreductase;
38-228 2.75e-39

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 138.90  E-value: 2.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDA----VSKAIDESGPID 113
Cdd:PRK12826   7 RVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVE-AAGGKARARQVDVRDRAAlkaaVAAGVEDFGRLD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaREGRGpaSISLVSSQAG-QAGIYGYTAYSASKFG 192
Cdd:PRK12826  86 ILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALI-RAGGG--RIVLTSSVAGpRVGYPGLAHYAASKAG 162
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQEL 228
Cdd:PRK12826 163 LVGFTRALALELAARNITVNSVHPGGVDTPMAGNLG 198
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
35-216 1.65e-38

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 136.74  E-value: 1.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAI----DESG 110
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVE-AYGVKVVIATADVSDYEEVTAAIeqlkNELG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  111 PIDVLIVNQGVF-IGKELEkQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSAS 189
Cdd:PRK07666  84 SIDILINNAGISkFGKFLE-LDPAEWEKIIQVNLMGVYYATRAVLPSMIERQS---GDIINISSTAGQKGAAVTSAYSAS 159
                        170       180
                 ....*....|....*....|....*..
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK07666 160 KFGVLGLTESLMQEVRKHNIRVTALTP 186
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
38-261 1.42e-36

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 130.95  E-value: 1.42e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlatGVEVATFSA-DVRDYDAVSKAI-DESGPIDVL 115
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGG---DVEAVPYDArDPEDARALVDALrDRFGRIDVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd08932  78 VHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALR-EAGSG--RVVFLNSLSGKRVLAGNAGYSASKFALRA 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239681 196 LAQALQQEVISDGIHVTLLFPPDTDTPGFEQElkkrpelTSIIAASSGSMKT-NEVAKICFDGIKAG 261
Cdd:cd08932 155 LAHALRQEGWDHGVRVSAVCPGFVDTPMAQGL-------TLVGAFPPEEMIQpKDIANLVRMVIELP 214
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
40-211 2.00e-36

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: 131.13  E-value: 2.00e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVS----KAIDESGPIDVL 115
Cdd:cd05333   3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIK-ALGGNAAALEADVSDREAVEalveKVEAEFGPVDIL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAM-KAREGRgpasISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:cd05333  82 VNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMiKRRSGR----IINISSVVGLIGNPGQANYAASKAGVI 157
                       170
                ....*....|....*..
gi 15239681 195 GLAQALQQEVISDGIHV 211
Cdd:cd05333 158 GFTKSLAKELASRGITV 174
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
39-279 1.38e-35

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: 129.28  E-value: 1.38e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  39 HVFITGGSSGIGLALAHRAVSEGAKVSILARsTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAID----ESGPIDV 114
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDI-NEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKkikkEVGDVTI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREgRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:cd05339  80 LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERN-HG--HIVTIASVAGLISPAGLADYCASKAAAV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 195 GLAQALQQEVIS---DGIHVTLLFPPDTDTPGFEQELKKRPELTSIIaassgsmKTNEVAKICFDGI-KAGKFTVTCHFI 270
Cdd:cd05339 157 GFHESLRLELKAygkPGIKTTLVCPYFINTGMFQGVKTPRPLLAPIL-------EPEYVAEKIVRAIlTNQQMLYLPFYA 229

                ....*....
gi 15239681 271 GFLLSIAST 279
Cdd:cd05339 230 YFLPILKRT 238
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
40-266 1.42e-35

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: 128.99  E-value: 1.42e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSI-QLATGVEVATFsaDVRDYDAVSKAI----DESGPIDV 114
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELlNPNPSVEVEIL--DVTDEERNQLVIaeleAELGGLDL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:cd05350  79 VIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAK-GRG--HLVLISSVAALRGLPGAAAYSASKAALS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239681 195 GLAQALQQEVISDGIHVTLLFPPDTDTPgfeqelkkrpeLTSIIAASSGSMKTNEVAKICFDGIKAGKFTVT 266
Cdd:cd05350 156 SLAESLRYDVKKRGIRVTVINPGFIDTP-----------LTANMFTMPFLMSVEQAAKRIYKAIKKGAAEPT 216
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
40-216 4.15e-35

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: 128.12  E-value: 4.15e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiqlATGVEVATFSADVRDYDAVSKAIDE----SGPIDVL 115
Cdd:cd05374   3 VLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGE----LLNDNLEVLELDVTDEESIKAAVKEvierFGRIDVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAM-KAREGRgpasISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:cd05374  79 VNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMrKQGSGR----IVNVSSVAGLVPTPFLGPYCASKAALE 154
                       170       180
                ....*....|....*....|..
gi 15239681 195 GLAQALQQEVISDGIHVTLLFP 216
Cdd:cd05374 155 ALSESLRLELAPFGIKVTIIEP 176
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
40-221 8.87e-35

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 127.32  E-value: 8.87e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDY----DAVSKAIDESGPIDVL 115
Cdd:cd05332   6 VIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDMSDLedaeQVVEEALKLFGGLDIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd05332  86 INNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIER-SQG--SIVVVSSIAGKIGVPFRTAYAASKHALQG 162
                       170       180
                ....*....|....*....|....*.
gi 15239681 196 LAQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:cd05332 163 FFDSLRAELSEPNISVTVVCPGLIDT 188
PRK12829 PRK12829
short chain dehydrogenase; Provisional
38-253 1.17e-34

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 127.10  E-value: 1.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiqLATGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:PRK12829  12 LRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAA---RLPGAKVTATVADVADPAQVERVFDtaveRFGGLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKE-LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGPASISLvSSQAGQAGIYGYTAYSASKFG 192
Cdd:PRK12829  89 VLVNNAGIAGPTGgIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKAS-GHGGVIIAL-SSVAGRLGYPGRTPYAASKWA 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSIIAAssgSMKTNEVAKI 253
Cdd:PRK12829 167 VVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLGIGLD---EMEQEYLEKI 224
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
40-221 1.88e-34

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: 125.70  E-value: 1.88e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiqlATGVEVATFSADVRDYDAVSKAID----ESGPIDVL 115
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAA----QELEGVLGLAGDVRDEADVRRAVDameeAFGGLDAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd08929  79 VNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGG---GTIVNVGSLAGKNAFKGGAAYNASKFGLLG 155
                       170       180
                ....*....|....*....|....*.
gi 15239681 196 LAQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:cd08929 156 LSEAAMLDLREANIRVVNVMPGSVDT 181
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
41-222 7.96e-34

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: 124.57  E-value: 7.96e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  41 FITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDY----DAVSKAIDESGPIDVLI 116
Cdd:cd08934   7 LVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELE-AEGGKALVLELDVTDEqqvdAAVERTVEALGRLDILV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 117 VNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:cd08934  86 NNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNK---GTIVNISSVAGRVAVRNSAVYNATKFGVNAF 162
                       170       180
                ....*....|....*....|....*.
gi 15239681 197 AQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:cd08934 163 SEGLRQEVTERGVRVVVIEPGTVDTE 188
PRK06180 PRK06180
short chain dehydrogenase; Provisional
41-216 8.00e-34

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 125.41  E-value: 8.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAE-AKRSIQLATGVEVatfsaDVRDYDA----VSKAIDESGPIDVL 115
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADfEALHPDRALARLL-----DVTDFDAidavVADAEATFGPIDVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGvfIGKE--LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK06180  83 VNNAG--YGHEgaIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRAR-RRG--HIVNITSMGGLITMPGIGYYCGSKFAL 157
                        170       180
                 ....*....|....*....|...
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK06180 158 EGISESLAKEVAPFGIHVTAVEP 180
PRK05872 PRK05872
short chain dehydrogenase; Provisional
38-222 2.35e-33

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 124.70  E-value: 2.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSiqLATGVEVATFSADVRDYDAVSKAIDES----GPID 113
Cdd:PRK05872  10 KVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAE--LGGDDRVLTVVADVTDLAAMQAAAEEAverfGGID 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRgpasISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK05872  88 VVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGY----VLQVSSLAAFAAAPGMAAYCASKAGV 163
                        170       180
                 ....*....|....*....|....*....
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK05872 164 EAFANALRLEVAHHGVTVGSAYLSWIDTD 192
PRK06181 PRK06181
SDR family oxidoreductase;
40-258 6.07e-33

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 122.78  E-value: 6.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK06181   4 VIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELA-DHGGEALVVPTDVSDAEACERLIEAAvarfGGIDIL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEV--KFMiDVNLTGSFNVIKAALPAMKAREGRgpasISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK06181  83 VNNAGITMWSRFDELTDLSVfeRVM-RVNYLGAVYCTHAALPHLKASRGQ----IVVVSSLAGLTGVPTRSGYAASKHAL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDTpgfeqELKKR-------PELTSIIaASSGSMKTNEVAKICFDGI 258
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVAT-----DIRKRaldgdgkPLGKSPM-QESKIMSAEECAEAILPAI 223
PRK09072 PRK09072
SDR family oxidoreductase;
40-221 1.23e-32

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 121.97  E-value: 1.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVatFSADVRDYD---AVSKAIDESGPIDVLI 116
Cdd:PRK09072   8 VLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHRW--VVADLTSEAgreAVLARAREMGGINVLI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  117 VNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKARegrGPASISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:PRK09072  86 NNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQ---PSAMVVNVGSTFGSIGYPGYASYCASKFALRGF 162
                        170       180
                 ....*....|....*....|....*
gi 15239681  197 AQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK09072 163 SEALRRELADTGVRVLYLAPRATRT 187
PRK08267 PRK08267
SDR family oxidoreductase;
40-222 1.80e-32

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 121.20  E-value: 1.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqlaTGVEVATFSADVRDYDAVSKAIDE-----SGPIDV 114
Cdd:PRK08267   4 IFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAEL---GAGNAWTGALDVTDRAAWDAALADfaaatGGRLDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREgrGPASISLVSSQA--GQAGIygyTAYSASKFG 192
Cdd:PRK08267  81 LFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATP--GARVINTSSASAiyGQPGL---AVYSATKFA 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK08267 156 VRGLTEALDLEWRRHGIRVADVMPLFVDTA 185
PRK07454 PRK07454
SDR family oxidoreductase;
38-227 5.52e-32

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 119.68  E-value: 5.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAIDES----GPID 113
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELR-STGVKAAAYSIDLSNPEAIAPGIAELleqfGCPD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK07454  86 VLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGG---GLIINVSSIAARNAFPQWGAYCVSKAAL 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQE 227
Cdd:PRK07454 163 AAFTKCLAEEERSHGIRVCTITLGAVNTPLWDTE 196
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
38-225 8.54e-32

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: 119.23  E-value: 8.54e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDES----GPID 113
Cdd:cd05369   4 KVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETlkefGKID 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVN-QGVFIGKeLEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKarEGRGPASI-SLVSSQAGQAGiyGYTAYS-ASK 190
Cdd:cd05369  84 ILINNaAGNFLAP-AESLSPNGFKTVIDIDLNGTFNTTKAVGKRLI--EAKHGGSIlNISATYAYTGS--PFQVHSaAAK 158
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15239681 191 FGLQGLAQALQQEVISDGIHVTLLFP-PDTDTPGFE 225
Cdd:cd05369 159 AGVDALTRSLAVEWGPYGIRVNAIAPgPIPTTEGME 194
PRK12827 PRK12827
short chain dehydrogenase; Provisional
38-226 2.14e-31

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 118.28  E-value: 2.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSIL---ARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAID----ESG 110
Cdd:PRK12827   7 RRVLITGGSGGLGRAIAVRLAADGADVIVLdihPMRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDagveEFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  111 PIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAreGRGPASISLVSSQAGQAGIYGYTAYSASK 190
Cdd:PRK12827  87 RLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIR--ARRGGRIVNIASVAGVRGNRGQVNYAASK 164
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15239681  191 FGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQ 226
Cdd:PRK12827 165 AGLIGLTKTLANELAPRGITVNAVAPGAINTPMADN 200
PRK07832 PRK07832
SDR family oxidoreductase;
40-222 1.17e-30

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 117.07  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDE----SGPIDVL 115
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRALDISDYDAVAAFAADihaaHGSMDVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGpASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK07832  83 MNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPM-VAAGRG-GHLVNVSSAAGLVALPWHAAYSASKFGLRG 160
                        170       180
                 ....*....|....*....|....*..
gi 15239681  196 LAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK07832 161 LSEVLRFDLARHGIGVSVVVPGAVKTP 187
PRK07825 PRK07825
short chain dehydrogenase; Provisional
33-290 1.19e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 116.96  E-value: 1.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   33 IPIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVatfsaDVRDYDA----VSKAIDE 108
Cdd:PRK07825   1 DDLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVVGGPL-----DVTDPASfaafLDAVEAD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  109 SGPIDVLIVNQGVF-IGKELEkQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYS 187
Cdd:PRK07825  76 LGPIDVLVNNAGVMpVGPFLD-EPDAVTRRILDVNVYGVILGSKLAAPRMVPR-GRG--HVVNVASLAGKIPVPGMATYC 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  188 ASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTpgfeqelkkrpELTSIIAAsSGSMKTNE---VAKICFDGIKAGKFT 264
Cdd:PRK07825 152 ASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNT-----------ELIAGTGG-AKGFKNVEpedVAAAIVGTVAKPRPE 219
                        250       260
                 ....*....|....*....|....*..
gi 15239681  265 VTC-HFIGFLLSIAsTGMSPQGSFWLA 290
Cdd:PRK07825 220 VRVpRALGPLAQAQ-RLLPRRVREALN 245
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
42-241 1.93e-30

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 115.63  E-value: 1.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDY----DAVSKAIDESGPIDVLIV 117
Cdd:PRK12824   7 VTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTeecaEALAEIEEEEGPVDILVN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:PRK12824  87 NAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCE---QGYGRIINISSVNGLKGQFGQTNYSAAKAGMIGFT 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15239681  198 QALQQEVISDGIHVTLLFPPDTDTPGFEQelkKRPELTSIIAAS 241
Cdd:PRK12824 164 KALASEGARYGITVNCIAPGYIATPMVEQ---MGPEVLQSIVNQ 204
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
39-216 3.76e-30

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: 115.07  E-value: 3.76e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  39 HVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAI----DESGPIDV 114
Cdd:cd05346   2 TVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDVSDRESIEAALenlpEEFRDIDI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQGVFIGKE-LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:cd05346  82 LVNNAGLALGLDpAQEADLEDWETMIDTNVKGLLNVTRLILPIMIA---RNQGHIINLGSIAGRYPYAGGNVYCATKAAV 158
                       170       180
                ....*....|....*....|...
gi 15239681 194 QGLAQALQQEVISDGIHVTLLFP 216
Cdd:cd05346 159 RQFSLNLRKDLIGTGIRVTNIEP 181
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
32-230 8.31e-30

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: 113.97  E-value: 8.31e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  32 TIPIKFRHVFITGGSSGIGLALAhRAVSE-GAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDES- 109
Cdd:cd05352   3 LFSLKGKVAIVTGGSRGIGLAIA-RALAEaGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIq 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 110 ---GPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAG--------QA 178
Cdd:cd05352  82 kdfGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQ-GKG--SLIITASMSGtivnrpqpQA 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15239681 179 giygytAYSASKFGLQGLAQALQQEVISDGIHVTLLFPP--DTDTPGF-EQELKK 230
Cdd:cd05352 159 ------AYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGyiDTDLTDFvDKELRK 207
PRK07576 PRK07576
short chain dehydrogenase; Provisional
38-241 1.01e-29

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 114.28  E-value: 1.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAI----DESGPID 113
Cdd:PRK07576  10 KNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQ-QAGPEGLGVSADVRDYAAVEAAFaqiaDEFGPID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVN-QGVFIGkELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpasiSLVSSQAGQAGI-YGYTAY-SASK 190
Cdd:PRK07576  89 VLVSGaAGNFPA-PAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGA------SIIQISAPQAFVpMPMQAHvCAAK 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15239681  191 FGLQGLAQALQQEVISDGIHVTLLFP-PDTDTPGFEQeLKKRPELTSIIAAS 241
Cdd:PRK07576 162 AGVDMLTRTLALEWGPEGIRVNSIVPgPIAGTEGMAR-LAPSPELQAAVAQS 212
PRK08219 PRK08219
SDR family oxidoreductase;
42-222 6.05e-29

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 111.18  E-value: 6.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAhRAVSEGAKVSILARSTEKLAEakrsiqLATGVEVAT-FSADVRDYDAVSKAIDESGPIDVLIVNQG 120
Cdd:PRK08219   8 ITGASRGIGAAIA-RELAPTHTLLLGGRPAERLDE------LAAELPGATpFPVDLTDPEAIAAAVEQLGRLDVLVHNAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  121 VFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpaSISLVSSQAGQAGIYGYTAYSASKFGLQGLAQAL 200
Cdd:PRK08219  81 VADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHG----HVVFINSGAGLRANPGWGSYAASKFALRALADAL 156
                        170       180
                 ....*....|....*....|..
gi 15239681  201 QQEViSDGIHVTLLFPPDTDTP 222
Cdd:PRK08219 157 REEE-PGNVRVTSVHPGRTDTD 177
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
35-262 1.92e-28

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: 109.70  E-value: 1.92e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKrsiqlATGVEVATFSADVRDYDAVSKAIDE---SGP 111
Cdd:cd05370   3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAK-----KELPNIHTIVLDVGDAESVEALAEAllsEYP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 112 -IDVLIVNQGVFIGKELEKQSPEEVKFM--IDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSA 188
Cdd:cd05370  78 nLDILINNAGIQRPIDLRDPASDLDKADteIDTNLIGPIRLIKAFLPHLKK---QPEATIVNVSSGLAFVPMAANPVYCA 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15239681 189 SKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEqelkkrpELTSIIAASSGSMKTNEVAKICFDGIKAGK 262
Cdd:cd05370 155 TKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHE-------ERRNPDGGTPRKMPLDEFVDEVVAGLERGR 221
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
40-234 3.47e-28

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: 109.78  E-value: 3.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSIlarsTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAID----ESGPIDVL 115
Cdd:cd05341   8 AIVTGGARGLGLAHARLLVAEGAKVVL----SDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDtareAFGRLDVL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd05341  84 VNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKE---AGGGSIINMSSIEGLVGDPALAAYNASKGAVRG 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15239681 196 L--AQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPEL 234
Cdd:cd05341 161 LtkSAALECATQGYGIRVNSVHPGYIYTPMTDELLIAQGEM 201
PRK08263 PRK08263
short chain dehydrogenase; Provisional
41-216 3.51e-28

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 110.13  E-value: 3.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAE-AKRSiqlatGVEVATFSADVRD----YDAVSKAIDESGPIDVL 115
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADlAEKY-----GDRLLPLALDVTDraavFAAVETAVEHFGRLDIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKA-REGRgpasISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:PRK08263  82 VNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREqRSGH----IIQISSIGGISAFPMSGIYHASKWALE 157
                        170       180
                 ....*....|....*....|..
gi 15239681  195 GLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK08263 158 GMSEALAQEVAEFGIKVTLVEP 179
PRK06139 PRK06139
SDR family oxidoreductase;
31-224 4.63e-28

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 111.35  E-value: 4.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   31 VTIPIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAV----SKAI 106
Cdd:PRK06139   1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECR-ALGAEVLVVPTDVTDADQVkalaTQAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  107 DESGPIDVLIVNQGV-FIGK--ELEKQSPEEVkfmIDVNLTGSFNVIKAALPAMKArEGRGpASISLVSSQAGQAGIYGy 183
Cdd:PRK06139  80 SFGGRIDVWVNNVGVgAVGRfeETPIEAHEQV---IQTNLIGYMRDAHAALPIFKK-QGHG-IFINMISLGGFAAQPYA- 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15239681  184 TAYSASKFGLQGLAQALQQEVISD-GIHVTLLFPPDTDTPGF 224
Cdd:PRK06139 154 AAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDTPGF 195
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
38-222 4.65e-28

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: 109.55  E-value: 4.65e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYD----AVSKAIDESGPID 113
Cdd:cd08945   4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELR-EAGVEADGRTCDVRSVPeieaLVAAAVARYGPID 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREgRGPASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:cd08945  83 VLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAGGMLE-RGTGRIINIASTGGKQGVVHAAPYSASKHGV 161
                       170       180
                ....*....|....*....|....*....
gi 15239681 194 QGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:cd08945 162 VGFTKALGLELARTGITVNAVCPGFVETP 190
PRK12828 PRK12828
short chain dehydrogenase; Provisional
38-228 4.96e-28

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 109.12  E-value: 4.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARStekLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDES----GPID 113
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARGARVALIGRG---AAPLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVnrqfGRLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK12828  85 ALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTA---SGGGRIVNIGAGAALKAGPGMGAYAAAKAGV 161
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQEL 228
Cdd:PRK12828 162 ARLTEALAAELLDRGITVNAVLPSIIDTPPNRADM 196
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
40-226 5.82e-28

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: 109.39  E-value: 5.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAkrSIQLAT--GVEVATFSADVRDYDAVSKAIDES----GPID 113
Cdd:cd05366   5 AIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKS--TIQEISeaGYNAVAVGADVTDKDDVEALIDQAvekfGSFD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:cd05366  83 VMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGG--KIINASSIAGVQGFPNLGAYSASKFAV 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 15239681 194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQ 226
Cdd:cd05366 161 RGLTQTAAQELAPKGITVNAYAPGIVKTEMWDY 193
PRK06482 PRK06482
SDR family oxidoreductase;
41-221 8.50e-28

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 109.43  E-value: 8.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsIQLATGVEVATFSADVRDYDAVSKAID----ESGPIDVLI 116
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRVAATVRRPDALDD----LKARYGDRLWVLQLDVTDSAAVRAVVDrafaALGRIDVVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  117 VNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:PRK06482  82 SNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGG---GRIVQVSSEGGQIAYPGFSLYHATKWGIEGF 158
                        170       180
                 ....*....|....*....|....*
gi 15239681  197 AQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK06482 159 VEAVAQEVAPFGIEFTIVEPGPART 183
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
42-242 9.16e-28

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: 108.52  E-value: 9.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVSI-LARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAIDE----SGPIDVLI 116
Cdd:cd05362   8 VTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAEIE-AAGGKAIAVQADVSDPSQVARLFDAaekaFGGVDILV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 117 VNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkaregRGPASISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:cd05362  87 NNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL-----RDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAF 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15239681 197 AQALQQEVISDGIHVTLLFPPDTDTPGFEQElkKRPELTSIIAASS 242
Cdd:cd05362 162 TRVLAKELGGRGITVNAVAPGPVDTDMFYAG--KTEEAVEGYAKMS 205
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
40-231 1.02e-27

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 108.44  E-value: 1.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK12429   7 ALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQ-KAGGKAIGVAMDVTDEEAINAGIDYAvetfGGVDIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK12429  86 VNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGG---GRIINMASVHGLVGSAGKAAYVSAKHGLIG 162
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15239681  196 LAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKR 231
Cdd:PRK12429 163 LTKVVALEGATHGVTVNAICPGYVDTPLVRKQIPDL 198
PRK07201 PRK07201
SDR family oxidoreductase;
27-222 1.49e-27

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 113.12  E-value: 1.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   27 RPRSVTIPIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAI 106
Cdd:PRK07201 361 RRRDLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIR-AKGGTAHAYTCDLTDSAAVDHTV 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  107 D----ESGPIDVLIVNQGVFIGKELEKQSP-----EEVkfmIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQ 177
Cdd:PRK07201 440 KdilaEHGHVDYLVNNAGRSIRRSVENSTDrfhdyERT---MAVNYFGAVRLILGLLPHMRER-RFG--HVVNVSSIGVQ 513
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15239681  178 AGIYGYTAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK07201 514 TNAPRFSAYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTP 558
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
42-222 1.90e-27

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: 107.76  E-value: 1.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsiQLATGVEVATFSADVRDYD----AVSKAIDESGPIDVLIV 117
Cdd:cd05371   7 VTGGASGLGLATVERLLAQGAKVVILDLPNSPGET-----VAKLGDNCRFVPVDVTSEKdvkaALALAKAKFGRLDIVVN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQGVFI------GKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREG-----RGpaSISLVSSQAGQAGIYGYTAY 186
Cdd:cd05371  82 CAGIAVaaktynKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPdqggeRG--VIINTASVAAFEGQIGQAAY 159
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15239681 187 SASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:cd05371 160 SASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTP 195
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
38-252 1.92e-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: 107.39  E-value: 1.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKlaEAKRSIQLATGVEVATF-SADVRDYD----AVSKAIDESGPI 112
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENP--GAAAELQAINPKVKATFvQCDVTSWEqlaaAFKKAIEKFGRV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 113 DVLIVNQGVF--IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPASISLVSSQAGQAGIYGYTAYSASK 190
Cdd:cd05323  79 DILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239681 191 FGLQGLAQALQQEVISD-GIHVTLLFPPDTDTPGFEQELKKRPELtsiiAASSGSMKTNEVAK 252
Cdd:cd05323 159 HGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPLLPDLVAKEAEM----LPSAPTQSPEVVAK 217
PRK07024 PRK07024
SDR family oxidoreductase;
39-222 1.98e-27

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 107.71  E-value: 1.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   39 HVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVatFSADVRDYDAVSKA----IDESGPIDV 114
Cdd:PRK07024   4 KVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAARVSV--YAADVRDADALAAAaadfIAAHGLPDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQGVFIGKELEKQSPEEVKFMI-DVNLTGSFNVIKAALPAMKAReGRGpasiSLV--SSQAGQAGIYGYTAYSASKF 191
Cdd:PRK07024  82 VIANAGISVGTLTEEREDLAVFREVmDTNYFGMVATFQPFIAPMRAA-RRG----TLVgiASVAGVRGLPGAGAYSASKA 156
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15239681  192 GLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK07024 157 AAIKYLESLRVELRPAGVRVVTIAPGYIRTP 187
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
40-222 3.70e-27

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: 106.38  E-value: 3.70e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVevaTFSADVRDYDAVSKAIDE-----SGPIDV 114
Cdd:cd08931   3 IFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVV---AGALDVTDRAAWAAALADfaaatGGRLDA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpasiSLVSSQAGQAGIYG---YTAYSASKF 191
Cdd:cd08931  80 LFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPG------ARVINTASSSAIYGqpdLAVYSATKF 153
                       170       180       190
                ....*....|....*....|....*....|.
gi 15239681 192 GLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:cd08931 154 AVRGLTEALDVEWARHGIRVADVWPWFVDTP 184
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
47-222 4.03e-27

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 106.36  E-value: 4.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681    47 SGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiqLATGVEVATFSADVRDYDAVSKAIDES----GPIDVLIVNQGV- 121
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEE---LAEELGAAVLPCDVTDEEQVEALVAAAvekfGRLDILVNNAGFa 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   122 -FIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKARegrgpASISLVSSQAGQAGIYGYTAYSASKFGLQGLAQAL 200
Cdd:pfam13561  83 pKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG-----GSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYL 157
                         170       180
                  ....*....|....*....|..
gi 15239681   201 QQEVISDGIHVTLLFPPDTDTP 222
Cdd:pfam13561 158 AVELGPRGIRVNAISPGPIKTL 179
PRK05650 PRK05650
SDR family oxidoreductase;
40-268 5.26e-27

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 107.05  E-value: 5.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGvEVATFSADVRDYD---AVSKAIDES-GPIDVL 115
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGG-DGFYQRCDVRDYSqltALAQACEEKwGGIDVI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK05650  82 VNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFK-RQKSG--RIVNIASMAGLMQGPAMSSYNVAKAGVVA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  196 LAQALQQEVISDGIHVTLLFPP----------DTDTPGFEQELKKRPELTSIIAAssgsmktnEVAKICFDGIKAGKFTV 265
Cdd:PRK05650 159 LSETLLVELADDEIGVHVVCPSffqtnlldsfRGPNPAMKAQVGKLLEKSPITAA--------DIADYIYQQVAKGEFLI 230

                 ...
gi 15239681  266 TCH 268
Cdd:PRK05650 231 LPH 233
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
38-237 8.56e-27

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 106.20  E-value: 8.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYD----AVSKAIDESGPID 113
Cdd:cd05344   2 KVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELR-AGGAGVLAVVADLTDPEdidrLVEKAGDAFGRVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:cd05344  81 ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGW---GRIVNISSLTVKEPEPNLVLSNVARAGL 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15239681 194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSI 237
Cdd:cd05344 158 IGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEARAEKEGI 201
PRK12939 PRK12939
short chain dehydrogenase; Provisional
38-226 1.15e-26

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 105.44  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAIDES----GPID 113
Cdd:PRK12939   8 KRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALE-AAGGRAHAIAADLADPASVQRFFDAAaaalGGLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaREGRGpASISLVSSQAGQAGIyGYTAYSASKFGL 193
Cdd:PRK12939  87 GLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLR-DSGRG-RIVNLASDTALWGAP-KLGAYVASKGAV 163
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQ 226
Cdd:PRK12939 164 IGMTRSLARELGGRGITVNAIAPGLTATEATAY 196
PRK06125 PRK06125
short chain dehydrogenase; Provisional
38-231 2.71e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 104.74  E-value: 2.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDESGPIDVLIV 117
Cdd:PRK06125   8 KRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVHALDLSSPEAREQLAAEAGDIDILVN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:PRK06125  88 NAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKA---RGSGVIVNVIGAAGENPDADYICGSAGNAALMAFT 164
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15239681  198 QALQQEVISDGIHVTLLFPPDTDTPGFEQELKKR 231
Cdd:PRK06125 165 RALGGKSLDDGVRVVGVNPGPVATDRMLTLLKGR 198
PRK07478 PRK07478
short chain dehydrogenase; Provisional
42-222 2.79e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 104.63  E-value: 2.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYD----AVSKAIDESGPIDVLIV 117
Cdd:PRK07478  11 ITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIR-AEGGEAVALAGDVRDEAyakaLVALAVERFGGLDIAFN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVfIG--KELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQ-AGIYGYTAYSASKFGLQ 194
Cdd:PRK07478  90 NAGT-LGemGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGG---GSLIFTSTFVGHtAGFPGMAAYAASKAGLI 165
                        170       180
                 ....*....|....*....|....*...
gi 15239681  195 GLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK07478 166 GLTQVLAAEYGAQGIRVNALLPGGTDTP 193
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
40-203 3.34e-26

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 104.65  E-value: 3.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiqlATGVEVATFSADVRDYD----AVSKAIDESGPIDVL 115
Cdd:PRK06200   9 ALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQ----RFGDHVLVVEGDVTSYAdnqrAVDQTVDAFGKLDCF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVF-IGKELEKQSPEEVK--F--MIDVNLTGSFNVIKAALPAMKAREGrgpaSISLVSSQAGQAGIYGYTAYSASK 190
Cdd:PRK06200  85 VGNAGIWdYNTSLVDIPAETLDtaFdeIFNVNVKGYLLGAKAALPALKASGG----SMIFTLSNSSFYPGGGGPLYTASK 160
                        170
                 ....*....|...
gi 15239681  191 FGLQGLAQALQQE 203
Cdd:PRK06200 161 HAVVGLVRQLAYE 173
PRK06500 PRK06500
SDR family oxidoreductase;
40-252 4.75e-26

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 103.88  E-value: 4.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiQLATGVEV-ATFSADVRDYDAVSKAIDESGP-IDVLIV 117
Cdd:PRK06500   9 ALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARA--ELGESALViRADAGDVAAQKALAQALAEAFGrLDAVFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkARegrgPASISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:PRK06500  87 NAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLL-AN----PASIVLNGSINAHIGMPNSSVYAASKAALLSLA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239681  198 QALQQEVISDGIHVTLLFPPDTDTP-----GFEQElkKRPELTSIIAAS--SGSMKT-NEVAK 252
Cdd:PRK06500 162 KTLSGELLPRGIRVNAVSPGPVQTPlygklGLPEA--TLDAVAAQIQALvpLGRFGTpEEIAK 222
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
42-216 5.60e-26

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: 103.45  E-value: 5.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADV----RDYDAVSKAIdESGPIDVLIV 117
Cdd:cd05356   6 VTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFsagdDIYERIEKEL-EGLDIGILVN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQGVF--IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd05356  85 NVGIShsIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKR-KKG--AIVNISSFAGLIPTPLLATYSASKAFLDF 161
                       170       180
                ....*....|....*....|.
gi 15239681 196 LAQALQQEVISDGIHVTLLFP 216
Cdd:cd05356 162 FSRALYEEYKSQGIDVQSLLP 182
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
42-216 9.04e-26

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: 103.21  E-value: 9.04e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPIDVLIV 117
Cdd:cd05347  10 VTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIE-KEGVEATAFTCDVSDEEAIKAAVEaieeDFGKIDILVN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkaREGRGPASISLVSSQAGQAGIyGYTAYSASKFGLQGLA 197
Cdd:cd05347  89 NAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHM--IKQGHGKIINICSLLSELGGP-PVPAYAASKGGVAGLT 165
                       170
                ....*....|....*....
gi 15239681 198 QALQQEVISDGIHVTLLFP 216
Cdd:cd05347 166 KALATEWARHGIQVNAIAP 184
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
40-211 9.65e-26

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 107.62  E-value: 9.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiQLATGVEVATFSADVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK08324 425 ALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAA--ELGGPDRALGVACDVTDEAAVQAAFEEAalafGGVDIV 502
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKArEGRGPASISLVSSQAGQAGIyGYTAYSASKFGLQG 195
Cdd:PRK08324 503 VSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKA-QGLGGSIVFIASKNAVNPGP-NFGAYGAAKAAELH 580
                        170
                 ....*....|....*.
gi 15239681  196 LAQALQQEVISDGIHV 211
Cdd:PRK08324 581 LVRQLALELGPDGIRV 596
PRK07063 PRK07063
SDR family oxidoreductase;
38-222 1.07e-25

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 103.21  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLA-TGVEVATFSADVRDYD----AVSKAIDESGPI 112
Cdd:PRK07063   8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDvAGARVLAVPADVTDAAsvaaAVAAAEEAFGPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:PRK07063  88 DVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVER-GRG--SIVNIASTHAFKIIPGCFPYPVAKHG 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK07063 165 LLGLTRALGIEYAARNVRVNAIAPGYIETQ 194
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
41-226 1.69e-25

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 102.96  E-value: 1.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILARS--TEKLAEAKRSiqlaTGVEVATFSADVRDYDAVSKAI----DESGPIDV 114
Cdd:PRK08226  10 LITGALQGIGEGIARVFARHGANLILLDISpeIEKLADELCG----RGHRCTAVVADVRDPASVAAAIkrakEKEGRIDI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQ-AGIYGYTAYSASKFGL 193
Cdd:PRK08226  86 LVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKD---GRIVMMSSVTGDmVADPGETAYALTKAAI 162
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQ 226
Cdd:PRK08226 163 VGLTKSLAVEYAQSGIRVNAICPGYVRTPMAES 195
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
41-222 1.77e-25

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 102.50  E-value: 1.77e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVAtFSADVRDYDAVSKAIDES----GPIDVLI 116
Cdd:PRK08643   6 LVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIA-VKADVSDRDQVFAAVRQVvdtfGDLNVVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  117 VNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKArEGRGPASISlVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:PRK08643  85 NNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKK-LGHGGKIIN-ATSQAGVVGNPELAVYSSTKFAVRGL 162
                        170       180
                 ....*....|....*....|....*.
gi 15239681  197 AQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK08643 163 TQTAARDLASEGITVNAYAPGIVKTP 188
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
40-211 1.77e-25

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: 102.08  E-value: 1.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAID----ESGPIDVL 115
Cdd:cd05373   2 AAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDlieeEIGPLEVL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd05373  82 VYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLAR-GRG--TIIFTGATASLRGRAGFAAFAGAKFALRA 158
                       170
                ....*....|....*.
gi 15239681 196 LAQALQQEVISDGIHV 211
Cdd:cd05373 159 LAQSMARELGPKGIHV 174
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
42-222 2.44e-25

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: 102.08  E-value: 2.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAV----SKAIDESGPIDVLIV 117
Cdd:cd05358   8 VTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVvalfQSAIKEFGTLDILVN 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkaREGRGPASISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:cd05358  88 NAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRF--RKSKIKGKIINMSSVHEKIPWPGHVNYAASKGGVKMMT 165
                       170       180
                ....*....|....*....|....*
gi 15239681 198 QALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:cd05358 166 KTLAQEYAPKGIRVNAIAPGAINTP 190
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
40-203 2.99e-25

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 102.04  E-value: 2.99e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsIQLATGVEVATFSADVRDYD----AVSKAIDESGPIDVL 115
Cdd:cd05348   7 ALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAE----LRADFGDAVVGVEGDVRSLAdnerAVARCVERFGKLDCF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEE-----VKFMIDVNLTGSFNVIKAALPAMKAREGrgpaSISLVSSQAGQAGIYGYTAYSASK 190
Cdd:cd05348  83 IGNAGIWDYSTSLVDIPEEkldeaFDELFHINVKGYILGAKAALPALYATEG----SVIFTVSNAGFYPGGGGPLYTASK 158
                       170
                ....*....|...
gi 15239681 191 FGLQGLAQALQQE 203
Cdd:cd05348 159 HAVVGLVKQLAYE 171
FabG-like PRK07231
SDR family oxidoreductase;
42-211 3.62e-25

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 101.45  E-value: 3.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQL---ATGVEV-ATFSADVRdyDAVSKAIDESGPIDVLIV 117
Cdd:PRK07231  10 VTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAggrAIAVAAdVSDEADVE--AAVAAALERFGSVDILVN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVF-IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKArEGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:PRK07231  88 NAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRG-EGGG--AIVNVASTAGLRPRPGLGWYNASKGAVITL 164
                        170
                 ....*....|....*
gi 15239681  197 AQALQQEVISDGIHV 211
Cdd:PRK07231 165 TKALAAELGPDKIRV 179
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
40-265 4.15e-25

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 101.39  E-value: 4.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlatgvEVATFSADVRDYDAVSKA----IDESGPIDVL 115
Cdd:COG3967   8 ILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANP-----GLHTIVLDVADPASIAALaeqvTAEFPDLNVL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKEL--EKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSqagqagIYGYTA------YS 187
Cdd:COG3967  83 INNAGIMRAEDLldEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPE---AAIVNVSS------GLAFVPlavtptYS 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239681 188 ASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTpgfeqelkkrpELTSIIAASSGSMKTNEVAKICFDGIKAGKFTV 265
Cdd:COG3967 154 ATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDT-----------DLTGGQGGDPRAMPLDEFADEVMAGLETGKYEI 220
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
40-254 4.58e-25

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: 101.01  E-value: 4.58e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiqlatGVEVATFSADVRDYDAVSKAIDESGPIDVLIVNQ 119
Cdd:cd05368   5 ALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELER------GPGITTRVLDVTDKEQVAALAKEEGRIDVLFNCA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 120 G-VFIGKELEkQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQ-AGIYGYTAYSASKFGLQGLA 197
Cdd:cd05368  79 GfVHHGSILD-CEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKD---GSIINMSSVASSiKGVPNRFVYSTTKAAVIGLT 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239681 198 QALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPE----LTSIIAAS-SGSMKT-NEVAKIC 254
Cdd:cd05368 155 KSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDpeeaLKAFAARQpLGRLATpEEVAALA 217
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
42-211 4.97e-25

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 101.07  E-value: 4.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSI-LARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAV----SKAIDESGPIDVLI 116
Cdd:PRK05565  10 VTGASGGIGRAIAELLAKEGAKVVIaYDINEEAAQELLEEIK-EEGGDAIAVKADVSSEEDVenlvEQIVEKFGKIDILV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  117 VNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:PRK05565  89 NNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKS---GVIVNISSIWGLIGASCEVLYSASKGAVNAF 165
                        170
                 ....*....|....*
gi 15239681  197 AQALQQEVISDGIHV 211
Cdd:PRK05565 166 TKALAKELAPSGIRV 180
PRK12937 PRK12937
short chain dehydrogenase; Provisional
41-245 5.38e-25

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 100.97  E-value: 5.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEA-KRSIQLATGVEVAtFSADVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK12937   9 IVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADElVAEIEAAGGRAIA-VQADVADAAAVTRLFDAAetafGRIDVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkareGRGPASISLVSSQAGQAgIYGYTAYSASKFGLQG 195
Cdd:PRK12937  88 VNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL----GQGGRIINLSTSVIALP-LPGYGPYAASKAAVEG 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15239681  196 LAQALQQEVISDGIHVTLLFPPDTDTpgfeqELKKRPELTSIIAASSGSM 245
Cdd:PRK12937 163 LVHVLANELRGRGITVNAVAPGPVAT-----ELFFNGKSAEQIDQLAGLA 207
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
40-226 1.21e-24

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: 100.16  E-value: 1.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEK------------LAEAKRSIQlATGVEVATFSADVRDYD----AVS 103
Cdd:cd05338   6 AFVTGASRGIGRAIALRLAKAGATVVVAAKTASEgdngsakslpgtIEETAEEIE-AAGGQALPIVVDVRDEDqvraLVE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 104 KAIDESGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGY 183
Cdd:cd05338  85 ATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVK---AGQGHILNISPPLSLRPARGD 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15239681 184 TAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPD-TDTPGFEQ 226
Cdd:cd05338 162 VAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTaIETPAATE 205
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
42-221 3.30e-24

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 98.92  E-value: 3.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDES----GPIDVLIV 117
Cdd:PRK12935  11 VTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAvnhfGKVDILVN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:PRK12935  91 NAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEE---GRIISISSIIGQAGGFGQTNYSAAKAGMLGFT 167
                        170       180
                 ....*....|....*....|....
gi 15239681  198 QALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK12935 168 KSLALELAKTNVTVNAICPGFIDT 191
PRK06841 PRK06841
short chain dehydrogenase; Provisional
40-216 5.93e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 98.58  E-value: 5.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARStEKLAEAKRSIqlaTGVEVATFSADVRDYDAVSKAID----ESGPIDVL 115
Cdd:PRK06841  18 AVVTGGASGIGHAIAELFAAKGARVALLDRS-EDVAEVAAQL---LGGNAKGLVCDVSDSQSVEAAVAavisAFGRIDIL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK06841  94 VNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAA-GGG--KIVNLASQAGVVALERHVAYCASKAGVVG 170
                        170       180
                 ....*....|....*....|.
gi 15239681  196 LAQALQQEVISDGIHVTLLFP 216
Cdd:PRK06841 171 MTKVLALEWGPYGITVNAISP 191
PRK07677 PRK07677
short chain dehydrogenase; Provisional
40-203 6.76e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 98.21  E-value: 6.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGvEVATFSADVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK07677   4 VIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPG-QVLTVQMDVRNPEDVQKMVEQIdekfGRIDAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVN-QGVFIGKElEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGpASISLVSSQAGQAGIyGYTAYSASKFGLQ 194
Cdd:PRK07677  83 INNaAGNFICPA-EDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIKG-NIINMVATYAWDAGP-GVIHSAAAKAGVL 159

                 ....*....
gi 15239681  195 GLAQALQQE 203
Cdd:PRK07677 160 AMTRTLAVE 168
PRK06138 PRK06138
SDR family oxidoreductase;
38-224 7.96e-24

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 97.91  E-value: 7.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqlATGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:PRK06138   6 RVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAI--AAGGRAFARQGDVGSAEAVEALVDfvaaRWGRLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK06138  84 VLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGG---GSIVNTASQLALAGGRGRAAYVASKGAI 160
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGF 224
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPYF 191
PRK07890 PRK07890
short chain dehydrogenase; Provisional
40-216 1.51e-23

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 97.34  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDA----VSKAIDESGPIDVL 115
Cdd:PRK07890   8 VVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEID-DLGRRALAVPTDITDEDQcanlVALALERFGRVDAL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVN---QGVFigKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpaSISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:PRK07890  87 VNNafrVPSM--KPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGG----SIVMINSMVLRHSQPKYGAYKMAKGA 160
                        170       180
                 ....*....|....*....|....
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK07890 161 LLAASQSLATELGPQGIRVNSVAP 184
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
38-254 2.40e-23

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 96.62  E-value: 2.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDkvkaEVGEID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK12938  84 VLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVE---RGWGRIINISSVNGQKGQFGQTNYSTAKAGI 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239681  194 QGLAQALQQEVISDGIHVtllfppDTDTPGF-EQELKK--RPELTSIIAASSGSMK---TNEVAKIC 254
Cdd:PRK12938 161 HGFTMSLAQEVATKGVTV------NTVSPGYiGTDMVKaiRPDVLEKIVATIPVRRlgsPDEIGSIV 221
PRK06182 PRK06182
short chain dehydrogenase; Validated
40-222 3.00e-23

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 96.95  E-value: 3.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKrsiqlATGVEVatFSADVRDYD----AVSKAIDESGPIDVL 115
Cdd:PRK06182   6 ALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLA-----SLGVHP--LSLDVTDEAsikaAVDTIIAEEGRIDVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKA-REGRgpasISLVSSQAGQagIYGYTA--YSASKFG 192
Cdd:PRK06182  79 VNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAqRSGR----IINISSMGGK--IYTPLGawYHATKFA 152
                        170       180       190
                 ....*....|....*....|....*....|
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK06182 153 LEGFSDALRLEVAPFGIDVVVIEPGGIKTE 182
PRK06179 PRK06179
short chain dehydrogenase; Provisional
40-226 3.81e-23

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 96.51  E-value: 3.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAeakrSIQlatGVEVATFsaDVRDYDAVSKAIDE----SGPIDVL 115
Cdd:PRK06179   7 ALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAA----PIP---GVELLEL--DVTDDASVQAAVDEviarAGRIDVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKA-REGRgpasISLVSSqagqagIYG-----YTA-YSA 188
Cdd:PRK06179  78 VNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAqGSGR----IINISS------VLGflpapYMAlYAA 147
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15239681  189 SKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTPgFEQ 226
Cdd:PRK06179 148 SKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTN-FDA 184
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
38-226 4.98e-23

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 95.86  E-value: 4.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqlatGVEVATFSADVRDYD----AVSKAIDESGPID 113
Cdd:PRK07067   7 KVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEI----GPAAIAVSLDVTRQDsidrIVAAAVERFGGID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGPASISLvSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK07067  83 ILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQ-GRGGKIINM-ASQAGRRGEALVSHYCATKAAV 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQ 226
Cdd:PRK07067 161 ISYTQSAALALIRHGINVNAIAPGVVDTPMWDQ 193
PRK05876 PRK05876
short chain dehydrogenase; Provisional
38-268 5.59e-23

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 96.18  E-value: 5.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAIDES----GPID 113
Cdd:PRK05876   7 RGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLR-AEGFDVHGVMCDVRHREEVTHLADEAfrllGHVD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGpASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK05876  86 VVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRL-LEQGTG-GHVVFTASFAGLVPNAGLGAYGVAKYGV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSIIAASSG---------SMKTNEVAKICFDGIKAGKFT 264
Cdd:PRK05876 164 VGLAETLAREVTADGIGVSVLCPMVVETNLVANSERIRGAACAQSSTTGSpgplplqddNLGVDDIAQLTADAILANRLY 243

                 ....
gi 15239681  265 VTCH 268
Cdd:PRK05876 244 VLPH 247
PRK06484 PRK06484
short chain dehydrogenase; Validated
38-222 8.35e-23

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 98.77  E-value: 8.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqlatGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSL----GPDHHALAMDVSDEAQIREGFEqlhrEFGRID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVF--IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKArEGRGPASISlVSSQAGQAGIYGYTAYSASKF 191
Cdd:PRK06484  82 VLVNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIE-QGHGAAIVN-VASGAGLVALPKRTAYSASKA 159
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15239681  192 GLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK06484 160 AVISLTRSLACEWAAKGIRVNAVLPGYVRTQ 190
PRK06914 PRK06914
SDR family oxidoreductase;
41-236 1.05e-22

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 95.48  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILARSTEK---LAEAKRSIQLATGVEVatFSADVRDYDAV---SKAIDESGPIDV 114
Cdd:PRK06914   7 IVTGASSGFGLLTTLELAKKGYLVIATMRNPEKqenLLSQATQLNLQQNIKV--QQLDVTDQNSIhnfQLVLKEIGRIDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:PRK06914  85 LVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKS---GKIINISSISGRVGFPGLSPYVSSKYALE 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15239681  195 GLAQALQQEVISDGIHVTLLFPPDTDTPGFE---QELKKRPELTS 236
Cdd:PRK06914 162 GFSESLRLELKPFGIDVALIEPGSYNTNIWEvgkQLAENQSETTS 206
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
40-233 2.26e-22

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: 93.69  E-value: 2.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsiqlaTGVEVATFSADVRDYDAV----SKAIDESGPIDVL 115
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLE--------YGDPLRLTPLDVADAAAVrevcSRLLAEHGPIDAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd05331  73 VNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRT---GAIVTVASNAAHVPRISMAAYGASKAALAS 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15239681 196 LAQALQQEVISDGIHVTLLFPPDTDTP----------GFEQELKKRPE 233
Cdd:cd05331 150 LSKCLGLELAPYGVRCNVVSPGSTDTAmqrtlwhdedGAAQVIAGVPE 197
PRK12742 PRK12742
SDR family oxidoreductase;
38-221 2.27e-22

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 93.67  E-value: 2.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAkrsiqLATGVEVATFSADVRDYDAVSKAIDESGPIDVLIV 117
Cdd:PRK12742   7 KKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAER-----LAQETGATAVQTDSADRDAVIDVVRKSGALDILVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNvikAALPAmkAREGRGPASISLVSSQAG-QAGIYGYTAYSASKFGLQGL 196
Cdd:PRK12742  82 NAGIAVFGDALELDADDIDRLFKINIHAPYH---ASVEA--ARQMPEGGRIIIIGSVNGdRMPVAGMAAYAASKSALQGM 156
                        170       180
                 ....*....|....*....|....*
gi 15239681  197 AQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK12742 157 ARGLARDFGPRGITINVVQPGPIDT 181
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
42-231 2.60e-22

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: 94.05  E-value: 2.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLAT-GVEVATFSADVRD----YDAVSKAIDESGPIDVLI 116
Cdd:cd08940   7 VTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKhGVKVLYHGADLSKpaaiEDMVAYAQRQFGGVDILV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 117 VNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKARE-GRgpasISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd08940  87 NNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGR----IINIASVHGLVASANKSAYVAAKHGVVG 162
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15239681 196 LAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKR 231
Cdd:cd08940 163 LTKVVALETAGTGVTCNAICPGWVLTPLVEKQISAL 198
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
40-216 3.06e-22

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: 93.68  E-value: 3.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSA---DVRDYDAVSKAID--ESGPIDV 114
Cdd:cd09806   3 VLITGCSSGIGLHLAVRLASDPSKRFKVYATMRDLKKKGRLWEAAGALAGGTLETlqlDVCDSKSVAAAVErvTERHVDV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:cd09806  83 LVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKR---RGSGRILVTSSVGGLQGLPFNDVYCASKFALE 159
                       170       180
                ....*....|....*....|..
gi 15239681 195 GLAQALQQEVISDGIHVTLLFP 216
Cdd:cd09806 160 GLCESLAVQLLPFNVHLSLIEC 181
PRK06194 PRK06194
hypothetical protein; Provisional
42-268 5.78e-22

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 93.54  E-value: 5.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAV----SKAIDESGPIDVLIV 117
Cdd:PRK06194  11 ITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELR-AQGAEVLGVRTDVSDAAQVealaDAALERFGAVHLLFN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPASISLVSSQAGQAGIYGYTA---YSASKFGLQ 194
Cdd:PRK06194  90 NAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEKDPAYEGHIVNTASMAGLLAPPAmgiYNVSKHAVV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  195 GLAQALQQ--EVISDGIHVTLLFPPDTDTpGFEQELKKRPE--------LTSIIAA--------SSGSMKTNEVAKICFD 256
Cdd:PRK06194 170 SLTETLYQdlSLVTDQVGASVLCPYFVPT-GIWQSERNRPAdlantappTRSQLIAqamsqkavGSGKVTAEEVAQLVFD 248
                        250
                 ....*....|..
gi 15239681  257 GIKAGKFTVTCH 268
Cdd:PRK06194 249 AIRAGRFYIYSH 260
PRK08264 PRK08264
SDR family oxidoreductase;
32-265 9.43e-22

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 91.87  E-value: 9.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   32 TIPIKFRHVFITGGSSGIGLALAHRAVSEGA-KVSILARSTEKLAEakrsiqlaTGVEVATFSADVRDYDAVSKAIDESG 110
Cdd:PRK08264   1 MMDIKGKVVLVTGANRGIGRAFVEQLLARGAaKVYAAARDPESVTD--------LGPRVVPLQLDVTDPASVAAAAEAAS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  111 PIDVLIVNQGVF-IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSAS 189
Cdd:PRK08264  73 DVTILVNNAGIFrTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAA---NGGGAIVNVLSVLSWVNFPNLGTYSAS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFPP--DTD-TPGFEQElKKRPEltsiiaassgsmktnEVAKICFDGIKAGKFTV 265
Cdd:PRK08264 150 KAAAWSLTQALRAELAPQGTRVLGVHPGpiDTDmAAGLDAP-KASPA---------------DVARQILDALEAGDEEV 212
PRK05866 PRK05866
SDR family oxidoreductase;
27-222 1.12e-21

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 92.88  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   27 RPRSVTIPIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqLATGVEVATFSADVRDYDAVSKAI 106
Cdd:PRK05866  30 RPPRQPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRI-TRAGGDAMAVPCDLSDLDAVDALV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  107 ----DESGPIDVLIVNQGVFIGKELEkQSPE---EVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAG 179
Cdd:PRK05866 109 adveKRIGGVDILINNAGRSIRRPLA-ESLDrwhDVERTMVLNYYAPLRLIRGLAPGMLE---RGDGHIINVATWGVLSE 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15239681  180 IYG-YTAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK05866 185 ASPlFSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATP 228
PRK07775 PRK07775
SDR family oxidoreductase;
28-221 1.33e-21

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 92.51  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   28 PRSVTIPIKfRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYD----AVS 103
Cdd:PRK07775   2 PRFEPHPDR-RPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIR-ADGGEAVAFPLDVTDPDsvksFVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  104 KAIDESGPIDVLIVNQG-VFIGKeLEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREgRGpaSISLVSSQAGQAGIYG 182
Cdd:PRK07775  80 QAEEALGEIEVLVSGAGdTYFGK-LHEISTEQFESQVQIHLVGANRLATAVLPGMIERR-RG--DLIFVGSDVALRQRPH 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15239681  183 YTAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK07775 156 MGAYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
PRK08278 PRK08278
SDR family oxidoreductase;
38-216 1.40e-21

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 92.27  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTE---KLA----EAKRSIQlATGVEVATFSADVRDYD----AVSKAI 106
Cdd:PRK08278   7 KTLFITGASRGIGLAIALRAARDGANIVIAAKTAEphpKLPgtihTAAEEIE-AAGGQALPLVGDVRDEDqvaaAVAKAV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  107 DESGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREgrGPASISL---VSSQAGQAGiyGY 183
Cdd:PRK08278  86 ERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSE--NPHILTLsppLNLDPKWFA--PH 161
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15239681  184 TAYSASKFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK08278 162 TAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
40-222 2.31e-21

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: 90.27  E-value: 2.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAeakrsiQLATGVEVATFSADVRDYDAVSKAIDESGPIDVLIVNQ 119
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALA------GLAAEVGALARPADVAAELEVWALAQELGPLDLLVYAA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 120 GVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPaMKAREGRGpasiSLVSSQAGQAGIYGYTAYSASKFGLQGLAQA 199
Cdd:cd11730  75 GAILGKPLARTKPAAWRRILDANLTGAALVLKHALA-LLAAGARL----VFLGAYPELVMLPGLSAYAAAKAALEAYVEV 149
                       170       180
                ....*....|....*....|...
gi 15239681 200 LQQEVisDGIHVTLLFPPDTDTP 222
Cdd:cd11730 150 ARKEV--RGLRLTLVRPPAVDTG 170
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
40-238 2.43e-21

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


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 91.36  E-value: 2.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLAtGVEVATFSADVRD-------YDAVSKAIDesGPI 112
Cdd:cd05329   9 ALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREK-GFKVEGSVCDVSSrserqelMDTVASHFG--GKL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKARegrGPASISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:cd05329  86 NILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKAS---GNGNIVFISSVAGVIAVPSGAPYGATKGA 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15239681 193 LQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSII 238
Cdd:cd05329 163 LNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVI 208
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
40-216 2.98e-21

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


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 90.93  E-value: 2.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqLATGV---EVATFSADVRDYDAVSKAIDES----GPI 112
Cdd:cd05364   6 AIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSC-LQAGVsekKILLVVADLTEEEGQDRIISTTlakfGRL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpaSISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:cd05364  85 DILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKG----EIVNVSSVAGGRSFPGVLYYCISKAA 160
                       170       180
                ....*....|....*....|....
gi 15239681 193 LQGLAQALQQEVISDGIHVTLLFP 216
Cdd:cd05364 161 LDQFTRCTALELAPKGVRVNSVSP 184
PRK08251 PRK08251
SDR family oxidoreductase;
40-216 3.21e-21

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 90.77  E-value: 3.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSI-QLATGVEVATFSADVRDYDAVSKAI----DESGPIDV 114
Cdd:PRK08251   5 ILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELlARYPGIKVAVAALDVNDHDQVFEVFaefrDELGGLDR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAGIYGY-TAYSASKFGL 193
Cdd:PRK08251  85 VIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQ-GSG--HLVLISSVSAVRGLPGVkAAYAASKAGV 161
                        170       180
                 ....*....|....*....|...
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK08251 162 ASLGEGLRAELAKTPIKVSTIEP 184
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
38-216 3.73e-21

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: 90.61  E-value: 3.73e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAkrsIQLATGVEvaTFSADVRDYDAVSKAIDESGPIDVLIV 117
Cdd:cd05351   8 KRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSL---VRECPGIE--PVCVDLSDWDATEEALGSVGPVDLLVN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREgrGPASISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:cd05351  83 NAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARG--VPGSIVNVSSQASQRALTNHTVYCSTKAALDMLT 160
                       170
                ....*....|....*....
gi 15239681 198 QALQQEVISDGIHVTLLFP 216
Cdd:cd05351 161 KVMALELGPHKIRVNSVNP 179
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
42-282 4.32e-21

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 90.73  E-value: 4.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPIDVLIV 117
Cdd:PRK13394  12 VTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEIN-KAGGKAIGVAMDVTNEDAVNAGIDkvaeRFGSVDILVS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAM-KAREGRGPASISLVSSQAGQAgiyGYTAYSASKFGLQGL 196
Cdd:PRK13394  91 NAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEASP---LKSAYVTAKHGLLGL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  197 AQALQQEVISDGIHVTLLFPPDTDTPGFEQELkkrPEltsiIAASSGSMKTNEVAKICFDGIKAGKFTV------TCHFI 270
Cdd:PRK13394 168 ARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQI---PE----QAKELGISEEEVVKKVMLGKTVDGVFTTvedvaqTVLFL 240
                        250
                 ....*....|..
gi 15239681  271 GFLLSIASTGMS 282
Cdd:PRK13394 241 SSFPSAALTGQS 252
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
40-222 6.63e-21

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 89.94  E-value: 6.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVsilarsteklAEAKRSIQLATGVEVATFSADVRDYDAVSKAID----ESGPIDVL 115
Cdd:PRK08220  11 VWVTGAAQGIGYAVALAFVEAGAKV----------IGFDQAFLTQEDYPFATFVLDVSDAAAVAQVCQrllaETGPLDVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK08220  81 VNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRS---GAIVTVGSNAAHVPRIGMAAYGASKAALTS 157
                        170       180
                 ....*....|....*....|....*..
gi 15239681  196 LAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK08220 158 LAKCVGLELAPYGVRCNVVSPGSTDTD 184
PRK06949 PRK06949
SDR family oxidoreductase;
30-221 1.22e-20

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 89.44  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   30 SVTIPIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYD----AVSKA 105
Cdd:PRK06949   2 GRSINLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIE-AEGGAAHVVSLDVTDYQsikaAVAHA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  106 IDESGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPAS-----ISLVSSQAGQAGI 180
Cdd:PRK06949  81 ETEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAGNTkpggrIINIASVAGLRVL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15239681  181 YGYTAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK06949 161 PQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDT 201
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
35-216 1.46e-20

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 89.07  E-value: 1.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqlatGVEvaTFSADVRDYDAVSKAIDE----SG 110
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREK----GVF--TIKCDVGNRDQVKKSKEVvekeFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  111 PIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAG-QAGIYGYTAYSAS 189
Cdd:PRK06463  79 RVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKN---GAIVNIASNAGiGTAAEGTTFYAIT 155
                        170       180
                 ....*....|....*....|....*..
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAP 182
PRK07074 PRK07074
SDR family oxidoreductase;
38-233 1.76e-20

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 89.06  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVA---TFSADVRDydAVSKAIDESGPIDV 114
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFVPVAcdlTDAASLAA--ALANAAAERGPVDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAGQAgIYGYTAYSASKFGLQ 194
Cdd:PRK07074  81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKR-SRG--AVVNIGSVNGMA-ALGHPAYSAAKAGLI 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15239681  195 GLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPE 233
Cdd:PRK07074 157 HYTKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAANPQ 195
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
40-230 2.33e-20

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: 88.73  E-value: 2.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSI-QLATGVEVATFSADVRDYDAVSKAIDES----GPIDV 114
Cdd:cd05330   6 VLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALlEIAPDAEVLLIKADVSDEAQVEAYVDATveqfGRIDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQGVfIGKE--LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:cd05330  86 FFNNAGI-EGKQnlTEDFGADEFDKVVSINLRGVFYGLEKVLKVMRE---QGSGMIVNTASVGGIRGVGNQSGYAAAKHG 161
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15239681 193 LQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKK 230
Cdd:cd05330 162 VVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSLKQ 199
PRK07060 PRK07060
short chain dehydrogenase; Provisional
38-222 3.53e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 87.85  E-value: 3.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAeakrsiQLATGVEVATFSADVRDYDAVSKAIDESGPIDVLIV 117
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALD------RLAGETGCEPLRLDVGDDAAIRAALAAAGAFDGLVN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGpASISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:PRK07060  84 CAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAM-IAAGRG-GSIVNVSSQAALVGLPDHLAYCASKAALDAIT 161
                        170       180
                 ....*....|....*....|....*
gi 15239681  198 QALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK07060 162 RVLCVELGPHGIRVNSVNPTVTLTP 186
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
42-216 4.68e-20

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: 87.45  E-value: 4.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVSIL---ARSTEKLAEAKRSIQLATGVEV-ATFSADVRDydAVSKAIDESGPIDVLIV 117
Cdd:cd08943   6 VTGGASGIGLAIAKRLAAEGAAVVVAdidPEIAEKVAEAAQGGPRALGVQCdVTSEAQVQS--AFEQAVLEFGGLDIVVS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaREGRGPASISLVSSQAGQAGIyGYTAYSASKFGLQGLA 197
Cdd:cd08943  84 NAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMK-SQGIGGNIVFNASKNAVAPGP-NAAAYSAAKAAEAHLA 161
                       170
                ....*....|....*....
gi 15239681 198 QALQQEVISDGIHVTLLFP 216
Cdd:cd08943 162 RCLALEGGEDGIRVNTVNP 180
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
38-231 5.62e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 87.52  E-value: 5.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:PRK07523  11 RRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLK-GQGLSAHALAFDVTDHDAVRAAIDafeaEIGPID 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPASISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK07523  90 ILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAVGNL 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15239681  194 -QGLA-----QALQQEVISDGIHVTLLFPPDTDTPGFEQELKKR 231
Cdd:PRK07523 170 tKGMAtdwakHGLQCNAIAPGYFDTPLNAALVADPEFSAWLEKR 213
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
38-224 5.91e-20

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: 87.67  E-value: 5.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSA-DVRDYD----AVSKAIDESGPI 112
Cdd:cd05327   2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAKVEVIQlDLSSLAsvrqFAEEFLARFPRL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 113 DVLIVNQGVFIGKELEkqSPEEVKFMIDVNLTGSFNVIKAALPAMKAREgrgPASISLVSSQAGQAGI------------ 180
Cdd:cd05327  82 DILINNAGIMAPPRRL--TKDGFELQFAVNYLGHFLLTNLLLPVLKASA---PSRIVNVSSIAHRAGPidfndldlennk 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15239681 181 --YGYTAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGF 224
Cdd:cd05327 157 eySPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELL 202
PRK08628 PRK08628
SDR family oxidoreductase;
40-229 7.33e-20

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 87.32  E-value: 7.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLatGVEVATFSADVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK08628  10 VIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEELRAL--QPRAEFVQVDLTDDAQCRDAVEQTvakfGRIDGL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEkQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpaSISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK08628  88 VNNAGVNDGVGLE-AGREAFVASLERNLIHYYVMAHYCLPHLKASRG----AIVNISSKTALTGQGGTSGYAAAKGAQLA 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15239681  196 LAQALQQEVISDGIHVTLLFPPDTDTPGFEQELK 229
Cdd:PRK08628 163 LTREWAVALAKDGVRVNAVIPAEVMTPLYENWIA 196
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
38-222 1.09e-19

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 86.48  E-value: 1.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADV-----RDYDAVSKAID-ESGP 111
Cdd:cd05340   5 RIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLltctsENCQQLAQRIAvNYPR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 112 IDVLIVNQGVFIGK-ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASK 190
Cdd:cd05340  85 LDGVLHNAGLLGDVcPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDA---GSLVFTSSSVGRQGRANWGAYAVSK 161
                       170       180       190
                ....*....|....*....|....*....|..
gi 15239681 191 FGLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:cd05340 162 FATEGL*QVLADEYQQRNLRVNCINPGGTRTA 193
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
40-211 1.11e-19

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 86.55  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLAtGVEVATFSADVRDYDAV----SKAIDESGPIDVL 115
Cdd:PRK08217   8 IVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGAL-GTEVRGYAANVTDEEDVeatfAQIAEDFGQLNGL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGV-----FI----GKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGPASISlVSSQAgQAGIYGYTAY 186
Cdd:PRK08217  87 INNAGIlrdglLVkakdGKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKM-IESGSKGVIIN-ISSIA-RAGNMGQTNY 163
                        170       180
                 ....*....|....*....|....*
gi 15239681  187 SASKFGLQGLAQALQQEVISDGIHV 211
Cdd:PRK08217 164 SASKAGVAAMTVTWAKELARYGIRV 188
PRK06484 PRK06484
short chain dehydrogenase; Validated
38-226 1.35e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.14  E-value: 1.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEklaEAKRSIQLATGVEVAtFSADVRDYDAVSKAIDES----GPID 113
Cdd:PRK06484 270 RVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAE---GAKKLAEALGDEHLS-VQADITDEAAVESAFAQIqarwGRLD 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVF-IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkaregRGPASISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:PRK06484 346 VLVNNAGIAeVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM-----SQGGVIVNLGSIASLLALPPRNAYCASKAA 420
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQ 226
Cdd:PRK06484 421 VTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLA 454
PRK09242 PRK09242
SDR family oxidoreductase;
38-238 1.70e-19

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 86.34  E-value: 1.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSI-QLATGVEVATFSADVRDYDAVSKAID----ESGPI 112
Cdd:PRK09242  10 QTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaEEFPEREVHGLAADVSDDEDRRAILDwvedHWDGL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:PRK09242  90 HILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQ---HASSAIVNIGSVSGLTHVRSGAPYGMTKAA 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSII 238
Cdd:PRK09242 167 LLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYEQVI 212
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
42-216 1.83e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 86.15  E-value: 1.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDA----VSKAIDESGPIDVLIV 117
Cdd:PRK08213  17 VTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLE-ALGIDALWIAADVADEADierlAEETLERFGHVDILVN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGpaSISLVSSQAGQAG----IYGYTAYSASKFGL 193
Cdd:PRK08213  96 NAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPRGYG--RIINVASVAGLGGnppeVMDTIAYNTSKGAV 173
                        170       180
                 ....*....|....*....|...
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK08213 174 INFTRALAAEWGPHGIRVNAIAP 196
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
40-222 2.23e-19

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 85.77  E-value: 2.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARStEKLAEAKRSIQlATGVEVATFSADVRDYD----AVSKAIDESGPIDVL 115
Cdd:PRK12823  11 VVVTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELR-AAGGEALALTADLETYAgaqaAMAAAVEAFGRIDVL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFI-GKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpaSISLVSSQAgQAGIYgYTAYSASKFGLQ 194
Cdd:PRK12823  89 INNVGGTIwAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQ-GGG--AIVNVSSIA-TRGIN-RVPYSAAKGGVN 163
                        170       180
                 ....*....|....*....|....*...
gi 15239681  195 GLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK12823 164 ALTASLAFEYAEHGIRVNAVAPGGTEAP 191
PRK06198 PRK06198
short chain dehydrogenase; Provisional
40-231 2.72e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 85.83  E-value: 2.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAK-VSILARSTEKlAEAKRSIQLATGVEVATFSADVRDYDA----VSKAIDESGPIDV 114
Cdd:PRK06198   9 ALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEK-GEAQAAELEALGAKAVFVQADLSDVEDcrrvVAAADEAFGRLDA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGP-ASISLVSSQAGQAGIygyTAYSASKFGL 193
Cdd:PRK06198  88 LVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEGTiVNIGSMSAHGGQPFL---AAYCASKGAL 164
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDTPGfEQELKKR 231
Cdd:PRK06198 165 ATLTRNAAYALLRNRIRVNGLNIGWMATEG-EDRIQRE 201
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
35-265 3.02e-19

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: 85.15  E-value: 3.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  35 IKFRHVFITGGSSGIGLALAHRAVSEGA-KVSILARSTEKLAEakrsIQLATGVEVATFSADVRDYDAVSKAIDESGPID 113
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAH----LVAKYGDKVVPLRLDVTDPESIKAAAAQAKDVD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVF-IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:cd05354  77 VVINNAGVLkPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGG---GAIVNLNSVASLKNFPAMGTYSASKSA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239681 193 LQGLAQALQQEVISDGIHVTLLFPPDTDTpgfeqelkkrpELTSIIAASSGSmkTNEVAKICFDGIKAGKFTV 265
Cdd:cd05354 154 AYSLTQGLRAELAAQGTLVLSVHPGPIDT-----------RMAAGAGGPKES--PETVAEAVLKALKAGEFHV 213
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
38-252 3.42e-19

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: 85.26  E-value: 3.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRD----YDAVSKAIDESGPID 113
Cdd:cd05343   7 RVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYQCDLSNeeqiLSMFSAIRTQHQGVD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGPASISLVSSQAGQAGIYGYTA--YSASKF 191
Cdd:cd05343  87 VCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKER-NVDDGHIININSMSGHRVPPVSVFhfYAATKH 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239681 192 GLQGLAQALQQEV--ISDGIHVTLLFPPDTDTPGFEQELKKRPELTSIIAASSGSMKTNEVAK 252
Cdd:cd05343 166 AVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPEDVAN 228
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
38-216 4.40e-19

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 85.07  E-value: 4.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSI------------LARSTEKLAEAkrsIQLATGVEVATFSaDVRDYDAVSK- 104
Cdd:cd05353   6 RVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgsgkSSSAADKVVDE---IKAAGGKAVANYD-SVEDGEKIVKt 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 105 AIDESGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKARE-GRgpasISLVSSQAGQAGIYGY 183
Cdd:cd05353  82 AIDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGR----IINTSSAAGLYGNFGQ 157
                       170       180       190
                ....*....|....*....|....*....|...
gi 15239681 184 TAYSASKFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:cd05353 158 ANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAP 190
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
34-222 5.76e-19

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 84.89  E-value: 5.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  34 PIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSteKLAEAKRSIQLATGVEVATFSADVRDYD----AVSKAIDES 109
Cdd:cd08937   1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS--ELVHEVLAEILAAGDAAHVHTADLETYAgaqgVVRAAVERF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 110 GPIDVLIVNQ-GVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQaGIYgYTAYSA 188
Cdd:cd08937  79 GRVDVLINNVgGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLE---RQQGVIVNVSSIATR-GIY-RIPYSA 153
                       170       180       190
                ....*....|....*....|....*....|....
gi 15239681 189 SKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:cd08937 154 AKGGVNALTASLAFEHARDGIRVNAVAPGGTEAP 187
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
42-225 7.67e-19

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 84.32  E-value: 7.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVA-TFSADV---RDYDAVSKAIDES-GPIDVLI 116
Cdd:PRK12384   7 VIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMAyGFGADAtseQSVLALSRGVDEIfGRVDLLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  117 VNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:PRK12384  87 YNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIQG--RIIQINSKSGKVGSKHNSGYSAAKFGGVGL 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 15239681  197 AQALQQEVISDGIHVTLLFPPD-TDTPGFE 225
Cdd:PRK12384 165 TQSLALDLAEYGITVHSLMLGNlLKSPMFQ 194
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
35-222 1.15e-18

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: 84.27  E-value: 1.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSIL--------ARSTEKLAEAKrsiqlatGVEVATFSADVRD----YDAV 102
Cdd:cd05355  24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINylpeeeddAEETKKLIEEE-------GRKCLLIPGDLGDesfcRDLV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 103 SKAIDESGPIDVLIVNQGVFIGKE-LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKarEGrgpASISLVSSQAGQAGIY 181
Cdd:cd05355  97 KEVVKEFGKLDILVNNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPHLK--KG---SSIINTTSVTAYKGSP 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15239681 182 GYTAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:cd05355 172 HLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTP 212
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
40-222 1.28e-18

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: 83.69  E-value: 1.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqlatGVEVATFSADVRDYDAVSKAID----ESGPIDVL 115
Cdd:cd08944   6 AIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQI----AGGALALRVDVTDEQQVAALFEraveEFGGLDLL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVF-IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:cd08944  82 VNNAGAMhLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGG---GSIVNLSSIAGQSGDPGYGAYGASKAAIR 158
                       170       180
                ....*....|....*....|....*...
gi 15239681 195 GLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:cd08944 159 NLTRTLAAELRHAGIRCNALAPGLIDTP 186
PRK07831 PRK07831
SDR family oxidoreductase;
38-196 3.75e-18

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 82.39  E-value: 3.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGS-SGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVE-VATFSADVRDYDAVSKAIDES----GP 111
Cdd:PRK07831  18 KVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGLGrVEAVVCDVTSEAQVDALIDAAverlGR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  112 IDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRG----PASISLVSSQAGQAgiygytAYS 187
Cdd:PRK07831  98 LDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGvivnNASVLGWRAQHGQA------HYA 171

                 ....*....
gi 15239681  188 ASKFGLQGL 196
Cdd:PRK07831 172 AAKAGVMAL 180
PRK06124 PRK06124
SDR family oxidoreductase;
42-216 3.78e-18

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 82.45  E-value: 3.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPIDVLIV 117
Cdd:PRK06124  16 VTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALR-AAGGAAEALAFDIADEEAVAAAFAridaEHGRLDILVN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:PRK06124  95 NVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMK-RQGYG--RIIAITSIAGQVARAGDAVYPAAKQGLTGLM 171
                        170
                 ....*....|....*....
gi 15239681  198 QALQQEVISDGIHVTLLFP 216
Cdd:PRK06124 172 RALAAEFGPHGITSNAIAP 190
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
40-227 4.00e-18

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: 82.12  E-value: 4.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSI-LARSTEKlaeAKRSIQLATGVEVATfSADVRDYDAVSKAIDES----GPIDV 114
Cdd:cd05349   3 VLVTGASRGLGAAIARSFAREGARVVVnYYRSTES---AEAVAAEAGERAIAI-QADVRDRDQVQAMIEEAknhfGPVDT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQ-GVFIGKELEKQSPEEVKF-----MIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSA 188
Cdd:cd05349  79 IVNNAlIDFPFDPDQRKTFDTIDWedyqqQLEGAVKGALNLLQAVLPDFKE---RGSGRVINIGTNLFQNPVVPYHDYTT 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15239681 189 SKFGLQGLAQALQQEVISDGIHVTLLFP---PDTDTPGFEQE 227
Cdd:cd05349 156 AKAALLGFTRNMAKELGPYGITVNMVSGgllKVTDASAATPK 197
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
40-211 6.52e-18

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: 81.13  E-value: 6.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSIL-ARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPIDV 114
Cdd:cd05324   3 ALVTGANRGIGFEIVRQLAKSGPGTVILtARDVERGQAAVEKLR-AEGLSVRFHQLDVTDDASIEAAADfveeKYGGLDI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQGVFiGKELEKQSP--EEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGiygyTAYSASKFG 192
Cdd:cd05324  82 LVNNAGIA-FKGFDDSTPtrEQARETMKTNFFGTVDVTQALLPLLKKSPA---GRIVNVSSGLGSLT----SAYGVSKAA 153
                       170
                ....*....|....*....
gi 15239681 193 LQGLAQALQQEVISDGIHV 211
Cdd:cd05324 154 LNALTRILAKELKETGIKV 172
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
39-287 6.81e-18

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: 81.56  E-value: 6.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  39 HVFITGGSSGIGLALAHRAVSEG--AKVSILARSTEKLAEAKRSIQlaTGVEVATFSADVRDYDAVSK---AIDESGP-I 112
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEELR--PGLRVTTVKADLSDAAGVEQlleAIRKLDGeR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 113 DVLIVNQGVF--IGKeLEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGpaSISLVSSQAGQAGIYGYTAYSASK 190
Cdd:cd05367  79 DLLINNAGSLgpVSK-IEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKK--TVVNVSSGAAVNPFKGWGLYCSSK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 191 FGLQGLAQALQQEvisdgihvtllfppdtdtpgfEQELKkrpeltsIIAASSGSMKTNEVAKIC-----------FDGIK 259
Cdd:cd05367 156 AARDMFFRVLAAE---------------------EPDVR-------VLSYAPGVVDTDMQREIRetsadpetrsrFRSLK 207
                       250       260
                ....*....|....*....|....*....
gi 15239681 260 AGKFTVTCHFIG-FLLSIASTGMSPQGSF 287
Cdd:cd05367 208 EKGELLDPEQSAeKLANLLEKDKFESGAH 236
PRK07069 PRK07069
short chain dehydrogenase; Validated
41-231 8.36e-18

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 81.29  E-value: 8.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEA-KRSIQLATGVEVA-TFSADVRDYD----AVSKAIDESGPIDV 114
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAfAAEINAAHGEGVAfAAVQDVTDEAqwqaLLAQAADAMGGLSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:PRK07069  83 LVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRA---SQPASIVNISSVAAFKAEPDYTAYNASKAAVA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15239681  195 GLAQAL-------QQEVISDGIHVTLLfppdtDTP---GFEQELKKR 231
Cdd:PRK07069 160 SLTKSIaldcarrGLDVRCNSIHPTFI-----RTGivdPIFQRLGEE 201
PRK07774 PRK07774
SDR family oxidoreductase;
42-221 9.60e-18

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 81.33  E-value: 9.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqLATGVEVATFSADVRDYDAV----SKAIDESGPIDVLIV 117
Cdd:PRK07774  11 VTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQI-VADGGTAIAVQVDVSDPDSAkamaDATVSAFGGIDYLVN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEV----KFMiDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAgqAGIYGyTAYSASKFGL 193
Cdd:PRK07774  90 NAAIYGGMKLDLLITVPWdyykKFM-SVNLDGALVCTRAVYKHMAKRGG---GAIVNQSSTA--AWLYS-NFYGLAKVGL 162
                        170       180
                 ....*....|....*....|....*...
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK07774 163 NGLTQQLARELGGMNIRVNAIAPGPIDT 190
PRK07062 PRK07062
SDR family oxidoreductase;
33-211 1.22e-17

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 81.24  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   33 IPIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLA-TGVEVATFSADVRDYDAVSKAIDES-- 109
Cdd:PRK07062   4 IQLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKfPGARLLAARCDVLDEADVAAFAAAVea 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  110 --GPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYS 187
Cdd:PRK07062  84 rfGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAA---ASIVCVNSLLALQPEPHMVATS 160
                        170       180
                 ....*....|....*....|....
gi 15239681  188 ASKFGLQGLAQALQQEVISDGIHV 211
Cdd:PRK07062 161 AARAGLLNLVKSLATELAPKGVRV 184
PRK07856 PRK07856
SDR family oxidoreductase;
38-203 1.36e-17

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 80.75  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsiqlatGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:PRK07856   7 RVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETVD---------GRPAEFHAADVRDPDQVAALVDaiveRHGRLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK07856  78 VLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGGG--SIVNIGSVSGRRPSPGTAAYGAAKAGL 155
                        170
                 ....*....|
gi 15239681  194 QGLAQALQQE 203
Cdd:PRK07856 156 LNLTRSLAVE 165
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
38-216 1.44e-17

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 80.57  E-value: 1.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTE---KLA----EAKRSIQLATGVEVATfSADVRDYD----AVSKAI 106
Cdd:cd09762   4 KTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpKLPgtiyTAAEEIEAAGGKALPC-IVDIRDEDqvraAVEKAV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 107 DESGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKarEGRGPASISLVSSQAGQAGIYG-YTA 185
Cdd:cd09762  83 EKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLK--KSKNPHILNLSPPLNLNPKWFKnHTA 160
                       170       180       190
                ....*....|....*....|....*....|.
gi 15239681 186 YSASKFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:cd09762 161 YTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK06701 PRK06701
short chain dehydrogenase; Provisional
40-222 1.81e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 81.23  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLA-EAKRSIQlATGVEVATFSADVRD----YDAVSKAIDESGPIDV 114
Cdd:PRK06701  49 ALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDAnETKQRVE-KEGVKCLLIPGDVSDeafcKDAVEETVRELGRLDI 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQGVFIGKE-LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaregRGPASISLVSsqagqagIYGYTA------YS 187
Cdd:PRK06701 128 LVNNAAFQYPQQsLEDITAEQLDKTFKTNIYSYFHMTKAALPHLK----QGSAIINTGS-------ITGYEGnetlidYS 196
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15239681  188 ASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK06701 197 ATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTP 231
PRK06172 PRK06172
SDR family oxidoreductase;
42-240 2.49e-17

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 80.18  E-value: 2.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGvEVATFSADV-RDYDA---VSKAIDESGPIDVLIV 117
Cdd:PRK06172  12 VTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGG-EALFVACDVtRDAEVkalVEQTIAAYGRLDYAFN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGK-ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:PRK06172  91 NAGIEIEQgRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLA---QGGGAIVNTASVAGLGAAPKMSIYAASKHAVIGL 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15239681  197 AQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSIIAA 240
Cdd:PRK06172 168 TKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEADPRKAEFAAA 211
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
41-203 4.15e-17

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 79.72  E-value: 4.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPIDVLI 116
Cdd:PRK07097  14 LITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYR-ELGIEAHGYVCDVTDEDGVQAMVSqiekEVGVIDILV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  117 VNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:PRK07097  93 NNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIK---KGHGKIINICSMMSELGRETVSAYAAAKGGLKML 169

                 ....*..
gi 15239681  197 AQALQQE 203
Cdd:PRK07097 170 TKNIASE 176
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
40-222 4.21e-17

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 79.77  E-value: 4.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLA-EAKRSIQLATGvEVATFSADVRDYDAV----SKAIDESGPIDV 114
Cdd:PRK08936  10 VVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEAnDVAEEIKKAGG-EAIAVKGDVTVESDVvnliQTAVKEFGTLDV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:PRK08936  89 MINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIKG--NIINMSSVHEQIPWPLFVHYAASKGGVK 166
                        170       180
                 ....*....|....*....|....*...
gi 15239681  195 GLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK08936 167 LMTETLAMEYAPKGIRVNNIGPGAINTP 194
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
42-226 5.03e-17

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: 79.20  E-value: 5.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVSIlarsTEKLAEAKRSIQLATGVEVATFSADVRDYD----AVSKAIDESGPIDVLIV 117
Cdd:cd05363   8 ITGSARGIGRAFAQAYVREGARVAI----ADINLEAARATAAEIGPAACAISLDVTDQAsidrCVAALVDRWGSIDILVN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKArEGRGPASISLvSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:cd05363  84 NAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIA-QGRGGKIINM-ASQAGRRGEALVGVYCATKAAVISLT 161
                       170       180
                ....*....|....*....|....*....
gi 15239681 198 QALQQEVISDGIHVTLLFPPDTDTPGFEQ 226
Cdd:cd05363 162 QSAGLNLIRHGINVNAIAPGVVDGEHWDG 190
PRK06123 PRK06123
SDR family oxidoreductase;
42-221 6.30e-17

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 79.05  E-value: 6.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVS---KAIDES-GPIDVLIV 117
Cdd:PRK06123   7 ITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLrlfEAVDRElGRLDALVN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGK-ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPASISLVSSQAGQAGIYG-YTAYSASKFGLQG 195
Cdd:PRK06123  87 NAGILEAQmRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRGGAIVNVSSMAARLGSPGeYIDYAASKGAIDT 166
                        170       180
                 ....*....|....*....|....*.
gi 15239681  196 LAQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK06123 167 MTIGLAKEVAAEGIRVNAVRPGVIYT 192
PRK06114 PRK06114
SDR family oxidoreductase;
41-236 8.83e-17

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 78.67  E-value: 8.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILA-RSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPIDVL 115
Cdd:PRK06114  12 FVTGAGSGIGQRIAIGLAQAGADVALFDlRTDDGLAETAEHIE-AAGRRAIQIAADVTSKADLRAAVArteaELGALTLA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGP----ASISLVSSQAG--QAgiygytAYSAS 189
Cdd:PRK06114  91 VNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLEN-GGGSivniASMSGIIVNRGllQA------HYNAS 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFPPDTDTPgfeqeLKKRPELTS 236
Cdd:PRK06114 164 KAGVIHLSKSLAMEWVGRGIRVNSISPGYTATP-----MNTRPEMVH 205
PRK07041 PRK07041
SDR family oxidoreductase;
42-222 3.27e-16

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 76.61  E-value: 3.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEvaTFSADVRDYDAVSKAIDESGPIDVLIVNQGV 121
Cdd:PRK07041   2 VVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPVR--TAALDITDEAAVDAFFAEAGPFDHVVITAAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  122 FIGKELEKQSPEEVKFMIDVNLTGSFNVIKAAlpamKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQGLAQALQ 201
Cdd:PRK07041  80 TPGGPVRALPLAAAQAAMDSKFWGAYRVARAA----RIAPG---GSLTFVSGFAAVRPSASGVLQGAINAALEALARGLA 152
                        170       180
                 ....*....|....*....|.
gi 15239681  202 QEVISdgIHVTLLFPPDTDTP 222
Cdd:PRK07041 153 LELAP--VRVNTVSPGLVDTP 171
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
40-222 3.33e-16

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 76.54  E-value: 3.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVsilarstekLAEAKRSIQLATGvEVATFSADVRDydAVSKAIDESGPIDVLIVNQ 119
Cdd:PRK06550   8 VLITGAASGIGLAQARAFLAQGAQV---------YGVDKQDKPDLSG-NFHFLQLDLSD--DLEPLFDWVPSVDILCNTA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  120 GVFIG-KELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGP----ASISlvSSQAGQAGIygytAYSASKFGLQ 194
Cdd:PRK06550  76 GILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLER-KSGIiinmCSIA--SFVAGGGGA----AYTASKHALA 148
                        170       180
                 ....*....|....*....|....*...
gi 15239681  195 GLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK06550 149 GFTKQLALDYAKDGIQVFGIAPGAVKTP 176
PRK06398 PRK06398
aldose dehydrogenase; Validated
40-200 3.71e-16

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 76.79  E-value: 3.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILarsteklaeakrSIQLATGVEVATFSADVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK06398   9 AIVTGGSQGIGKAVVNRLKEEGSNVINF------------DIKEPSYNDVDYFKVDVSNKEQVIKGIDYViskyGRIDIL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPASISLVSSQAGQAGIygyTAYSASKFGLQG 195
Cdd:PRK06398  77 VNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNA---AAYVTSKHAVLG 153

                 ....*
gi 15239681  196 LAQAL 200
Cdd:PRK06398 154 LTRSI 158
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
42-222 3.95e-16

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: 76.73  E-value: 3.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVsILARSTEKLAEAkrsiqLATGV---EVATFSADVRDYDAVSKAIDES----GPIDV 114
Cdd:cd05326   9 ITGGASGIGEATARLFAKHGARV-VIADIDDDAGQA-----VAAELgdpDISFVHCDVTVEADVRAAVDTAvarfGRLDI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQGVfIGK---ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGpaSISLVSSQAGQAGIYGYTAYSASKF 191
Cdd:cd05326  83 MFNNAGV-LGApcySILETSLEEFERVLDVNVYGAFLGTKHAARVM-IPAKKG--SIVSVASVAGVVGGLGPHAYTASKH 158
                       170       180       190
                ....*....|....*....|....*....|.
gi 15239681 192 GLQGLAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:cd05326 159 AVLGLTRSAATELGEHGIRVNCVSPYGVATP 189
PRK06057 PRK06057
short chain dehydrogenase; Provisional
42-233 4.01e-16

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 76.69  E-value: 4.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILArsteklAEAKRSIQLATGVEVATFSADVRDYDAV----SKAIDESGPIDVLIV 117
Cdd:PRK06057  12 ITGGGSGIGLATARRLAAEGATVVVGD------IDPEAGKAAADEVGGLFVPTDVTDEDAVnalfDTAAETYGSVDIAFN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKE--LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaREGRGpASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK06057  86 NAGISPPEDdsILNTGLDAWQRVQDVNLTSVYLCCKAALPHMV-RQGKG-SIINTASFVAVMGSATSQISYTASKGGVLA 163
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15239681  196 LAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPE 233
Cdd:PRK06057 164 MSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKDPE 201
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
40-209 5.50e-16

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 78.81  E-value: 5.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVAT-FSADVRDYDAVSKAID----ESGPIDV 114
Cdd:COG3347 428 ALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADAVDaTDVDVTAEAAVAAAFGfaglDIGGSDI 507
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQGVFIGKELEKQSPE-EVKFMiDVNLTGSFNVIKAALPAMKaREGRGPASISLVSSQAGQAGiYGYTAYSASKFGL 193
Cdd:COG3347 508 GVANAGIASSSPEEETRLSfWLNNF-AHLSTGQFLVARAAFQGTG-GQGLGGSSVFAVSKNAAAAA-YGAAAAATAKAAA 584
                       170
                ....*....|....*.
gi 15239681 194 QGLAQALQQEVISDGI 209
Cdd:COG3347 585 QHLLRALAAEGGANGI 600
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
34-216 7.00e-16

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 76.04  E-value: 7.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  34 PIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADV---RDYDA-VSKAIDES 109
Cdd:cd08936   7 PLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQ-GEGLSVTGTVCHVgkaEDRERlVATAVNLH 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 110 GPIDVLIVNQGV--FIGKELEkqSPEEV-KFMIDVNLTGSFNVIKAALPAMkarEGRGPASISLVSSQAGQAGIYGYTAY 186
Cdd:cd08936  86 GGVDILVSNAAVnpFFGNILD--STEEVwDKILDVNVKATALMTKAVVPEM---EKRGGGSVVIVSSVAAFHPFPGLGPY 160
                       170       180       190
                ....*....|....*....|....*....|
gi 15239681 187 SASKFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:cd08936 161 NVSKTALLGLTKNLAPELAPRNIRVNCLAP 190
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
38-216 7.40e-16

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 75.72  E-value: 7.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLaeakRSIQLATGVEVATFSADVRDYDAVS----KAIDESGPID 113
Cdd:PRK12936   7 RKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKL----EALAAELGERVKIFPANLSDRDEVKalgqKAEADLEGVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAAL-PAMKAREGRgpasISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:PRK12936  83 ILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGR----IINITSVVGVTGNPGQANYCASKAG 158
                        170       180
                 ....*....|....*....|....
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK12936 159 MIGFSKSLAQEIATRNVTVNCVAP 182
PRK07577 PRK07577
SDR family oxidoreductase;
38-255 7.89e-16

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 75.53  E-value: 7.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTeklaeakrsIQLATGVEVATFSADVRDYDAVSKAIDESGPIDVLIV 117
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQVIGIARSA---------IDDFPGELFACDLADIEQTAATLAQINEIHPVDAIVN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKARE-GRgpasISLVSSQAGQaGIYGYTAYSASKFGLQGL 196
Cdd:PRK07577  75 NVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREqGR----IVNICSRAIF-GALDRTSYSAAKSALVGC 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239681  197 AQALQQEVISDGIHVTLLFPPDTDTPGFEQ------ELKKRpELTSIIAASSGsmKTNEVAK-ICF 255
Cdd:PRK07577 150 TRTWALELAEYGITVNAVAPGPIETELFRQtrpvgsEEEKR-VLASIPMRRLG--TPEEVAAaIAF 212
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
40-216 1.29e-15

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 75.18  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIqlatGVEVATFSADVRDYDAVSKAIDESGP----IDVL 115
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDEL----GDNLYIAQLDVRNRAAIEEMLASLPAewrnIDVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKE-LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREgRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:PRK10538  79 VNNAGLALGLEpAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERN-HG--HIINIGSTAGSWPYAGGNVYGATKAFVR 155
                        170       180
                 ....*....|....*....|..
gi 15239681  195 GLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK10538 156 QFSLNLRTDLHGTAVRVTDIEP 177
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
35-216 3.00e-15

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 74.03  E-value: 3.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSiqLATGVEVATFSADVRDYDAVSKAIDESG---- 110
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKT--LSKYGNIHYVVGDVSSTESARNVIEKAAkvln 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  111 PIDVLIVNQGVFIGKELEkqSPEEVKFMIDVNLTGSFNVIKAALPAMkaREGrgpASISLVSSqagQAGIYG----YTAY 186
Cdd:PRK05786  81 AIDGLVVTVGGYVEDTVE--EFSGLEEMLTNHIKIPLYAVNASLRFL--KEG---SSIVLVSS---MSGIYKaspdQLSY 150
                        170       180       190
                 ....*....|....*....|....*....|
gi 15239681  187 SASKFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK05786 151 AVAKAGLAKAVEILASELLGRGIRVNGIAP 180
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
40-229 3.62e-15

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: 73.93  E-value: 3.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLA-EAKRSIQlATGVEVATFSADVRDYDAVSKAIDE----SGPIDV 114
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAaEVAAEIE-ELGGKAVVVRADVSQPQDVEEMFAAvkerFGRLDV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVN--QGVFigKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkaREGRGPASISLVSSQAGQAGIyGYTAYSASKFG 192
Cdd:cd05359  80 LVSNaaAGAF--RPLSELTPAHWDAKMNTNLKALVHCAQQAAKLM--RERGGGRIVAISSLGSIRALP-NYLAVGTAKAA 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15239681 193 LQGLAQALQQEVISDGIHVTLLFPPDTDT------PGFEQELK 229
Cdd:cd05359 155 LEALVRYLAVELGPRGIRVNAVSPGVIDTdalahfPNREDLLE 197
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
40-230 4.19e-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: 73.48  E-value: 4.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEG-AKVSILARSTEKLAEAKrsiQLATGVEVATF-SADVRDY-----DAVSKAIDESGpI 112
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELA---ALGASHSRLHIlELDVTDEiaesaEAVAERLGDAG-L 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 113 DVLIVNQGVFI-GKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAG---IYGYTAYSA 188
Cdd:cd05325  77 DVLINNAGILHsYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLK---GARAKIINISSRVGSIGdntSGGWYSYRA 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15239681 189 SKFGLQGLAQALQQEVISDGIHVTLLFPP--DTDTPGFEQELKK 230
Cdd:cd05325 154 SKAALNMLTKSLAVELKRDGITVVSLHPGwvRTDMGGPFAKNKG 197
PRK12743 PRK12743
SDR family oxidoreductase;
42-222 4.78e-15

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 73.53  E-value: 4.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAID----ESGPIDVLIV 117
Cdd:PRK12743   7 VTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDkliqRLGRIDVLVN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGPASISLVSSQAGQAGIyGYTAYSASKFGLQGLA 197
Cdd:PRK12743  87 NAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHM-VKQGQGGRIINITSVHEHTPLP-GASAYTAAKHALGGLT 164
                        170       180
                 ....*....|....*....|....*
gi 15239681  198 QALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK12743 165 KAMALELVEHGILVNAVAPGAIATP 189
PRK05867 PRK05867
SDR family oxidoreductase;
38-216 6.54e-15

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 73.15  E-value: 6.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:PRK05867  10 KRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIG-TSGGKVVPVCCDVSQHQQVTSMLDqvtaELGGID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGPASISLVSSQAGQAGIYGYTA-YSASKFG 192
Cdd:PRK05867  89 IAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAM-VKQGQGGVIINTASMSGHIINVPQQVShYCASKAA 167
                        170       180
                 ....*....|....*....|....
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK05867 168 VIHLTKAMAVELAPHKIRVNSVSP 191
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
41-211 9.36e-15

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 72.69  E-value: 9.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILA-RSTEKLAEAKRSIQlATGVEVATFSADVRDYDA----VSKAIDESGPIDVL 115
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELR-ALGVEVIFFPADVADLSAheamLDAAQAAWGRIDCL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGK--ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPA---SISLVSSQAGQAGIYGYTAYSASK 190
Cdd:PRK12745  85 VNNAGVGVKVrgDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEELphrSIVFVSSVNAIMVSPNRGEYCISK 164
                        170       180
                 ....*....|....*....|.
gi 15239681  191 FGLQGLAQALQQEVISDGIHV 211
Cdd:PRK12745 165 AGLSMAAQLFAARLAEEGIGV 185
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
40-214 1.01e-14

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 72.81  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsiQLAT--GVEVATFSADVRDYDAVSKAIDES-----GPI 112
Cdd:PRK08642   8 VLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAE-----ALADelGDRAIALQADVTDREQVQAMFATAtehfgKPI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  113 DVLIVNQGV---FIG---KELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAR-EGRgpasISLVSSQAGQAGIYGYTA 185
Cdd:PRK08642  83 TTVVNNALAdfsFDGdarKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQgFGR----IINIGTNLFQNPVVPYHD 158
                        170       180
                 ....*....|....*....|....*....
gi 15239681  186 YSASKFGLQGLAQALQQEVISDGIHVTLL 214
Cdd:PRK08642 159 YTTAKAALLGLTRNLAAELGPYGITVNMV 187
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
42-226 1.23e-14

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: 72.42  E-value: 1.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKV---SILARSTEKLAEAKRSIQLATGVEVaTFSADVRdyDAVSKAIDESGPIDVLIVN 118
Cdd:cd05345  10 VTGAGSGFGEGIARRFAQEGARVviaDINADGAERVAADIGEAAIAIQADV-TKRADVE--AMVEAALSKFGRLDILVNN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 119 QGV-FIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkarEGRGPASISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:cd05345  87 AGItHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHM---EEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVTAT 163
                       170       180
                ....*....|....*....|....*....
gi 15239681 198 QALQQEVISDGIHVTLLFPPDTDTPGFEQ 226
Cdd:cd05345 164 KAMAVELAPRNIRVNCLCPVAGETPLLSM 192
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
42-225 1.40e-14

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: 72.50  E-value: 1.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADV---RDYDAVSKAIDES-GPIDVLIV 117
Cdd:cd05322   7 VIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADAtneQSVIALSKGVDEIfKRVDLLVY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:cd05322  87 SAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIQG--RIIQINSKSGKVGSKHNSGYSAAKFGGVGLT 164
                       170       180
                ....*....|....*....|....*....
gi 15239681 198 QALQQEVISDGIHVTLLFPPD-TDTPGFE 225
Cdd:cd05322 165 QSLALDLAEHGITVNSLMLGNlLKSPMFQ 193
PRK09730 PRK09730
SDR family oxidoreductase;
42-216 1.86e-14

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 71.80  E-value: 1.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYD---AVSKAID-ESGPIDVLIV 117
Cdd:PRK09730   6 VTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENqvvAMFTAIDqHDEPLAALVN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGV-FIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPASISLVSSQAGQAGIYG-YTAYSASKFGLQG 195
Cdd:PRK09730  86 NAGIlFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSGGAIVNVSSAASRLGAPGeYVDYAASKGAIDT 165
                        170       180
                 ....*....|....*....|.
gi 15239681  196 LAQALQQEVISDGIHVTLLFP 216
Cdd:PRK09730 166 LTTGLSLEVAAQGIRVNCVRP 186
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
38-203 2.13e-14

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 71.83  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATF-----SADVRDYDAVSKAI-DESGP 111
Cdd:PRK08945  13 RIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIpldllTATPQNYQQLADTIeEQFGR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  112 IDVLIVNQGVfIGK--ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSAS 189
Cdd:PRK08945  93 LDGVLHNAGL-LGElgPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPA---ASLVFTSSSVGRQGRANWGAYAVS 168
                        170
                 ....*....|....
gi 15239681  190 KFGLQGLAQALQQE 203
Cdd:PRK08945 169 KFATEGMMQVLADE 182
PRK06128 PRK06128
SDR family oxidoreductase;
38-250 2.19e-14

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 72.58  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKlAEAKRSIQL--ATGVEVATFSADVRD----YDAVSKAIDESGP 111
Cdd:PRK06128  56 RKALITGADSGIGRATAIAFAREGADIALNYLPEEE-QDAAEVVQLiqAEGRKAVALPGDLKDeafcRQLVERAVKELGG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  112 IDVLIVNQG--VFIgKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregrGPASISLVSSQAGQAGIyGYTAYSAS 189
Cdd:PRK06128 135 LDILVNIAGkqTAV-KDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPP----GASIINTGSIQSYQPSP-TLLDYAST 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  190 KFGLQGLAQALQQEVISDGIHV---------TLLFP----PDTDTPGFEQELK-KRP-------ELTSIIAASSGSMKTN 248
Cdd:PRK06128 209 KAAIVAFTKALAKQVAEKGIRVnavapgpvwTPLQPsggqPPEKIPDFGSETPmKRPgqpvemaPLYVLLASQESSYVTG 288

                 ..
gi 15239681  249 EV 250
Cdd:PRK06128 289 EV 290
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
40-228 2.90e-14

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: 70.24  E-value: 2.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGA-KVSILARsteklaeakrsiqlatgvevatfsadvRDYDAVSKAIDESGPIDVLIvn 118
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGSpKVLVVSR---------------------------RDVVVHNAAILDDGRLIDLT-- 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 119 qgvfigkeleKQSPEEVkfmIDVNLTGSFNVIKAALPAMKARegrGPASISLVSSQAGQAGIYGYTAYSASKFGLQGLAQ 198
Cdd:cd02266  52 ----------GSRIERA---IRANVVGTRRLLEAARELMKAK---RLGRFILISSVAGLFGAPGLGGYAASKAALDGLAQ 115
                       170       180       190
                ....*....|....*....|....*....|
gi 15239681 199 ALQQEVISDGIHVTLLFPPDTDTPGFEQEL 228
Cdd:cd02266 116 QWASEGWGNGLPATAVACGTWAGSGMAKGP 145
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
35-216 3.16e-14

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: 71.72  E-value: 3.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAIDES----G 110
Cdd:cd08935   3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEIT-ALGGRAIALAADVLDRASLERAREEIvaqfG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 111 PIDVLIVNQG--------------VFIGKELEKQSPEEVKFMIDVNLTGSFnvikaaLPAM---KAREGRGPASISLVSS 173
Cdd:cd08935  82 TVDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSF------LPSQvfgKDMLEQKGGSIINISS 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15239681 174 QAGQAGIYGYTAYSASKFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:cd08935 156 MNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAP 198
PRK08589 PRK08589
SDR family oxidoreductase;
42-222 3.99e-14

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 71.35  E-value: 3.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVsILARSTEKLAEAKRSIQLATGvEVATFSADVRDYDAV----SKAIDESGPIDVLIV 117
Cdd:PRK08589  11 ITGASTGIGQASAIALAQEGAYV-LAVDIAEAVSETVDKIKSNGG-KAKAYHVDISDEQQVkdfaSEIKEQFGRVDVLFN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEV-KFMIDVNLTGSFNVIKAALPAMKAREGrgpaSISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:PRK08589  89 NAGVDNAAGRIHEYPVDVfDKIMAVDMRGTFLMTKMLLPLMMEQGG----SIINTSSFSGQAADLYRSGYNAAKGAVINF 164
                        170       180
                 ....*....|....*....|....*.
gi 15239681  197 AQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK08589 165 TKSIAIEYGRDGIRANAIAPGTIETP 190
PRK08017 PRK08017
SDR family oxidoreductase;
40-216 4.94e-14

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 70.89  E-value: 4.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAeakRSIQLA-TGVEVatfsaDVRDYDAVSKAIDE-----SGPID 113
Cdd:PRK08017   5 VLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVA---RMNSLGfTGILL-----DLDDPESVERAADEvialtDNRLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAR-EGRgpasISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:PRK08017  77 GLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHgEGR----IVMTSSVMGLISTPGRGAYAASKYA 152
                        170       180
                 ....*....|....*....|....
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK08017 153 LEAWSDALRMELRHSGIKVSLIEP 176
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
40-211 5.18e-14

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 71.08  E-value: 5.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKA----IDESGPIDVL 115
Cdd:PRK08277  13 AVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIK-AAGGEALAVKADVLDKESLEQArqqiLEDFGPCDIL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 I------VNQGVFIGKELEKQSP---------EEVKFMIDVNLTGSFnvikaaLPAM---KAREGRGPASISLVSSQAGQ 177
Cdd:PRK08277  92 IngaggnHPKATTDNEFHELIEPtktffdldeEGFEFVFDLNLLGTL------LPTQvfaKDMVGRKGGNIINISSMNAF 165
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15239681  178 AGIYGYTAYSASKFGLQGLAQALQQEVISDGIHV 211
Cdd:PRK08277 166 TPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRV 199
PRK05993 PRK05993
SDR family oxidoreductase;
38-216 5.53e-14

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 70.83  E-value: 5.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKrsiqlATGVEvaTFSADVRDYDAVSKAIDE-----SGPI 112
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALE-----AEGLE--AFQLDYAEPESIAALVAQvlelsGGRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  113 DVLIvNQGVFiGK--ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAR-EGRgpasISLVSSQAGQAGIYGYTAYSAS 189
Cdd:PRK05993  78 DALF-NNGAY-GQpgAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQgQGR----IVQCSSILGLVPMKYRGAYNAS 151
                        170       180
                 ....*....|....*....|....*..
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK05993 152 KFAIEGLSLTLRMELQGSGIHVSLIEP 178
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
40-254 6.62e-14

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: 70.64  E-value: 6.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDES----GPIDVL 115
Cdd:cd08933  12 VIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDVTKEEDIKTLISVTverfGRIDCL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVF-IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpaSISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:cd08933  92 VNNAGWHpPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQG----NIINLSSLVGSIGQKQAAPYVATKGAIT 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239681 195 GLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKRPELTSII-----AASSGSMKT-NEVAKIC 254
Cdd:cd08933 168 AMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATIkegelAQLLGRMGTeAESGLAA 233
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
40-240 8.10e-14

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: 69.61  E-value: 8.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEklAEAKRSIQ--LATGVEVATFSADVRDYDA----VSKAIDESGPID 113
Cdd:cd05357   3 ALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSE--AEAQRLKDelNALRNSAVLVQADLSDFAAcadlVAAAFRAFGRCD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKarEGRGPASISLVSSQAGQaGIYGYTAYSASKFGL 193
Cdd:cd05357  81 VLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLA--GSRNGSIINIIDAMTDR-PLTGYFAYCMSKAAL 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 194 QGLAQALQQEV--------ISDGihvTLLFPPDTDTPGFEQELKK-----RPELTSIIAA 240
Cdd:cd05357 158 EGLTRSAALELapnirvngIAPG---LILLPEDMDAEYRENALRKvplkrRPSAEEIADA 214
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
40-231 1.06e-13

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: 69.67  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAID----ESGPIDVL 115
Cdd:cd08930   5 ILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIEsyleKFGRIDIL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGV---FIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaREGRGpaSISLVSSQAGQAG----IYGYTA--- 185
Cdd:cd08930  85 INNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFK-KQGKG--SIINIASIYGVIApdfrIYENTQmys 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15239681 186 ---YSASKFGLQGLAQALQQEVISDGIHVTLLFP---PDTDTPGFEQELKKR 231
Cdd:cd08930 162 pveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPggiLNNQPSEFLEKYTKK 213
PRK09135 PRK09135
pteridine reductase; Provisional
40-203 1.25e-13

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 69.57  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAkrsiqLATGVE------VATFSADVRDYDA----VSKAIDES 109
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADA-----LAAELNalrpgsAAALQADLLDPDAlpelVAACVAAF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  110 GPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAgIYGYTAYSAS 189
Cdd:PRK09135  84 GRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRG---AIVNITDIHAERP-LKGYPVYCAA 159
                        170
                 ....*....|....
gi 15239681  190 KFGLQGLAQALQQE 203
Cdd:PRK09135 160 KAALEMLTRSLALE 173
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
38-253 1.35e-13

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 69.33  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEK----LAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDESGPID 113
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKeltkLAEQYNSNLTFHSLDLQDVHELETNFNEILSSIQEDNVSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIG--KELEKQSPEEVKFMIDVNLTGSfnVIKAALPAMKAREGRGPASISLVSSQAGQAGIYGYTAYSASKF 191
Cdd:PRK06924  82 IHLINNAGMVApiKPIEKAESEELITNVHLNLLAP--MILTSTFMKHTKDWKVDKRVINISSGAAKNPYFGWSAYCSSKA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239681  192 GLQglaqalqqevisdgihvtlLFppdTDTPGFEQELKKRPelTSIIAASSGSMKTNEVAKI 253
Cdd:PRK06924 160 GLD-------------------MF---TQTVATEQEEEEYP--VKIVAFSPGVMDTNMQAQI 197
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
40-211 1.76e-13

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 69.27  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILarsteKLAEAKRSIQLATGVEVatfsaDVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK06171  12 IIVTGGSSGIGLAIVKELLANGANVVNA-----DIHGGDGQHENYQFVPT-----DVSSAEEVNHTVAEIiekfGRIDGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKF---------MIDVNLTGSFNVIKAALPAM-KAREGrgpaSISLVSSQAGQAGIYGYTA 185
Cdd:PRK06171  82 VNNAGINIPRLLVDEKDPAGKYelneaafdkMFNINQKGVFLMSQAVARQMvKQHDG----VIVNMSSEAGLEGSEGQSC 157
                        170       180
                 ....*....|....*....|....*.
gi 15239681  186 YSASKFGLQGLAQALQQEVISDGIHV 211
Cdd:PRK06171 158 YAATKAALNSFTRSWAKELGKHNIRV 183
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
39-217 2.48e-13

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 69.24  E-value: 2.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  39 HVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsIQLATGVEVatFSADVRDYDAVSKAIDEsgpIDVlIVN 118
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAAN----LAALPGVEF--VRGDLRDPEALAAALAG---VDA-VVH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 119 QGVFIGKELEkqSPEEvkfMIDVNLTGSFNVIKAALPAmkaregrGPASISLVSSqagqAGIYGY--------------T 184
Cdd:COG0451  71 LAAPAGVGEE--DPDE---TLEVNVEGTLNLLEAARAA-------GVKRFVYASS----SSVYGDgegpidedtplrpvS 134
                       170       180       190
                ....*....|....*....|....*....|...
gi 15239681 185 AYSASKFGLQGLAQALQQEvisDGIHVTLLFPP 217
Cdd:COG0451 135 PYGASKLAAELLARAYARR---YGLPVTILRPG 164
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
33-202 3.37e-13

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: 69.70  E-value: 3.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  33 IPIKFRHVF-ITGGSSGIGLALA-HRAVSEGAKVSILARSTEKLAEAKRSIQL----ATGVEVATFSADVRDYDAVSKAI 106
Cdd:cd08953 200 APLKPGGVYlVTGGAGGIGRALArALARRYGARLVLLGRSPLPPEEEWKAQTLaaleALGARVLYISADVTDAAAVRRLL 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 107 DE----SGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAAlpamkarEGRGPASISLVSSQAGQAGIYG 182
Cdd:cd08953 280 EKvrerYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQAL-------ADEPLDFFVLFSSVSAFFGGAG 352
                       170       180
                ....*....|....*....|
gi 15239681 183 YTAYSASKFGLQGLAQALQQ 202
Cdd:cd08953 353 QADYAAANAFLDAFAAYLRQ 372
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
40-210 3.41e-13

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 68.29  E-value: 3.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSaDVRDYDAVSKAIDESGPIDVLIVNQ 119
Cdd:cd08951  10 IFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLS-SLAETRKLADQVNAIGRFDAVIHNA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 120 GVFIGkELEKQSPEEVKFMIDVNLTGSFnVIKAALpamkaregRGPASISLVSSQ-------------AGQAGIYGYTAY 186
Cdd:cd08951  89 GILSG-PNRKTPDTGIPAMVAVNVLAPY-VLTALI--------RRPKRLIYLSSGmhrggnaslddidWFNRGENDSPAY 158
                       170       180
                ....*....|....*....|....*..
gi 15239681 187 SASKFGLQGLAQALQ---QEVISDGIH 210
Cdd:cd08951 159 SDSKLHVLTLAAAVArrwKDVSSNAVH 185
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
38-216 1.03e-12

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: 66.74  E-value: 1.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSiqLATGVEVATFSADVRDYDA----VSKAIDESGPID 113
Cdd:cd08942   7 KIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEE--LSAYGECIAIPADLSSEEGiealVARVAERSDRLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVFIGKELEkQSPEEV--KFMiDVNLTGSFNVIKAALPAM-KAREGRGPASISLVSSQAG--QAGIYGYtAYSA 188
Cdd:cd08942  85 VLVNNAGATWGAPLE-AFPESGwdKVM-DINVKSVFFLTQALLPLLrAAATAENPARVINIGSIAGivVSGLENY-SYGA 161
                       170       180
                ....*....|....*....|....*...
gi 15239681 189 SKFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:cd08942 162 SKAAVHQLTRKLAKELAGEHITVNAIAP 189
PRK05875 PRK05875
short chain dehydrogenase; Provisional
38-222 1.43e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 66.75  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSI-QLATGVEVATFSADVRDYDAVSKAIDES----GPI 112
Cdd:PRK05875   8 RTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIeALKGAGAVRYEPADVTDEDQVARAVDAAtawhGRL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  113 DVLIVNQGvfiGKE----LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGpaSISLVSSQAGQAGIYGYTAYSA 188
Cdd:PRK05875  88 HGVVHCAG---GSEtigpITQIDSDAWRRTVDLNVNGTMYVLKHAAREL-VRGGGG--SFVGISSIAASNTHRWFGAYGV 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15239681  189 SKFGLQGLAQALQQEV---------ISDGIHVTLLFPPDTDTP 222
Cdd:PRK05875 162 TKSAVDHLMKLAADELgpswvrvnsIRPGLIRTDLVAPITESP 204
PRK07814 PRK07814
SDR family oxidoreductase;
42-193 1.67e-12

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 66.34  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDA----VSKAIDESGPIDVLIV 117
Cdd:PRK07814  15 VTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIR-AAGRRAHVVAADLAHPEAtaglAGQAVEAFGRLDIVVN 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK07814  94 NVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGGG--SVINISSTMGRLAGRGFAAYGTAKAAL 167
PLN02253 PLN02253
xanthoxin dehydrogenase
42-216 2.32e-12

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 66.39  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSiqLATGVEVATFSADVRDYDAVSKAIDES----GPIDVLIV 117
Cdd:PLN02253  23 VTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDS--LGGEPNVCFFHCDVTVEDDVSRAVDFTvdkfGTLDIMVN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGK--ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PLN02253 101 NAGLTGPPcpDIRNVELSEFEKVFDVNVKGVFLGMKHAARIM-IPLKKG--SIVSLCSVASAIGGLGPHAYTGSKHAVLG 177
                        170       180
                 ....*....|....*....|.
gi 15239681  196 LAQALQQEVISDGIHVTLLFP 216
Cdd:PLN02253 178 LTRSVAAELGKHGIRVNCVSP 198
PRK12746 PRK12746
SDR family oxidoreductase;
41-253 3.12e-12

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 65.44  E-value: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSI-LARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAIDE----------S 109
Cdd:PRK12746  10 LVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIE-SNGGKAFLIEADLNSIDGVKKLVEQlknelqirvgT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  110 GPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKArEGRgpasISLVSSQAGQAGIYGYTAYSAS 189
Cdd:PRK12746  89 SEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRA-EGR----VINISSAEVRLGFTGSIAYGLS 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFPPDTDTpGFEQELKKRPELTSIIAASSGSMKTNEVAKI 253
Cdd:PRK12746 164 KGALNTMTLPLAKHLGERGITVNTIMPGYTKT-DINAKLLDDPEIRNFATNSSVFGRIGQVEDI 226
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
42-216 3.44e-12

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 65.53  E-value: 3.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVsILARSTEKLAEAKRSIQLAtGVEVATFSADVRDYDA----VSKAIDESGPIDVLIV 117
Cdd:PRK06935  20 VTGGNTGLGQGYAVALAKAGADI-IITTHGTNWDETRRLIEKE-GRKVTFVQVDLTKPESaekvVKEALEEFGKIDILVN 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGPAsISLVSSQAGQAGIYgYTAYSASKFGLQGLA 197
Cdd:PRK06935  98 NAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVM-AKQGSGKI-INIASMLSFQGGKF-VPAYTASKHGVAGLT 174
                        170
                 ....*....|....*....
gi 15239681  198 QALQQEVISDGIHVTLLFP 216
Cdd:PRK06935 175 KAFANELAAYNIQVNAIAP 193
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
40-230 5.66e-12

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: 64.99  E-value: 5.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVsiLARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKA-------IDESGpI 112
Cdd:cd09805   3 VLITGCDSGFGNLLAKKLDSLGFTV--LAGCLTKNGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAaqwvkehVGEKG-L 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 113 DVLIVNQGVFIGKELEKQSPEEV-KFMIDVNLTGSFNVIKAALPAMKAREGRgpasISLVSSQAGQAGIYGYTAYSASKF 191
Cdd:cd09805  80 WGLVNNAGILGFGGDEELLPMDDyRKCMEVNLFGTVEVTKAFLPLLRRAKGR----VVNVSSMGGRVPFPAGGAYCASKA 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15239681 192 GLQGLAQALQQEVISDGIHVTLLFP-----PDTDTPGFEQELKK 230
Cdd:cd09805 156 AVEAFSDSLRRELQPWGVKVSIIEPgnfktGITGNSELWEKQAK 199
PRK12744 PRK12744
SDR family oxidoreductase;
35-247 6.36e-12

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 64.76  E-value: 6.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   35 IKFRHVFITGGSSGIGLALAHRAVSEGAK-VSILARSTEKLAEAKRSIQL--ATGVEVATFSADVRDYDAVSK----AID 107
Cdd:PRK12744   6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKaVAIHYNSAASKADAEETVAAvkAAGAKAVAFQADLTTAAAVEKlfddAKA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  108 ESGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAAlpamkareGR----GPASISLVSSQAGqAGIYGY 183
Cdd:PRK12744  86 AFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEA--------GRhlndNGKIVTLVTSLLG-AFTPFY 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239681  184 TAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGF-EQELKKRPELTSIIAASSGSMKT 247
Cdd:PRK12744 157 SAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFFyPQEGAEAVAYHKTAAALSPFSKT 221
PRK05855 PRK05855
SDR family oxidoreductase;
40-221 9.04e-12

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 65.77  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIG----LALAHRavseGAKVSIlarSTEKLAEAKRSIQL--ATGVEVATFSADVRDYDAVSK----AIDES 109
Cdd:PRK05855 318 VVVTGAGSGIGretaLAFARE----GAEVVA---SDIDEAAAERTAELirAAGAVAHAYRVDVSDADAMEAfaewVRAEH 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  110 GPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAReGRGpASISLVSSQAGQAGIYGYTAYSAS 189
Cdd:PRK05855 391 GVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVER-GTG-GHIVNVASAAAYAPSRSLPAYATS 468
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK05855 469 KAAVLMLSECLRAELAAAGIGVTAICPGFVDT 500
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
42-211 2.32e-11

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: 62.87  E-value: 2.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDES----GPIDVLIV 117
Cdd:cd05337   6 VTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAwedfGRLDCLVN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQGVFIGK--ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGR--GP-ASISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:cd05337  86 NAGIAVRPrgDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRfdGPhRSIIFVTSINAYLVSPNRGEYCISKAG 165
                       170
                ....*....|....*....
gi 15239681 193 LQGLAQALQQEVISDGIHV 211
Cdd:cd05337 166 LSMATRLLAYRLADEGIAV 184
PRK05693 PRK05693
SDR family oxidoreductase;
40-211 3.45e-11

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 62.89  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsiqlatgVEVATFSA---DVRDYDAVSKAID----ESGPI 112
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEA----------LAAAGFTAvqlDVNDGAALARLAEeleaEHGGL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkaREGRG----PASIS--LVSSQAGqagiygytAY 186
Cdd:PRK05693  74 DVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLL--RRSRGlvvnIGSVSgvLVTPFAG--------AY 143
                        170       180
                 ....*....|....*....|....*
gi 15239681  187 SASKFGLQGLAQALQQEVISDGIHV 211
Cdd:PRK05693 144 CASKAAVHALSDALRLELAPFGVQV 168
PRK06101 PRK06101
SDR family oxidoreductase;
40-222 4.38e-11

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 62.19  E-value: 4.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKrsiqlATGVEVATFSADVRDYDAVSKAIDESGPI-DVLIVN 118
Cdd:PRK06101   4 VLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELH-----TQSANIFTLAFDVTDHPGTKAALSQLPFIpELWIFN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  119 QGvfiGKELEKQSPEEVKFM---IDVNLTGSFNVIKAALPAMKaregRGpASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK06101  79 AG---DCEYMDDGKVDATLMarvFNVNVLGVANCIEGIQPHLS----CG-HRVVIVGSIASELALPRAEAYGASKAAVAY 150
                        170       180
                 ....*....|....*....|....*..
gi 15239681  196 LAQALQQEVISDGIHVTLLFPPDTDTP 222
Cdd:PRK06101 151 FARTLQLDLRPKGIEVVTVFPGFVATP 177
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
38-216 5.03e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 62.08  E-value: 5.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVSKAID----ESGPID 113
Cdd:PRK08085  10 KNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLR-QEGIKAHAAPFNVTHKQEVEAAIEhiekDIGPID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPASISLVSSQAGQAGIygyTAYSASKFGL 193
Cdd:PRK08085  89 VLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTI---TPYAASKGAV 165
                        170       180
                 ....*....|....*....|...
gi 15239681  194 QGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK08085 166 KMLTRGMCVELARHNIQVNGIAP 188
PRK07985 PRK07985
SDR family oxidoreductase;
35-254 5.42e-11

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 62.32  E-value: 5.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSI--LARSTEKLAEAKRSIQLAtGVEVATFSADVRD----YDAVSKAIDE 108
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAIsyLPVEEEDAQDVKKIIEEC-GRKAVLLPGDLSDekfaRSLVHEAHKA 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  109 SGPIDVLIVNQGVFIG-KELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAregrGPASISLVSSQAGQAGIYgYTAYS 187
Cdd:PRK07985 126 LGGLDIMALVAGKQVAiPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPK----GASIITTSSIQAYQPSPH-LLDYA 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  188 ASKFGLQGLAQALQQEVISDGIHVTLLFP-------------PDTDTPGFEQE--LKK--RP-ELTSI---IAASSGSMK 246
Cdd:PRK07985 201 ATKAAILNYSRGLAKQVAEKGIRVNIVAPgpiwtalqisggqTQDKIPQFGQQtpMKRagQPaELAPVyvyLASQESSYV 280

                 ....*...
gi 15239681  247 TNEVAKIC 254
Cdd:PRK07985 281 TAEVHGVC 288
PRK06947 PRK06947
SDR family oxidoreductase;
40-221 7.31e-11

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 61.36  E-value: 7.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRD-------YDAVSKAIdesGPI 112
Cdd:PRK06947   5 VLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRAAGGRACVVAGDVANeadviamFDAVQSAF---GRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  113 DVLIVNQG-VFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAM-KAREGRGpASISLVSSQAGQAGI-YGYTAYSAS 189
Cdd:PRK06947  82 DALVNNAGiVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLsTDRGGRG-GAIVNVSSIASRLGSpNEYVDYAGS 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK06947 161 KGAVDTLTLGLAKELGPHGVRVNAVRPGLIET 192
PRK07791 PRK07791
short chain dehydrogenase; Provisional
38-216 9.97e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 61.61  E-value: 9.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSI------LARSTEKLAEAKRSIQ--LATGVEVATFSADVRDYDA----VSKA 105
Cdd:PRK07791   7 RVVIVTGAGGGIGRAHALAFAAEGARVVVndigvgLDGSASGGSAAQAVVDeiVAAGGEAVANGDDIADWDGaanlVDAA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  106 IDESGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIK--AALPAMKAREGRGP-ASISLVSSQAGQAGIYG 182
Cdd:PRK07791  87 VETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRhaAAYWRAESKAGRAVdARIINTSSGAGLQGSVG 166
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15239681  183 YTAYSASKFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PRK07791 167 QGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP 200
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
42-200 1.14e-10

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 62.16  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSIL--ARSTEKLAEakrsiqLATGVEVATFSADVRDYDAVSK----AIDESGPIDVL 115
Cdd:PRK08261 215 VTGAARGIGAAIAEVLARDGAHVVCLdvPAAGEALAA------VANRVGGTALALDITAPDAPARiaehLAERHGGLDIV 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:PRK08261 289 VHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDG---GRIVGVSSISGIAGNRGQTNYAASKAGVIG 365

                 ....*
gi 15239681  196 LAQAL 200
Cdd:PRK08261 366 LVQAL 370
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
38-200 1.97e-10

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: 60.29  E-value: 1.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiqlATGVEVATFSADVRDYDAVS----KAIDESGPID 113
Cdd:cd09761   2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAE----AEGPNLFFVHGDVADETLVKfvvyAMLEKLGRID 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRgpaSISLVSSQAGQAGIyGYTAYSASKFGL 193
Cdd:cd09761  78 VLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGR---IINIASTRAFQSEP-DSEAYAASKGGL 153

                ....*..
gi 15239681 194 QGLAQAL 200
Cdd:cd09761 154 VALTHAL 160
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
42-211 2.26e-10

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 60.12  E-value: 2.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSI-LARSTEKLAEAKRSIQlATGVEVATFSADVRDYDAVS---KAIDES-GPIDVLI 116
Cdd:PRK08063   9 VTGSSRGIGKAIALRLAEEGYDIAVnYARSRKAAEETAEEIE-ALGRKALAVKANVGDVEKIKemfAQIDEEfGRLDVFV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  117 VNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKarEGRGPASISLVSSQAGQAgIYGYTAYSASKFGLQGL 196
Cdd:PRK08063  88 NNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLME--KVGGGKIISLSSLGSIRY-LENYTTVGVSKAALEAL 164
                        170
                 ....*....|....*
gi 15239681  197 AQALQQEVISDGIHV 211
Cdd:PRK08063 165 TRYLAVELAPKGIAV 179
PRK08265 PRK08265
short chain dehydrogenase; Provisional
42-211 3.27e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 59.64  E-value: 3.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARsteklaEAKRSIQLATGV-EVATFSA-DVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK08265  11 VTGGATLIGAAVARALVAAGARVAIVDI------DADNGAAVAASLgERARFIAtDITDDAAIERAVATVvarfGRVDIL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKELeKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISL--VSSQAGQAGIYgytAYSASKFGL 193
Cdd:PRK08265  85 VNLACTYLDDGL-ASSRADWLAALDVNLVSAAMLAQAAHPHLARGGG---AIVNFtsISAKFAQTGRW---LYPASKAAI 157
                        170
                 ....*....|....*...
gi 15239681  194 QGLAQALQQEVISDGIHV 211
Cdd:PRK08265 158 RQLTRSMAMDLAPDGIRV 175
PRK07102 PRK07102
SDR family oxidoreductase;
40-262 4.96e-10

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 58.78  E-value: 4.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDESGP-IDVLIVN 118
Cdd:PRK07102   4 ILIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSTHELDILDTASHAAFLDSLPAlPDIVLIA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  119 QGVFIGKELEKQSPEEVKFMIDVNLTGSfnvikAALPAMKAR--EGRGPASISLVSSQAGQAG-----IYGytaysASKF 191
Cdd:PRK07102  84 VGTLGDQAACEADPALALREFRTNFEGP-----IALLTLLANrfEARGSGTIVGISSVAGDRGrasnyVYG-----SAKA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15239681  192 GLQGLAQALQQEVISDGIHVTLLFPPDTDTPgFEQELKKRPELTSiiaassgsmKTNEVAKICFDGIKAGK 262
Cdd:PRK07102 154 ALTAFLSGLRNRLFKSGVHVLTVKPGFVRTP-MTAGLKLPGPLTA---------QPEEVAKDIFRAIEKGK 214
PRK09291 PRK09291
SDR family oxidoreductase;
38-211 9.94e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 58.09  E-value: 9.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIG----LALAHRAVSEGAKVSILARSTEKLAEAKRSiqlatGVEVATFSADVRDYDAVSKAIDESgpID 113
Cdd:PRK09291   3 KTILITGAGSGFGrevaLRLARKGHNVIAGVQIAPQVTALRAEAARR-----GLALRVEKLDLTDAIDRAQAAEWD--VD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkAREGRGpaSISLVSSQAGQAGIYGYTAYSASKFGL 193
Cdd:PRK09291  76 VLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKM-VARGKG--KVVFTSSMAGLITGPFTGAYCASKHAL 152
                        170
                 ....*....|....*...
gi 15239681  194 QGLAQALQQEVISDGIHV 211
Cdd:PRK09291 153 EAIAEAMHAELKPFGIQV 170
PRK09186 PRK09186
flagellin modification protein A; Provisional
40-284 1.01e-09

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 58.08  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSA-DVRDYDAVSKAIDES----GPIDV 114
Cdd:PRK09186   7 ILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLVElDITDQESLEEFLSKSaekyGKIDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LiVN----QGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSqagqagIYGYTA----- 185
Cdd:PRK09186  87 A-VNcaypRNKDYGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGG---GNLVNISS------IYGVVApkfei 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  186 -----------YSASKFGLQGLAQALQQEVISDGIHVTLLFPP---DTDTPGFEQELKKRpeltsiiAASSGSMKTNEVa 251
Cdd:PRK09186 157 yegtsmtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGgilDNQPEAFLNAYKKC-------CNGKGMLDPDDI- 228
                        250       260       270
                 ....*....|....*....|....*....|...
gi 15239681  252 kicfdgikagkftvtCHFIGFLLSIASTGMSPQ 284
Cdd:PRK09186 229 ---------------CGTLVFLLSDQSKYITGQ 246
PRK05854 PRK05854
SDR family oxidoreductase;
27-196 1.37e-09

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 58.15  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   27 RPRSVTIP-IKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSI-QLATGVEVATFSADVRDYDAVSK 104
Cdd:PRK05854   3 KPLDITVPdLSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIrTAVPDAKLSLRALDLSSLASVAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  105 AID----ESGPIDVLIVNQGVFIGKelEKQSPE---EVKFmiDVNLTGSFNVIKAALPAMKAREGRgpaSISLVSSQAGQ 177
Cdd:PRK05854  83 LGEqlraEGRPIHLLINNAGVMTPP--ERQTTAdgfELQF--GTNHLGHFALTAHLLPLLRAGRAR---VTSQSSIAARR 155
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15239681  178 AGI----------Y-GYTAYSASK--FGLQGL 196
Cdd:PRK05854 156 GAInwddlnwersYaGMRAYSQSKiaVGLFAL 187
PRK07035 PRK07035
SDR family oxidoreductase;
41-221 1.43e-09

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 57.72  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   41 FITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATG--VEVATFSADVRDYDAVSKAIDES-GPIDVLIV 117
Cdd:PRK07035  12 LVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGkaEALACHIGEMEQIDALFAHIRERhGRLDILVN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGV--FIGKELEKqspEEVKF--MIDVNLTGSFNVIKAALPAMKArEGRGP----ASISLVSSQAGQaGIygytaYSAS 189
Cdd:PRK07035  92 NAAAnpYFGHILDT---DLGAFqkTVDVNIRGYFFMSVEAGKLMKE-QGGGSivnvASVNGVSPGDFQ-GI-----YSIT 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFPPDTDT 221
Cdd:PRK07035 162 KAAVISMTKAFAKECAPFGIRVNALLPGLTDT 193
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
40-216 2.23e-09

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: 57.19  E-value: 2.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYD---AVSKAIDESGPIDVLI 116
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDleaVVKATVSQFGGITILV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 117 VNQGVFIGKELE-KQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd05365  82 NNAGGGGPKPFDmPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGG---GAILNISSMSSENKNVRIAAYGSSKAAVNH 158
                       170       180
                ....*....|....*....|.
gi 15239681 196 LAQALQQEVISDGIHVTLLFP 216
Cdd:cd05365 159 MTRNLAFDLGPKGIRVNAVAP 179
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
40-222 2.49e-09

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: 56.05  E-value: 2.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEklaeakrsiqlatgvevaTFSADVRDYDAVSKAIDESGPIDVLIVNQ 119
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSG------------------DYQVDITDEASIKALFEKVGHFDAIVSTA 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 120 GVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKARegrgpASISLVSSQAGQAGIYGYTAYSASKFGLQGLAQA 199
Cdd:cd11731  63 GDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLNDG-----GSITLTSGILAQRPIPGGAAAATVNGALEGFVRA 137
                       170       180
                ....*....|....*....|...
gi 15239681 200 LQQEvISDGIHVTLLFPPDTDTP 222
Cdd:cd11731 138 AAIE-LPRGIRINAVSPGVVEES 159
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
38-223 3.04e-09

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 56.18  E-value: 3.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEklAEAKRSIqLATGVEVATFSADVrdydAVSKAIDESGPIDVLIV 117
Cdd:cd05334   2 RVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAEN--EEADASI-IVLDSDSFTEQAKQ----VVASVARLSGKVDALIC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQGVFIGKELEKQSP-EEVKFMIDVNLTGSFNVIKAALPAMKArEGRgpasISLVSSQAGQAGIYGYTAYSASKFGLQGL 196
Cdd:cd05334  75 VAGGWAGGSAKSKSFvKNWDLMWKQNLWTSFIASHLATKHLLS-GGL----LVLTGAKAALEPTPGMIGYGAAKAAVHQL 149
                       170       180
                ....*....|....*....|....*....
gi 15239681 197 AQALQQE--VISDGIHVTLLFPPDTDTPG 223
Cdd:cd05334 150 TQSLAAEnsGLPAGSTANAILPVTLDTPA 178
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
38-268 3.89e-09

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 56.25  E-value: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEG-AKVSILARSTE-KLAEAKRSIQLATGVEVATFSADVRDYDAVSKAIDES---GPI 112
Cdd:PRK07904   9 QTILLLGGTSEIGLAICERYLKNApARVVLAALPDDpRRDAAVAQMKAAGASSVEVIDFDALDTDSHPKVIDAAfagGDV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVikAALPAMKAREgRGPASISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:PRK07904  89 DVAIVAFGLLGDAEELWQNQRKAVQIAEINYTAAVSV--GVLLGEKMRA-QGFGQIIAMSSVAGERVRRSNFVYGSTKAG 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239681  193 LQGLAQALQQEVISDGIHVTLLFPPDTDTPgFEQELKKRPeLTsiiaassgsMKTNEVAKICFDGIKAGKFTVTCH 268
Cdd:PRK07904 166 LDGFYLGLGEALREYGVRVLVVRPGQVRTR-MSAHAKEAP-LT---------VDKEDVAKLAVTAVAKGKELVWAP 230
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
28-200 4.17e-09

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 56.71  E-value: 4.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   28 PRSVTIPIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDY---DAVSK 104
Cdd:PRK07792   3 RTTNTTDLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVLDEIRAAGAKAVAVAGDISQRataDELVA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  105 AIDESGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIK--AALPAMKAREGRGPASISLV--SSQAGQAGI 180
Cdd:PRK07792  83 TAVGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRnaAAYWRAKAKAAGGPVYGRIVntSSEAGLVGP 162
                        170       180
                 ....*....|....*....|....
gi 15239681  181 YGYTAYSASKFGLQGL----AQAL 200
Cdd:PRK07792 163 VGQANYGAAKAGITALtlsaARAL 186
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
40-188 4.21e-09

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 55.18  E-value: 4.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681     40 VFITGGSSGIGLALAHRAVSEGA-KVSILARSTEKLAEAKRSIQL--ATGVEVATFSADVRDYDAVSKAIDE----SGPI 112
Cdd:smart00822   3 YLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAEleAAGARVTVVACDVADRDALAAVLAAipavEGPL 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239681    113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALpamkareGRGPASISLVSSQAGQAGIYGYTAYSA 188
Cdd:smart00822  83 TGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTA-------DLPLDFFVLFSSIAGVLGSPGQANYAA 151
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
38-214 5.74e-09

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


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 56.62  E-value: 5.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAK-VSILARSTEKLAEAKRSIQL-ATGVEVATFSADVRDYDAVSKAIDE---SGPI 112
Cdd:cd05274 151 GTYLITGGLGGLGLLVARWLAARGARhLVLLSRRGPAPRAAARAALLrAGGARVSVVRCDVTDPAALAALLAElaaGGPL 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIkAALPamkareGRGPASISLVSSQAGQAGIYGYTAYSASKFG 192
Cdd:cd05274 231 AGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLH-ELTP------DLPLDFFVLFSSVAALLGGAGQAAYAAANAF 303
                       170       180
                ....*....|....*....|..
gi 15239681 193 LQGLAQALQqeviSDGIHVTLL 214
Cdd:cd05274 304 LDALAAQRR----RRGLPATSV 321
PRK12747 PRK12747
short chain dehydrogenase; Provisional
35-253 6.02e-09

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 55.85  E-value: 6.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDY---DAVSKAIDE--- 108
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLhgvEALYSSLDNelq 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  109 ----SGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkaregRGPASISLVSSQAGQAGIYGYT 184
Cdd:PRK12747  82 nrtgSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL-----RDNSRIINISSAATRISLPDFI 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15239681  185 AYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTpGFEQELKKRPELTSIIAASSGSMKTNEVAKI 253
Cdd:PRK12747 157 AYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKT-DMNAELLSDPMMKQYATTISAFNRLGEVEDI 224
PRK08703 PRK08703
SDR family oxidoreductase;
34-232 1.47e-08

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 54.55  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   34 PIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVAT-----FSADVRDYDAVSKAIDE 108
Cdd:PRK08703   3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAirfdlMSAEEKEFEQFAATIAE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  109 --SGPIDVLIVNQGVFIG-KELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaregRGP-ASISLVSSQAGQAGIYGYT 184
Cdd:PRK08703  83 atQGKLDGIVHCAGYFYAlSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLK----QSPdASVIFVGESHGETPKAYWG 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15239681  185 AYSASKFGLQGLAQALQQEVISDG-IHVTLLFPPDTDTPgfeQELKKRP 232
Cdd:PRK08703 159 GFGASKAALNYLCKVAADEWERFGnLRANVLVPGPINSP---QRIKSHP 204
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
35-203 2.88e-08

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 53.96  E-value: 2.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   35 IKFRHVFITGGSSGIGLALAHRAVSEGAKVSILA-RSTEKLAEAKRSIQLATGVEVATFsADVRDYDA----VSKAIDES 109
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAkKRAEEMNETLKMVKENGGEGIGVL-ADVSTREGcetlAKATIDRY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  110 GPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkaREGrgpASISLVSSQAGQAGIYGYTAYSAS 189
Cdd:PRK06077  83 GVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REG---GAIVNIASVAGIRPAYGLSIYGAM 157
                        170
                 ....*....|....
gi 15239681  190 KFGLQGLAQALQQE 203
Cdd:PRK06077 158 KAAVINLTKYLALE 171
PRK06523 PRK06523
short chain dehydrogenase; Provisional
38-243 3.90e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 53.37  E-value: 3.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARS-TEKLAEAKRSIQ--LATGVEVATFSADVRdydavskaiDESGPIDV 114
Cdd:PRK06523  10 KRALVTGGTKGIGAATVARLLEAGARVVTTARSrPDDLPEGVEFVAadLTTAEGCAAVARAVL---------ERLGGVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  115 LIVNQG---------VFIGKELEKQSpeevkfmIDVNLTGSFNVIKAALPAMKAregRGPASISLVSSQAGQAGIYG-YT 184
Cdd:PRK06523  81 LVHVLGgssapaggfAALTDEEWQDE-------LNLNLLAAVRLDRALLPGMIA---RGSGVIIHVTSIQRRLPLPEsTT 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15239681  185 AYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEqELKKRpeltsiIAASSG 243
Cdd:PRK06523 151 AYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAV-ALAER------LAEAAG 202
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
40-202 7.78e-08

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: 51.41  E-value: 7.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681    40 VFITGGSSGIGLALAHRAVSEGAK-VSILARSTEKLAEAKRSIQL--ATGVEVATFSADVRDYDAVSKAIDES----GPI 112
Cdd:pfam08659   3 YLITGGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAQALIAEleARGVEVVVVACDVSDPDAVAALLAEIkaegPPI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   113 DVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPamkaregrgpasISL-----VSSQAGQAGIYGYTAYS 187
Cdd:pfam08659  83 RGVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPD------------EPLdffvlFSSIAGLLGSPGQANYA 150
                         170
                  ....*....|....*
gi 15239681   188 ASKFGLQGLAQALQQ 202
Cdd:pfam08659 151 AANAFLDALAEYRRS 165
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
40-191 1.74e-07

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


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 50.48  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsiqlaTGVEVATFS-ADVRDYDAVSKAIDEsgpIDVLIVN 118
Cdd:cd05226   1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKRLSK--------EDQEPVAVVeGDLRDLDSLSDAVQG---VDVVIHL 69
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239681 119 QGvfigkelekqSPEEVKFMIDVNLTGSFNVIKAAlpamkarEGRGPASISLVSSqagqAGIYG----YTAYSASKF 191
Cdd:cd05226  70 AG----------APRDTRDFCEVDVEGTRNVLEAA-------KEAGVKHFIFISS----LGAYGdlheETEPSPSSP 125
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
38-234 1.79e-07

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 51.42  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADVRDYDAVSKAideSGPIDVLIV 117
Cdd:cd05361   2 SIALVTHARHFAGPASAEALTEDGYTVVCHDASFADAAERQAFESENPGTKALSEQKPEELVDAVLQA---GGAIDVLVS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 118 NQgvFIGKE---LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQ 194
Cdd:cd05361  79 ND--YIPRPmnpIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGG---GSIIFITSAVPKKPLAYNSLYGPARAAAV 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15239681 195 GLAQALQQEVISDGIHVTLLFPPDTDTPGF--EQELKKRPEL 234
Cdd:cd05361 154 ALAESLAKELSRDNILVYAIGPNFFNSPTYfpTSDWENNPEL 195
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
42-216 4.71e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 50.29  E-value: 4.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAkvSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDA----VSKAIDESGPIDVLIV 117
Cdd:PRK12481  13 ITGCNTGLGQGMAIGLAKAGA--DIVGVGVAEAPETQAQVE-ALGRKFHFITADLIQQKDidsiVSQAVEVMGHIDILIN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFnVIKAALPAMKAREGRGPASISLVSSQAGQAGIYgYTAYSASKFGLQGLA 197
Cdd:PRK12481  90 NAGIIRRQDLLEFGNKDWDDVININQKTVF-FLSQAVAKQFVKQGNGGKIINIASMLSFQGGIR-VPSYTASKSAVMGLT 167
                        170
                 ....*....|....*....
gi 15239681  198 QALQQEVISDGIHVTLLFP 216
Cdd:PRK12481 168 RALATELSQYNINVNAIAP 186
KR_1_FAS_SDR_x cd08954
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; ...
42-148 5.42e-07

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs; NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP 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 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: 187657 [Multi-domain]  Cd Length: 452  Bit Score: 50.91  E-value: 5.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAK--VSILARSTEKLAEAKRSIQL-ATGVEVATFSADVRDYDAVSKAIDE------SGPI 112
Cdd:cd08954 223 ITGGSGGLGLEILKWLVKRGAVenIIILSRSGMKWELELLIREWkSQNIKFHFVSVDVSDVSSLEKAINLilnapkIGPI 302
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15239681 113 DVLIVNQGVFIGKELEKQSPEevkFMIDVNL---TGSFN 148
Cdd:cd08954 303 GGIFHLAFVLIDKVLEIDTES---LFISVNKakvMGAIN 338
PRK08339 PRK08339
short chain dehydrogenase; Provisional
33-231 6.35e-07

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 49.85  E-value: 6.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   33 IPIKFRHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATFSADV---RDYDAVSKAIDES 109
Cdd:PRK08339   4 IDLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLtkrEDLERTVKELKNI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  110 GPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMkarEGRGPASISLVSSQAGQAGIYGYTAYSAS 189
Cdd:PRK08339  84 GEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAM---ERKGFGRIIYSTSVAIKEPIPNIALSNVV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKR 231
Cdd:PRK08339 161 RISMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDR 202
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
40-216 1.24e-06

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


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 49.21  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsiQLATGVEVATfsADVRDYDAVSKAIDEsgpIDVLIVNQ 119
Cdd:cd05228   1 ILVTGATGFLGSNLVRALLAQGYRVRALVRSGSDAVL-----LDGLPVEVVE--GDLTDAASLAAAMKG---CDRVFHLA 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 120 GVFigkeleKQSPEEVKFMIDVNLTGSFNVIKAALpamKAREGR----------GPASISLVSSQAGQAGIYGYTAYSAS 189
Cdd:cd05228  71 AFT------SLWAKDRKELYRTNVEGTRNVLDAAL---EAGVRRvvhtssiaalGGPPDGRIDETTPWNERPFPNDYYRS 141
                       170       180
                ....*....|....*....|....*..
gi 15239681 190 KFglqgLAQALQQEVISDGIHVTLLFP 216
Cdd:cd05228 142 KL----LAELEVLEAAAEGLDVVIVNP 164
PLN02780 PLN02780
ketoreductase/ oxidoreductase
42-216 1.42e-06

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 49.09  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATG-VEVAT----FSADVRDYDAVSKAIDESGPIDVLI 116
Cdd:PLN02780  58 VTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSkTQIKTvvvdFSGDIDEGVKRIKETIEGLDVGVLI 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  117 VNQGVF--IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAM-KAREGrgpasiSLVSSQAGQAGIYG----YTAYSAS 189
Cdd:PLN02780 138 NNVGVSypYARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMlKRKKG------AIINIGSGAAIVIPsdplYAVYAAT 211
                        170       180
                 ....*....|....*....|....*..
gi 15239681  190 KFGLQGLAQALQQEVISDGIHVTLLFP 216
Cdd:PLN02780 212 KAYIDQFSRCLYVEYKKSGIDVQCQVP 238
PRK05717 PRK05717
SDR family oxidoreductase;
38-200 1.45e-06

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 48.73  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiqlATGVEVATFSADVRDYDAVSKAIDES----GPID 113
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAK----ALGENAWFIAMDVADEAQVAAGVAEVlgqfGRLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  114 VLIVNQGVF--IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIyGYTAYSASKF 191
Cdd:PRK05717  87 ALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNG---AIVNLASTRARQSEP-DTEAYAASKG 162

                 ....*....
gi 15239681  192 GLQGLAQAL 200
Cdd:PRK05717 163 GLLALTHAL 171
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
38-159 1.48e-06

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


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 49.22  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGvEVATFSADVRDYDAVS---KAIDESG-PID 113
Cdd:COG5748   7 STVIITGASSGVGLYAAKALADRGWHVIMACRDLEKAEAAAQELGIPPD-SYTIIHIDLASLESVRrfvADFRALGrPLD 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15239681 114 VLIVNQGVFIGKELEKQ-SPEEVKFMIDVNLTGSFNVIKAALPAMKA 159
Cdd:COG5748  86 ALVCNAAVYYPLLKEPLrSPDGYELSVATNHLGHFLLCNLLLEDLKK 132
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
40-154 1.64e-06

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 48.45  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681    40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEklAEAKRSIQLATGVEVatfsaDVRDYDAVSKAIDESGPiDVlIVNQ 119
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTS--ASNTARLADLRFVEG-----DLTDRDALEKLLADVRP-DA-VIHL 71
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 15239681   120 GVFIGKELEKQSPEEVkfmIDVNLTGSFNVIKAAL 154
Cdd:pfam01370  72 AAVGGVGASIEDPEDF---IEANVLGTLNLLEAAR 103
PRK06196 PRK06196
oxidoreductase; Provisional
42-121 1.93e-06

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 48.91  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQlatGVEVATFsaDVRDYDAV---SKAIDESGP-IDVLIV 117
Cdd:PRK06196  31 VTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGID---GVEVVML--DLADLESVrafAERFLDSGRrIDILIN 105

                 ....
gi 15239681  118 NQGV 121
Cdd:PRK06196 106 NAGV 109
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
42-197 2.18e-06

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (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 oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses 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 the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 48.82  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  42 ITGGSSGIGLALAHRAVSEGAK-VSILARSTEKLAEAKRSIQL-ATGVEVATFSADVRDYDAVSKA---IDESGP-IDVL 115
Cdd:cd08955 154 ITGGLGGLGLLVAEWLVERGARhLVLTGRRAPSAAARQAIAALeEAGAEVVVLAADVSDRDALAAAlaqIRASLPpLRGV 233
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 116 IVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAAlpamkarEGRGPASISLVSSQAGQAGIYGYTAYSASKFGLQG 195
Cdd:cd08955 234 IHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLT-------QDLPLDFFVLFSSVASLLGSPGQANYAAANAFLDA 306

                ..
gi 15239681 196 LA 197
Cdd:cd08955 307 LA 308
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
38-228 3.69e-06

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 47.59  E-value: 3.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATG-----VEVATFSADVRDYDAVSKAIDESGPI 112
Cdd:cd09808   2 RSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGnqnifLHIVDMSDPKQVWEFVEEFKEEGKKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 113 DVLIVNQGVFIGKelEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREgrGPASISlVSSqagqAGIY------GYTAY 186
Cdd:cd09808  82 HVLINNAGCMVNK--RELTEDGLEKNFATNTLGTYILTTHLIPVLEKEE--DPRVIT-VSS----GGMLvqklntNNLQS 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15239681 187 SASKF-GLQGLAQALQQEVI--------SDGIHVTLLFPPDTDTPGFEQEL 228
Cdd:cd09808 153 ERTAFdGTMVYAQNKRQQVImteqwakkHPEIHFSVMHPGWADTPAVRNSM 203
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
40-176 4.41e-06

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: 47.51  E-value: 4.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILA-RSTEKLAEAKRSIQLATGvEVATFSADVRDYDAVSKAIDE----SGPIDV 114
Cdd:cd09810   4 VVITGASSGLGLAAAKALARRGEWHVVMAcRDFLKAEQAAQEVGMPKD-SYSVLHCDLASLDSVRQFVDNfrrtGRPLDA 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15239681 115 LIVNQGVFI--GKELeKQSPEEVKFMIDVNLTGSFNVIKAALPAMKaREGRGPASISLVSSQAG 176
Cdd:cd09810  83 LVCNAAVYLptAKEP-RFTADGFELTVGVNHLGHFLLTNLLLEDLQ-RSENASPRIVIVGSITH 144
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
40-153 4.84e-06

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


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 46.76  E-value: 4.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSiqlatGVEVATfsADVRDYDAVSKAIDEsgpIDVLIVNQ 119
Cdd:COG0702   2 ILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAA-----GVEVVQ--GDLDDPESLAAALAG---VDAVFLLV 71
                        90       100       110
                ....*....|....*....|....*....|....
gi 15239681 120 GvfigkelekqSPEEVKFMIDVNLTGsfNVIKAA 153
Cdd:COG0702  72 P----------SGPGGDFAVDVEGAR--NLADAA 93
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
38-179 5.23e-06

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 47.08  E-value: 5.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATG-VEVATFSADVRDYDAV----SKAIDESGPI 112
Cdd:cd09807   2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLnHEVIVRHLDLASLKSIrafaAEFLAEEDRL 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239681 113 DVLIVNQGVFIGKELEKQSPEEVKFmiDVNLTGSFNVIKAALPAMKAREgrgPASISLVSSQAGQAG 179
Cdd:cd09807  82 DVLINNAGVMRCPYSKTEDGFEMQF--GVNHLGHFLLTNLLLDLLKKSA---PSRIVNVSSLAHKAG 143
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
40-230 5.60e-06

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: 47.06  E-value: 5.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTE-KLAEAKRSIQLATGVEVATFsADVRDYDAVSKAID-----ESGPID 113
Cdd:cd09763   6 ALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEARGGKCIPVR-CDHSDDDEVEALFErvareQQGRLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 114 VLIVNQGVFIGKELEKQSPeevKF----------MIDVNLTGSFNVIKAALPAMKArEGRGpaSISLVSSQAGQAGIYGY 183
Cdd:cd09763  85 ILVNNAYAAVQLILVGVAK---PFweepptiwddINNVGLRAHYACSVYAAPLMVK-AGKG--LIVIISSTGGLEYLFNV 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15239681 184 tAYSASKFGLQGLAQALQQEVISDGIHVTLLFP-----------PDTDTPGFEQELKK 230
Cdd:cd09763 159 -AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPgfvrtelvlemPEDDEGSWHAKERD 215
PRK06197 PRK06197
short chain dehydrogenase; Provisional
38-121 5.68e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 47.33  E-value: 5.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGL----ALAHRavseGAKVSILARSTEKLAEAKRSI-QLATGVEVATFSADVRDYDAVSKAIDESGP- 111
Cdd:PRK06197  17 RVAVVTGANTGLGYetaaALAAK----GAHVVLAVRNLDKGKAAAARItAATPGADVTLQELDLTSLASVRAAADALRAa 92
                         90
                 ....*....|...
gi 15239681  112 ---IDVLIVNQGV 121
Cdd:PRK06197  93 yprIDLLINNAGV 105
PRK08177 PRK08177
SDR family oxidoreductase;
38-204 6.37e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 46.56  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKlAEAkrsIQLATGVEVATFSADVRD-YDAVSKAIDESgPIDVLI 116
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQ-DTA---LQALPGVHIEKLDMNDPAsLDQLLQRLQGQ-RFDLLF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  117 VNQGVF--IGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPamKAREGRGpaSISLVSSQAGQAGI---YGYTAYSASKF 191
Cdd:PRK08177  77 VNAGISgpAHQSAADATAAEIGQLFLTNAIAPIRLARRLLG--QVRPGQG--VLAFMSSQLGSVELpdgGEMPLYKASKA 152
                        170
                 ....*....|...
gi 15239681  192 GLQGLAQALQQEV 204
Cdd:PRK08177 153 ALNSMTRSFVAEL 165
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
40-154 7.21e-06

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 46.84  E-value: 7.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAK-VSILARSTEKLAEAKRSI-QLATGVEVATFSADVRDYDAVSKAIDESGPiDVlIV 117
Cdd:cd05237   5 ILVTGGAGSIGSELVRQILKFGPKkLIVFDRDENKLHELVRELrSRFPHDKLRFIIGDVRDKERLRRAFKERGP-DI-VF 82
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15239681 118 NQGVFIGKELEKQSPEEvkfMIDVNLTGSFNVIKAAL 154
Cdd:cd05237  83 HAAALKHVPSMEDNPEE---AIKTNVLGTKNVIDAAI 116
PRK08340 PRK08340
SDR family oxidoreductase;
40-120 8.87e-06

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 46.34  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEvaTFSADVRDYDAVSKAIDES----GPIDVL 115
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGEVY--AVKADLSDKDDLKNLVKEAwellGGIDAL 80

                 ....*
gi 15239681  116 IVNQG 120
Cdd:PRK08340  81 VWNAG 85
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
42-216 1.61e-05

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 45.63  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAkvSILARSTEKLAEAKRSIQlATGVEVATFSADVRDYDA----VSKAIDESGPIDVLIV 117
Cdd:PRK08993  15 VTGCDTGLGQGMALGLAEAGC--DIVGINIVEPTETIEQVT-ALGRRFLSLTADLRKIDGipalLERAVAEFGHIDILVN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKArEGRGPASISLVSSQAGQAGIYgYTAYSASKFGLQGLA 197
Cdd:PRK08993  92 NAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIA-QGNGGKIINIASMLSFQGGIR-VPSYTASKSGVMGVT 169
                        170
                 ....*....|....*....
gi 15239681  198 QALQQEVISDGIHVTLLFP 216
Cdd:PRK08993 170 RLMANEWAKHNINVNAIAP 188
PRK06953 PRK06953
SDR family oxidoreductase;
40-193 3.25e-05

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 44.29  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKrsiqlATGVEvaTFSADVRDYDAVS----KAIDESgpIDVL 115
Cdd:PRK06953   4 VLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQ-----ALGAE--ALALDVADPASVAglawKLDGEA--LDAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  116 IVNQGVFIGKE--LEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRGPASISLVSSQAGQAGIYGYTaYSASKFGL 193
Cdd:PRK06953  75 VYVAGVYGPRTegVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIGDATGTTGWL-YRASKAAL 153
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
42-234 6.80e-05

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 43.68  E-value: 6.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATfSADVRD----YDAVSKAIDESGPIDVLIV 117
Cdd:PRK06113  16 ITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFAC-RCDITSeqelSALADFALSKLGKVDILVN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  118 NQGVFIGKELEkQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGrgpASISLVSSQAGQAGIYGYTAYSASKFGLQGLA 197
Cdd:PRK06113  95 NAGGGGPKPFD-MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGG---GVILTITSMAAENKNINMTSYASSKAAASHLV 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15239681  198 QALQQEVISDGIHVTLLFPP--DTD------TPGFEQELKKRPEL 234
Cdd:PRK06113 171 RNMAFDLGEKNIRVNGIAPGaiLTDalksviTPEIEQKMLQHTPI 215
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
42-268 7.49e-05

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 43.75  E-value: 7.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681    42 ITGGSSGIGLA----LAHRAVSEGAKVSILARSTEKLAEAKRSIQLAT-GVEVATFSADV---RDYDAVSKAIDESGPID 113
Cdd:TIGR01500   5 VTGASRGFGRTiaqeLAKCLKSPGSVLVLSARNDEALRQLKAEIGAERsGLRVVRVSLDLgaeAGLEQLLKALRELPRPK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   114 -----VLIVNQGVF--IGK-ELEKQSPEEVKFMIDVNLTGSFNVIKAALPAMKAREGRgPASISLVSSQAGQAGIYGYTA 185
Cdd:TIGR01500  85 glqrlLLINNAGTLgdVSKgFVDLSDSTQVQNYWALNLTSMLCLTSSVLKAFKDSPGL-NRTVVNISSLCAIQPFKGWAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   186 YSASKFGLQGLAQALQQEVISDGIHVtLLFPP---DTDTPGFEQELKKRPELTSIIAA--SSGSMKT-NEVAKICFDGIK 259
Cdd:TIGR01500 164 YCAGKAARDMLFQVLALEEKNPNVRV-LNYAPgvlDTDMQQQVREESVDPDMRKGLQElkAKGKLVDpKVSAQKLLSLLE 242

                  ....*....
gi 15239681   260 AGKFTVTCH 268
Cdd:TIGR01500 243 KDKFKSGAH 251
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
40-222 9.49e-05

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 43.25  E-value: 9.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVsilarsteklaeakrsiqLATGVEVATFSADVRDYDAVSKAIDE-----SGPIDV 114
Cdd:cd05328   2 IVITGAASGIGAATAELLEDAGHTV------------------IGIDLREADVIADLSTPEGRAAAIADvlarcSGVLDG 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 115 LIVNQGVfigkelekQSPEEVKFMIDVNLTGSFNVIKAALPAMkaREGRGPAsISLVSSQAG------------------ 176
Cdd:cd05328  64 LVNCAGV--------GGTTVAGLVLKVNYFGLRALMEALLPRL--RKGHGPA-AVVVSSIAGagwaqdklelakalaagt 132
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15239681 177 ---------QAGIYGYTAYSASKFGLQGLAQALQQEVISD-GIHVTLLFPPDTDTP 222
Cdd:cd05328 133 earavalaeHAGQPGYLAYAGSKEALTVWTRRRAATWLYGaGVRVNTVAPGPVETP 188
PRK07806 PRK07806
SDR family oxidoreductase;
38-159 1.06e-04

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 43.17  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARS----TEKLAEAKRsiqlATGVEVATFSADVRDYDAV----SKAIDES 109
Cdd:PRK07806   7 KTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkaprANKVVAEIE----AAGGRASAVGADLTDEESVaalmDTAREEF 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 15239681  110 GPIDVLIVNQgvfiGKELEKQSPEEvkFMIDVNLTGSFNVIKAALPAMKA 159
Cdd:PRK07806  83 GGLDALVLNA----SGGMESGMDED--YAMRLNRDAQRNLARAALPLMPA 126
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
38-231 1.08e-04

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 43.14  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGS--SGIGLALAHRAVSEGAKV-----SILARSTEKLAEAKRSIQLA-----TGVEVATFSADVRDYDA---- 101
Cdd:PRK12748   6 KIALVTGASrlNGIGAAVCRRLAAKGIDIfftywSPYDKTMPWGMHDKEPVLLKeeiesYGVRCEHMEIDLSQPYApnrv 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  102 VSKAIDESGPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFnvikaALPAMKAREGRGPASISLVSSQAGQ--AG 179
Cdd:PRK12748  86 FYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATM-----LLSSAFAKQYDGKAGGRIINLTSGQslGP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15239681  180 IYGYTAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKKR 231
Cdd:PRK12748 161 MPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWITEELKHH 212
NAD_binding_10 pfam13460
NAD(P)H-binding;
44-120 1.59e-04

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 41.82  E-value: 1.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239681    44 GGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsIQLATGVEVatFSADVRDYDAVSKAIDesgPIDVLIVNQG 120
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALVRNPEKLAD----LEDHPGVEV--VDGDVLDPDDLAEALA---GQDAVISALG 68
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
42-230 1.85e-04

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 42.47  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   42 ITGGS--SGIGLALAHRAVSEGAKV-----SILARSTEKLAEAKRSIQLA-----TGVEVATFSADVRDYDAVSKAIDES 109
Cdd:PRK12859  11 VTGVSrlDGIGAAICKELAEAGADIfftywTAYDKEMPWGVDQDEQIQLQeellkNGVKVSSMELDLTQNDAPKELLNKV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  110 ----GPIDVLIVNQGVFIGKELEKQSPEEVKFMIDVNLTGSFnvikaALPAMKAR---EGRGPASISLVSSQaGQAGIYG 182
Cdd:PRK12859  91 teqlGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATT-----LLSSQFARgfdKKSGGRIINMTSGQ-FQGPMVG 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15239681  183 YTAYSASKFGLQGLAQALQQEVISDGIHVTLLFPPDTDTPGFEQELKK 230
Cdd:PRK12859 165 ELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMTEEIKQ 212
PRK07023 PRK07023
SDR family oxidoreductase;
39-203 2.16e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 41.92  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   39 HVFI-TGGSSGIGLALAHRAVSEGAKVSILARSTE----------------KLAEAKRSIQLATGVEVATFSADVRDYda 101
Cdd:PRK07023   2 VRAIvTGHSRGLGAALAEQLLQPGIAVLGVARSRHpslaaaagerlaevelDLSDAAAAAAWLAGDLLAAFVDGASRV-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  102 vskaidesgpidVLIVNQGVF--IGKeLEKQSPEEVKFMIDVNLTGSFnVIKAALpaMKAREGRGPASISLVSSQAGQAG 179
Cdd:PRK07023  80 ------------LLINNAGTVepIGP-LATLDAAAIARAVGLNVAAPL-MLTAAL--AQAASDAAERRILHISSGAARNA 143
                        170       180
                 ....*....|....*....|....
gi 15239681  180 IYGYTAYSASKFGLQGLAQALQQE 203
Cdd:PRK07023 144 YAGWSVYCATKAALDHHARAVALD 167
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
40-160 5.58e-04

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 41.20  E-value: 5.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEAKRSIQLATGVEVATF-SADVRDYDAVSKAIDesgpIDVLIVN 118
Cdd:cd05263   1 VFVTGGTGFLGRHLVKRLLENGFKVLVLVRSESLGEAHERIEEAGLEADRVRVlEGDLTQPNLGLSAAA----SRELAGK 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15239681 119 QGVFI--GKELEKQSPEEVkfMIDVNLTGSFNVIKAALPAMKAR 160
Cdd:cd05263  77 VDHVIhcAASYDFQAPNED--AWRTNIDGTEHVLELAARLDIQR 118
PRK06940 PRK06940
short chain dehydrogenase; Provisional
38-121 5.60e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 41.16  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRaVSEGAKVSILARSTEKLAEAKRSIQLAtGVEVATFSADVRDYDAVSKAIDES---GPIDV 114
Cdd:PRK06940   2 KEVVVVIGAGGIGQAIARR-VGAGKKVLLADYNEENLEAAAKTLREA-GFDVSTQEVDVSSRESVKALAATAqtlGPVTG 79

                 ....*..
gi 15239681  115 LIVNQGV 121
Cdd:PRK06940  80 LVHTAGV 86
PRK09134 PRK09134
SDR family oxidoreductase;
38-122 6.63e-04

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 40.68  E-value: 6.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   38 RHVFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEA-KRSIQlATGVEVATFSADVRDYDAVS----KAIDESGPI 112
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVAVHYNRSRDEAEAlAAEIR-ALGRRAVALQADLADEAEVRalvaRASAALGPI 88
                         90
                 ....*....|
gi 15239681  113 DVLIVNQGVF 122
Cdd:PRK09134  89 TLLVNNASLF 98
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
40-116 1.41e-03

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 39.73  E-value: 1.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLA---LAHRAvseGAKVSILARSTEKLAEAKrsiQLatGVEVAtFSADVRDYDAVSKAIDESGPIDVLI 116
Cdd:cd05276 143 VLIHGGASGVGTAaiqLAKAL---GARVIATAGSEEKLEACR---AL--GADVA-INYRTEDFAEEVKEATGGRGVDVIL 213
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
39-105 2.60e-03

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 38.87  E-value: 2.60e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15239681  39 HVFITGGSSGIGLALAHRAVSEGAKVSILARStEKLAEAKRSIqlatGVEVatFSADVRDYDAVSKA 105
Cdd:cd05262   2 KVFVTGATGFIGSAVVRELVAAGHEVVGLARS-DAGAAKLEAA----GAQV--HRGDLEDLDILRKA 61
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
40-254 5.02e-03

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


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 37.60  E-value: 5.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTEKLAEakrsiQLATGVEVatFSADVRDYDAVSKAIDesgPIDVLIVNQ 119
Cdd:cd05243   2 VLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEK-----LEAAGAEV--VVGDLTDAESLAAALE---GIDAVISAA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 120 GVfigkelekqSPEEVKFMIDVNLTGSFNVIKAalpAMKAREGRgpasISLVSSqagqagiYGYTAYSASKFGLQGLAQA 199
Cdd:cd05243  72 GS---------GGKGGPRTEAVDYDGNINLIDA---AKKAGVKR----FVLVSS-------IGADKPSHPLEALGPYLDA 128
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681 200 ---LQQEVISDGIHVTLLFPpdtdtPGFEQEL--KKRPELTSIIAASSGSMKTNEVAKIC 254
Cdd:cd05243 129 krkAEDYLRASGLDYTIVRP-----GGLTDDPagTGRVVLGGDGTRLDGPISRADVAEVL 183
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
40-79 5.13e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 38.21  E-value: 5.13e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15239681  40 VFITGGSSGIGLA---LAHRAvseGAKVSILARSTEKLAEAKR 79
Cdd:COG0604 143 VLVHGAAGGVGSAavqLAKAL---GARVIATASSPEKAELLRA 182
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
42-156 5.47e-03

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 38.12  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681    42 ITGGSSGIGLALAHRAVSEGAKVSI----LARSTEKLAEAKRSiQLATGVEVatfsaDVRDYDAVSKAIDESgpiDVLIV 117
Cdd:pfam01073   2 VTGGGGFLGRHIIKLLVREGELKEVrvfdLRESPELLEDFSKS-NVIKYIQG-----DVTDKDDLDNALEGV---DVVIH 72
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 15239681   118 NQGvfIGKELEKQSPEEVkfmIDVNLTGSFNVIKAALPA 156
Cdd:pfam01073  73 TAS--AVDVFGKYTFDEI---MKVNVKGTQNVLEACVKA 106
FR_SDR_e cd08958
flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended ...
40-154 5.82e-03

flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended SDR-type and related proteins. These FRs act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites; they have the characteristic active site triad of the SDRs (though not the upstream active site Asn) and a NADP-binding motif that is very similar to the typical extended SDR motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187661 [Multi-domain]  Cd Length: 293  Bit Score: 37.94  E-value: 5.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681  40 VFITGGSSGIGLALAHRAVSEGAKVSILARSTE---------KLAEAKRSIQLatgvevatFSADVRDYDAVSKAIDESg 110
Cdd:cd08958   1 VCVTGASGFIGSWLVKRLLQRGYTVRATVRDPGdekkvahllELEGAKERLKL--------FKADLLDYGSFDAAIDGC- 71
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15239681 111 pidvlivnQGVF-----IgkELEKQSPEEVkfMIDVNLTGSFNVIKAAL 154
Cdd:cd08958  72 --------DGVFhvaspV--DFDSEDPEEE--MIEPAVKGTLNVLEACA 108
PRK08309 PRK08309
short chain dehydrogenase; Provisional
39-117 8.15e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236232  Cd Length: 177  Bit Score: 36.65  E-value: 8.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239681   39 HVFITGGSsGIGLALAHRAVSEGAKVSILARSTEKLAEAKRsiQLATGVEVATFSADVRDYDAV----SKAIDESGPIDV 114
Cdd:PRK08309   2 HALVIGGT-GMLKRVSLWLCEKGFHVSVIARREVKLENVKR--ESTTPESITPLPLDYHDDDALklaiKSTIEKNGPFDL 78

                 ...
gi 15239681  115 LIV 117
Cdd:PRK08309  79 AVA 81
 
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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