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Conserved domains on  [gi|2462599477|ref|XP_054207097|]
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3-oxoacyl-[acyl-carrier-protein] reductase isoform X2 [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10142575)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-191 1.17e-63

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: 197.12  E-value: 1.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   5 CAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAieALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05233    81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNIS----------SVAGLRPLPGQAAYAASK 150

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05233   151 AALEGLTRSLALELAPYGIRVNAVAPGLV 179
 
Name Accession Description Interval E-value
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-191 1.17e-63

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: 197.12  E-value: 1.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   5 CAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAieALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05233    81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNIS----------SVAGLRPLPGQAAYAASK 150

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05233   151 AALEGLTRSLALELAPYGIRVNAVAPGLV 179
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-188 7.25e-63

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: 195.77  E-value: 7.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:COG1028     5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAAFGRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:COG1028    85 DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNIS----------SIAGLRGSPGQAA 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:COG1028   155 YAASKAAVVGLTRSLALELAPRGIRVNAVAP 185
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-191 1.47e-62

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 194.99  E-value: 1.47e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK05653    4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraaGGEARVLVFDVSDEAAVRALIEAAVEAFGAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK05653   84 DILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNIS----------SVSGVTGNPGQTN 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK05653  154 YSAAKAGVIGFTKALALELASRGITVNAVAPGFI 187
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-201 1.53e-56

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 177.81  E-value: 1.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAkelGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNIS----------SVAGLVPYPGGSAYS 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELI--PRTVSIRKME 201
Cdd:pfam00106 151 ASKAAVIGFTRSLALELAPHGIRVNAVAPGGVdtDMTKELREDE 194
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-160 3.20e-11

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: 59.80  E-value: 3.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477    9 GGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAA------GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:smart00822   7 GGLGGLGRALARWLAERGARrLVLLSRSGPDAPGAAallaelEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSmltckaamrtmiqqqggsiVNVgHRremLLHKR---------SIVGLKGN 152
Cdd:smart00822  87 HAAGVLDDGVLASLTPERFAAVLAPKAAGA-------------------WNL-HE---LTADLpldffvlfsSIAGVLGS 143


                   ....*...
gi 2462599477  153 SGQSVYSA 160
Cdd:smart00822 144 PGQANYAA 151
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 4-191 1.86e-08

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: 52.99  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   4 VCAVFGGSRGIGRAVAQLMAR----KGYRLAVIARNLEGAKAAAGDLGGDHLA-----FSCDVAKEHDVQNTFEELEKhL 74
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERSGlrvvrVSLDLGAEAGLEQLLKALRE-L 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  75 GRVNFLVNAAGINRDGLLVRT-KTEDMVSQL-------HTNLLGSMLTCKAAMRTMIQQQGG--SIVNVGhrremllhkr 144
Cdd:TIGR01500  81 PRPKGLQRLLLINNAGTLGDVsKGFVDLSDStqvqnywALNLTSMLCLTSSVLKAFKDSPGLnrTVVNIS---------- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462599477 145 SIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:TIGR01500 151 SLCAIQPFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVL 197
 
Name Accession Description Interval E-value
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 5-191 1.17e-63

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: 197.12  E-value: 1.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   5 CAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAieALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05233    81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNIS----------SVAGLRPLPGQAAYAASK 150

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05233   151 AALEGLTRSLALELAPYGIRVNAVAPGLV 179
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 3-191 1.47e-63

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: 197.39  E-value: 1.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVeeiKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd05333    81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINIS----------SVVGLIGNPGQANYA 150

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05333   151 ASKAGVIGFTKSLAKELASRGITVNAVAPGFI 182
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-188 7.25e-63

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: 195.77  E-value: 7.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:COG1028     5 KGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAAFGRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:COG1028    85 DILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNIS----------SIAGLRGSPGQAA 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:COG1028   155 YAASKAAVVGLTRSLALELAPRGIRVNAVAP 185
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-191 1.47e-62

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 194.99  E-value: 1.47e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK05653    4 QGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELraaGGEARVLVFDVSDEAAVRALIEAAVEAFGAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK05653   84 DILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNIS----------SVSGVTGNPGQTN 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK05653  154 YSAAKAGVIGFTKALALELASRGITVNAVAPGFI 187
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-191 6.09e-57

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 180.77  E-value: 6.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK05557    4 EGKVALVTGASRGIGRAIAERLAAQGANVVInYASSEAGAEALVaeiGALGGKALAVQGDVSDAESVERAVDEAKAEFGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK05557   84 VDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINIS----------SVVGLMGNPGQA 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK05557  154 NYAASKAGVIGFTKSLARELASRGITVNAVAPGFI 188
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 3-201 1.53e-56

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 177.81  E-value: 1.53e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAkelGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNIS----------SVAGLVPYPGGSAYS 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELI--PRTVSIRKME 201
Cdd:pfam00106 151 ASKAAVIGFTRSLALELAPHGIRVNAVAPGGVdtDMTKELREDE 194
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 2-188 2.69e-56

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: 178.84  E-value: 2.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:COG4221     5 GKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:COG4221    85 NNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNIS----------SIAGLRPYPGGAVYAAT 154

                         170       180
                  ....*....|....*....|....*..
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:COG4221   155 KAAVRGLSESLRAELRPTGIRVTVIEP 181
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-188 9.86e-55

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 175.06  E-value: 9.86e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:COG0300     4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELraaGARVEVVALDVTDPDAVAALAEAVLARFGPI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:COG0300    84 DVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVS----------SVAGLRGLPGMAA 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:COG0300   154 YAASKAALEGFSESLRAELAPTGVRVTAVCP 184
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-191 1.91e-49

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 161.57  E-value: 1.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR-NLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK12825    5 MGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEaveALGRRAQAVQADVTDKAALEAAVAAAVERFGR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK12825   85 IDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNIS----------SVAGLPGWPGRS 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK12825  155 NYAAAKAGLVGLTKALARELAEYGITVNMVAPGDI 189
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-188 4.04e-48

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 158.08  E-value: 4.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-ARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK05565    4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLeeiKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK05565   84 IDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNIS----------SIWGLIGASCEV 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05565  154 LYSASKGAVNAFTKALAKELAPSGIRVNAVAP 185
PRK12826 PRK12826
SDR family oxidoreductase;
1-191 1.29e-44

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 149.30  E-value: 1.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK12826    5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVeaaGGKARARQVDVRDRAALKAAVAAGVEDFGRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGL-KGNSGQS 156
Cdd:PRK12826   85 DILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTS----------SVAGPrVGYPGLA 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK12826  155 HYAASKAGLVGFTRALALELAARNITVNSVHPGGV 189
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-188 1.66e-44

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: 148.35  E-value: 1.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  12 RGIGRAVAQLMARKGYRLAVIARNLEGAKAA---AGDLGGDhlAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI-- 86
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVeelAEELGAA--VLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFap 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLV 166
Cdd:pfam13561  84 KLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLS----------SIGAERVVPNYNAYGAAKAALE 151

                         170       180
                  ....*....|....*....|..
gi 2462599477 167 GFSRALAKEVARKKIRVNVVAP 188
Cdd:pfam13561 152 ALTRYLAVELGPRGIRVNAISP 173
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-191 6.68e-43

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 144.72  E-value: 6.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08217    5 DKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNqekLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQ---------LHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVghrremllhkrSIVG 148
Cdd:PRK08217   85 GLINNAGILRDGLLVKAKDGKVTSKmsleqfqsvIDVNLTGVFLCGREAAAKMIESgSKGVIINI-----------SSIA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462599477 149 LKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK08217  154 RAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVI 196
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-210 4.23e-40

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 143.45  E-value: 4.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06484    6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK06484   86 NAGVTDPTMtaTLDTTLEEFARLQAINLTGAYLVAREALRLMIEQgHGAAIVNVA----------SGAGLVALPKRTAYS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVSIRKMEKGDRINVTL 210
Cdd:PRK06484  156 ASKAAVISLTRSLACEWAAKGIRVNAVLPGYV-RTQMVAELERAGKLDPSA 205
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-188 6.04e-39

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 134.51  E-value: 6.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAA---GDLGGDHL---AFSCDVAKEHDVQNTFEELEKHL 74
Cdd:PRK12824    1 MKKIALVTGAKRGIGSAIARELLNDGYR--VIATYFSGNDCAKdwfEEYGFTEDqvrLKELDVTDTEECAEALAEIEEEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG 154
Cdd:PRK12824   79 GPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINIS----------SVNGLKGQFG 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12824  149 QTNYSAAKAGMIGFTKALASEGARYGITVNCIAP 182
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 2-191 1.19e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 134.02  E-value: 1.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06841   15 GKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNvghrremLLHKRSIVGLKGNSGqsvYSAS 161
Cdd:PRK06841   95 NSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVN-------LASQAGVVALERHVA---YCAS 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK06841  165 KAGVVGMTKVLALEWGPYGITVNAISPTVV 194
PRK06138 PRK06138
SDR family oxidoreductase;
2-191 1.71e-37

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 131.04  E-value: 1.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL--GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06138    5 GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIaaGGRAFARQGDVGSAEAVEALVDFVAARWGRLDV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllHKRSIVGLKGNSGqsvYS 159
Cdd:PRK06138   85 LVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTA-------SQLALAGGRGRAA---YV 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK06138  155 ASKGAIASLTRAMALDHATDGIRVNAVAPGTI 186
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 3-188 1.05e-36

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: 128.63  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05347     6 KVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIekeGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd05347    86 LVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINIC----------SLLSELGGPPVPAYA 155

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05347   156 ASKGGVAGLTKALATEWARHGIQVNAIAP 184
FabG-like PRK07231
SDR family oxidoreductase;
2-188 1.61e-36

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 128.41  E-value: 1.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07231    5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILagGRAIAVAADVSDEADVEAAVAAALERFGSVDI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGIN-RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK07231   85 LVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVA----------STAGLRPRPGLGWY 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07231  155 NASKGAVITLTKALAAELGPDKIRVNAVAP 184
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 2-188 1.16e-35

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 126.15  E-value: 1.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK12429    4 GKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALqkaGGKAIGVAMDVTDEEAINAGIDYAVETFGGVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK12429   84 ILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMA----------SVHGLVGSAGKAAY 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12429  154 VSAKHGLIGLTKVVALEGATHGVTVNAICP 183
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 2-188 1.69e-35

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: 125.44  E-value: 1.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLA-------FSCDVAKEHDVQNTFEELEKHL 74
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANAsgqkvsyISADLSDYEEVEQAFAQAVEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG 154
Cdd:cd08939    81 GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVS----------SQAALVGIYG 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08939   151 YSAYCPSKFALRGLAESLRQELKPYNIRVSVVYP 184
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-208 1.78e-35

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 130.74  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06484  270 RVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVN 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGL-LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:PRK06484  350 NAGIAEVFKpSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLG----------SIASLLALPPRNAYCAS 417

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVSIRKMEKGDRINV 208
Cdd:PRK06484  418 KAAVTMLSRSLACEWAPAGIRVNTVAPGYI-ETPAVLALKASGRADF 463
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 3-194 5.18e-34

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: 121.80  E-value: 5.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVnYYRSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINR--DGLLVRTKT----EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05349    81 NNALIDFpfDPDQRKTFDtidwEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIG----------TNLFQNPVVPY 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRT 194
Cdd:cd05349   151 HDYTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVT 189
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 3-188 6.60e-34

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 121.62  E-value: 6.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12939    8 KRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALeaaGGRAHAIAADLADPASVQRFFDAAAAALGGLDG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK12939   88 LVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLA----------SDTALWGAPKLGAYV 157

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12939  158 ASKGAVIGMTRSLARELGGRGITVNAIAP 186
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 3-188 6.93e-34

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: 121.18  E-value: 6.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05374    81 NAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVS----------SVAGLVPTPFLGPYCASK 150

                         170       180
                  ....*....|....*....|....*.
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05374   151 AALEALSESLRLELAPFGIKVTIIEP 176
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-191 1.38e-33

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 120.56  E-value: 1.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07666    8 KNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEayGVKVVIaTADVSDYEEVTAAIEQLKNELGSIDI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK07666   88 LINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINIS----------STAGQKGAAVTSAYS 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK07666  158 ASKFGVLGLTESLMQEVRKHNIRVTALTPSTV 189
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 3-188 2.86e-33

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: 119.69  E-value: 2.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd05362     4 KVALVTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAeieAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:cd05362    84 ILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINIS----------SSLTAAYTPNYGAY 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05362   152 AGSKAAVEAFTRVLAKELGGRGITVNAVAP 181
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 3-203 3.08e-33

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 120.05  E-value: 3.08e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR---NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK08213   13 KTALVTGGSRGLGLQIAEALGEAGARVVLSARkaeELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDgllvrTKTEDMVSQ-----LHTNLLGS-MLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNS 153
Cdd:PRK08213   93 LVNNAGATWG-----APAEDHPVEawdkvMNLNVRGLfLLSQAVAKRSMIPRGYGRIINVA----------SVAGLGGNP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462599477 154 GQSV----YSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPrtvsiRKMEKG 203
Cdd:PRK08213  158 PEVMdtiaYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFP-----TKMTRG 206
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 2-188 4.00e-33

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


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 119.36  E-value: 4.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05352     8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYgvktKAYKCDVSSQESVEKTFKQIQKDFGKI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRD-GLLVRTKtEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN--SG 154
Cdd:cd05352    88 DILIANAGITVHkPALDYTY-EQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITA----------SMSGTIVNrpQP 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05352   157 QAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISP 190
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 2-194 6.77e-33

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 119.35  E-value: 6.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaaAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06171    9 GKIIIVTGGSSGIGLAIVKELLANGANVVNADIH-------GGDGQHENYQFvPTDVSSAEEVNHTVAEIIEKFGRIDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHT---------NLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKG 151
Cdd:PRK06171   82 VNNAGINIPRLLVDEKDPAGKYELNEaafdkmfniNQKGVFLMSQAVARQMVKQHDGVIVNMS----------SEAGLEG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462599477 152 NSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRT 194
Cdd:PRK06171  152 SEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEAT 194
PRK06172 PRK06172
SDR family oxidoreductase;
2-191 7.66e-33

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 118.70  E-value: 7.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNL---EGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06172    7 GKVALVTGGAAGIGRATALAFAREGAKVVVADRDAaggEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK06172   87 YAFNNAGIEIEQGRLAEGSEAEFDAImGVNVKGVWLCMKYQIPLMLAQGGGAIVNTA----------SVAGLGAAPKMSI 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK06172  157 YAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVI 190
PRK07326 PRK07326
SDR family oxidoreductase;
1-188 1.24e-32

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 117.80  E-value: 1.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07326    5 KGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNnkGNVLGLAADVRDEADVQRAVDAIVAAFGGLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK07326   85 VLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINIS----------SLAGTNFFAGGAAY 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07326  154 NASKFGLVGFSEAAMLDLRQYGIKVSTIMP 183
PRK07063 PRK07063
SDR family oxidoreductase;
3-191 1.59e-32

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 118.23  E-value: 1.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK07063    8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIardvaGARVLAVPADVTDAASVAAAVAAAEEAFGPL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGIN--RDGLlvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremlLHKRSIVglkgnSGQ 155
Cdd:PRK07063   88 DVLVNNAGINvfADPL--AMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIAS-----THAFKII-----PGC 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK07063  156 FPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYI 191
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 2-212 5.38e-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: 116.53  E-value: 5.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05369     3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEIssatGGRAHPIQCDVRDPEAVEAAVDETLKEFGKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINrdgllVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKG 151
Cdd:cd05369    83 DILINNAAGN-----FLAPAESLSPNgfktvIDIDLNGTFNTTKAVGKRLIEAKhGGSILNIS----------ATYAYTG 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462599477 152 NSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKGDRINVTLRS 212
Cdd:cd05369   148 SPFQVHSAAAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGMERLAPSGKSEKKMIE 208
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 7-191 6.43e-32

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 116.17  E-value: 6.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:PRK12936   11 VTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEGVDILVNNAGI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLV 166
Cdd:PRK12936   91 TKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINI----------TSVVGVTGNPGQANYCASKAGMI 160

                         170       180
                  ....*....|....*....|....*
gi 2462599477 167 GFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK12936  161 GFSKSLAQEIATRNVTVNCVAPGFI 185
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 2-191 7.81e-32

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: 116.22  E-value: 7.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELragGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:cd05344    81 ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNIS----------SLTVKEPEPNLVLS 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05344   151 NVARAGLIGLVKTLSRELAPDGVTVNSVLPGYI 183
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 3-192 9.82e-32

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: 115.86  E-value: 9.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLE-GAKAAAGDLGGDHLA--FSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENpGAAAELQAINPKVKAtfVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGIN--RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ---GGSIVNVGhrremllhkrSIVGLKGNSG 154
Cdd:cd05323    81 LINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkGGVIVNIG----------SVAGLYPAPQ 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462599477 155 QSVYSASKGGLVGFSRALAKEVARKK-IRVNVVAPELIP 192
Cdd:cd05323   151 FPVYSASKHGVVGFTRSLADLLEYKTgVRVNAICPGFTN 189
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 3-191 1.36e-31

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: 115.56  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAViarNLEGAKAAAGDL-------GGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:cd05358     4 KVALVTGASSGIGKAIAIRLATAGANVVV---NYRSKEDAAEEVveeikavGGKAIAVQADVSKEEDVVALFQSAIKEFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGHRREMLLHkrsivglkgnSG 154
Cdd:cd05358    81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIkGKIINMSSVHEKIPW----------PG 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462599477 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05358   151 HVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAI 187
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 2-191 1.99e-31

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 115.17  E-value: 1.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05341     5 GKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGRLDVLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:cd05341    85 NNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMS----------SIEGLVGDPALAAYNAS 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 162 KGGLVGFSRALAKEVARKK--IRVNVVAPELI 191
Cdd:cd05341   155 KGAVRGLTKSAALECATQGygIRVNSVHPGYI 186
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 4-191 2.84e-31

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: 114.26  E-value: 2.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETAnnvRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:cd05339    81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIA----------SVAGLISPAGLADYCA 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 161 SKGGLVGFSRALAKEVAR---KKIRVNVVAPELI 191
Cdd:cd05339   151 SKAAAVGFHESLRLELKAygkPGIKTTLVCPYFI 184
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 3-203 1.12e-30

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: 112.97  E-value: 1.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd08944     4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDLLVN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGI-NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:cd08944    84 NAGAmHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLS----------SIAGQSGDPGYGAYGAS 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAPELI--PRTVSIRKMEKG 203
Cdd:cd08944   154 KAAIRNLTRTLAAELRHAGIRCNALAPGLIdtPLLLAKLAGFEG 197
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-191 1.22e-30

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 113.18  E-value: 1.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAViarNLEGAKAAA-------GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK12935    7 KVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAenlvnelGKEGHDVYAVQADVSKVEDANRLVEEAVNHFG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK12935   84 KVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISIS----------SIIGQAGGFGQ 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK12935  154 TNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFI 189
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 2-188 1.66e-30

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 112.80  E-value: 1.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAV----IARNLEGAKAAAGDL--------GGDHLAFSCDVAkehDVQNTFEE 69
Cdd:cd05353     5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVndlgGDRKGSGKSSSAADKvvdeikaaGGKAVANYDSVE---DGEKIVKT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  70 LEKHLGRVNFLVNAAGINRDGLLVRTKTE--DMVSQLHtnLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIV 147
Cdd:cd05353    82 AIDAFGRVDILVNNAGILRDRSFAKMSEEdwDLVMRVH--LKGSFKVTRAAWPYMRKQKFGRIINTS----------SAA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462599477 148 GLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05353   150 GLYGNFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAP 190
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 3-191 3.25e-30

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 111.81  E-value: 3.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFS-CDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK12828    8 KVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGgIDLVDPQAARRAVDEVNRQFGRLDALV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:PRK12828   88 NIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIG----------AGAALKAGPGMGAYAAA 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK12828  158 KAGVARLTEALAAELLDRGITVNAVLPSII 187
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 3-188 3.61e-30

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: 111.06  E-value: 3.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd08929     1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd08929    81 NAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVG----------SLAGKNAFKGGAAYNASK 150

                         170       180
                  ....*....|....*....|....*.
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08929   151 FGLLGLSEAAMLDLREANIRVVNVMP 176
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-191 1.31e-29

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 110.53  E-value: 1.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGG-DHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12829   10 DGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGaKVTATVADVADPAQVERVFDTAVERFGGLDV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGI-NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK12829   90 LVNNAGIaGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhGGVIIALS----------SVAGRLGYPGRTP 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK12829  160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPGIV 193
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-191 1.37e-29

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 110.19  E-value: 1.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIA----RNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKH 73
Cdd:PRK12827    5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVLDihpmRGRAEADAVAAGIeaaGGKALGLAFDVRDFAATRAALDAGVEE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  74 LGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQ-QQGGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:PRK12827   85 FGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIA----------SVAGVRGN 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462599477 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK12827  155 RGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAI 193
PRK09730 PRK09730
SDR family oxidoreductase;
3-217 2.10e-29

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 109.55  E-value: 2.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK09730    2 AIALVTGGSRGIGRATALLLAQEGYTVAVnYQQNLHAAQEVVNLItqaGGKAFVLQADISDENQVVAMFTAIDQHDEPLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGInrdgLLVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQ---QGGSIVNVGhrremllhkrSIVGLK 150
Cdd:PRK09730   82 ALVNNAGI----LFTQCTVENLTAErinrvLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVS----------SAASRL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477 151 GNSGQSV-YSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKG--DRINVTLrsPEQHG 217
Cdd:PRK09730  148 GAPGEYVdYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGrvDRVKSNI--PMQRG 215
PRK07035 PRK07035
SDR family oxidoreductase;
3-190 2.43e-29

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 109.72  E-value: 2.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07035    9 KIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIvaaGGKAEALACHIGEMEQIDALFAHIRERHGRLDI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGIN-------RDGLLVRTKTEDMvsqlhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:PRK07035   89 LVNNAAANpyfghilDTDLGAFQKTVDV------NIRGYFFMSVEAGKLMKEQGGGSIVNVA----------SVNGVSPG 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462599477 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPEL 190
Cdd:PRK07035  153 DFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGL 190
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 4-187 2.58e-29

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 109.01  E-value: 2.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05360     2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVrelGGEAIAVVADVADAAQVERAADTAVERFGRIDTW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:cd05360    82 VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVG----------SLLGYRSAPLQAAYSA 151

                         170       180
                  ....*....|....*....|....*..
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:cd05360   152 SKHAVRGFTESLRAELAHDGAPISVTL 178
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 1-190 3.65e-29

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: 109.30  E-value: 3.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGdlGGDHLAFS-CDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05371     1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK--LGDNCRFVpVDVTSEKDVKAALALAKAKFGRLDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGI-------NRDGLLVRtKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG------GSIVNVGhrremllhkrSI 146
Cdd:cd05371    79 VVNCAGIavaaktyNKKGQQPH-SLELFQRVINVNLIGTFNVIRLAAGAMGKNEPdqggerGVIINTA----------SV 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 147 VGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPEL 190
Cdd:cd05371   148 AAFEGQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGL 191
PRK06123 PRK06123
SDR family oxidoreductase;
1-191 4.59e-29

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 108.71  E-value: 4.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKA---AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK06123    1 MRKVMIITGASRGIGAATALLAAERGYAVCLnYLRNRDAAEAvvqAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGInrdgLLVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQ---QGGSIVNVGhrremllhkrSIVG 148
Cdd:PRK06123   81 LDALVNNAGI----LEAQMRLEQMDAArltriFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVS----------SMAA 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 149 LKGNSGQSV-YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK06123  147 RLGSPGEYIdYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVI 190
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 2-188 4.79e-29

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 110.78  E-value: 4.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07109    8 RQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIraaGGEALAVVADVADAEAVQAAADRAEEELGPID 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremLLHKRSIVgLkgnsgQSVY 158
Cdd:PRK07109   88 TWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGS----ALAYRSIP-L-----QSAY 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 159 SASKGGLVGFSRALAKEV--ARKKIRVNVVAP 188
Cdd:PRK07109  158 CAAKHAIRGFTDSLRCELlhDGSPVSVTMVQP 189
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 2-188 5.36e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 108.66  E-value: 5.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06057    7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVGG--LFVPTDVTDEDAVNALFDTAAETYGSVDIAF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGIN--RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN-SGQSVY 158
Cdd:PRK06057   85 NNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTA----------SFVAVMGSaTSQISY 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06057  155 TASKGGVLAMSRELGVQFARQGIRVNALCP 184
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 1-188 7.53e-29

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: 108.62  E-value: 7.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLE-GAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05366     1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEeAAKSTIQEIseaGYNAVAVGADVTDKDDVEALIDQAVEKFGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05366    81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINAS----------SIAGVQGFPNL 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05366   151 GAYSASKFAVRGLTQTAAQELAPKGITVNAYAP 183
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 3-188 9.98e-29

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: 107.45  E-value: 9.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDlGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd08932    80 NAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLN----------SLSGKRVLAGNAGYSASK 149

                         170       180
                  ....*....|....*....|....*.
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08932   150 FALRALAHALRQEGWDHGVRVSAVCP 175
PRK09072 PRK09072
SDR family oxidoreductase;
9-188 1.37e-28

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 108.11  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEG--AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHlGRVNFLVNAAGI 86
Cdd:PRK09072   12 GASGGIGQALAEALAAAGARLLLVGRNAEKleALAARLPYPGRHRWVVADLTSEAGREAVLARAREM-GGINVLINNAGV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLV 166
Cdd:PRK09072   91 NHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVG----------STFGSIGYPGYASYCASKFALR 160

                         170       180
                  ....*....|....*....|..
gi 2462599477 167 GFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK09072  161 GFSEALRRELADTGVRVLYLAP 182
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 2-188 2.53e-28

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: 106.77  E-value: 2.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05326     4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFvHCDVTVEADVRAAVDTAVARFGRLDIM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGI--NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:cd05326    84 FNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVA----------SVAGVVGGLGPHAY 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05326   154 TASKHAVLGLTRSAATELGEHGIRVNCVSP 183
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 1-188 3.32e-28

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 107.04  E-value: 3.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK12384    1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYgegmaYGFGADATSEQSVLALSRGVDEIFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllHKRSIVGLKGNSG 154
Cdd:PRK12384   81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDgIQGRIIQIN-------SKSGKVGSKHNSG 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 155 qsvYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12384  154 ---YSAAKFGGVGLTQSLALDLAEYGITVHSLML 184
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 3-188 5.09e-28

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 105.98  E-value: 5.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAViarNLEGAKAAAGDL-------GGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK12937    6 KVAIVTGASRGIGAAIARRLAADGFAVAV---NYAGSAAAADELvaeieaaGGRAIAVQADVADAAAVTRLFDAAETAFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVghrremllhKRSIVGLKGNSGq 155
Cdd:PRK12937   83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINL---------STSVIALPLPGY- 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12937  151 GPYAASKAAVEGLVHVLANELRGRGITVNAVAP 183
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 3-194 5.53e-28

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 105.94  E-value: 5.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN-----------LEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTF 67
Cdd:cd05338     4 KVAFVTGASRGIGRAIALRLAKAGATVVVAAKTasegdngsaksLPGtieeTAEEIEAAGGQALPIVVDVRDEDQVRALV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  68 EELEKHLGRVNFLVNAAGInrdglLVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllh 142
Cdd:cd05338    84 EATVDQFGRLDILVNNAGA-----IWLSLVEDTPAKrfdlmQRVNLRGTYLLSQAALPHMVKAGQGHILNIS-------- 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462599477 143 krSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRT 194
Cdd:cd05338   151 --PPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIET 200
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 3-191 5.78e-28

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: 105.70  E-value: 5.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08934     4 KVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELeaeGGKALVLELDVTDEQQVDAAVERTVEALGRLDI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd08934    84 LVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNIS----------SVAGRVAVRNSAVYN 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd08934   154 ATKFGVNAFSEGLRQEVTERGVRVVVIEPGTV 185
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 2-202 7.31e-28

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 106.66  E-value: 7.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06701   46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdaneTKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELGRL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAG--INRDGLlvrtktEDMVSQ-----LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLK 150
Cdd:PRK06701  126 DILVNNAAfqYPQQSL------EDITAEqldktFKTNIYSYFHMTKAALPHL--KQGSAIINTG----------SITGYE 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599477 151 GNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP-----ELIPRTVSIRKMEK 202
Cdd:PRK06701  188 GNETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPgpiwtPLIPSDFDEEKVSQ 244
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 2-188 8.85e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 105.86  E-value: 8.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06198    6 GKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELealGAKAVFVQADLSDVEDCRRVVAAADEAFGRL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK06198   86 DALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIG----------SMSAHGGQPFLA 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06198  156 AYCASKGALATLTRNAAYALLRNRIRVNGLNI 187
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 9-188 1.00e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 106.15  E-value: 1.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINR 88
Cdd:PRK06180   11 GVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVLVNNAGYGH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  89 DGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYSASKGGLVGF 168
Cdd:PRK06180   91 EGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNI----------TSMGGLITMPGIGYYCGSKFALEGI 160

                         170       180
                  ....*....|....*....|
gi 2462599477 169 SRALAKEVARKKIRVNVVAP 188
Cdd:PRK06180  161 SESLAKEVAPFGIHVTAVEP 180
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
3-193 1.43e-27

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 109.55  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGG--DHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK08324  423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGpdRALGVACDVTDEAAVQAAFEEAALAFGGVDIV 502

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllHKRSIVGLKGNSGqsvYS 159
Cdd:PRK08324  503 VSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIA-------SKNAVNPGPNFGA---YG 572

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELIPR 193
Cdd:PRK08324  573 AAKAAELHLVRQLALELGPDGIRVNGVNPDAVVR 606
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 2-188 1.64e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 105.41  E-value: 1.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07825    5 GKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVV-GGPLDVTDPASFAAFLDAVEADLGPIDVLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:PRK07825   84 NNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVA----------SLAGKIPVPGMATYCAS 153

                         170       180
                  ....*....|....*....|....*..
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07825  154 KHAVVGFTDAARLELRGTGVHVSVVLP 180
PRK07454 PRK07454
SDR family oxidoreductase;
9-188 3.52e-27

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 103.89  E-value: 3.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK07454   13 GASSGIGKATALAFAKAGWDLALVARSqdaLEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDVLINNAG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGL 165
Cdd:PRK07454   93 MAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVS----------SIAARNAFPQWGAYCVSKAAL 162

                         170       180
                  ....*....|....*....|...
gi 2462599477 166 VGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07454  163 AAFTKCLAEEERSHGIRVCTITL 185
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 6-191 4.43e-27

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: 103.56  E-value: 4.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH---LAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05350     2 LITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNpsvEVEILDVTDEERNQLVIAELEAELGGLDLVII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05350    82 NAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLIS----------SVAALRGLPGAAAYSASK 151

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05350   152 AALSSLAESLRYDVKKRGIRVTVINPGFI 180
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
1-188 5.67e-27

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 103.65  E-value: 5.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08643    1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLskdGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINrDGLLVRTKTEDMVSQLH-TNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK08643   81 NVVVNNAGVA-PTTPIETITEEQFDKVYnINVGGVIWGIQAAQEAFKKLgHGGKIINAT----------SQAGVVGNPEL 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08643  150 AVYSSTKFAVRGLTQTAARDLASEGITVNAYAP 182
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 3-188 1.02e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 102.49  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFscDVAKEHDVQNTFEELekhlGRVNFLVN 82
Cdd:PRK07060   10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRL--DVGDDAAIRAALAAA----GAFDGLVN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMI-QQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:PRK07060   84 CAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIaAGRGGSIVNVS----------SQAALVGLPDHLAYCAS 153

                         170       180
                  ....*....|....*....|....*..
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07060  154 KAALDAITRVLCVELGPHGIRVNSVNP 180
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 1-184 1.17e-26

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: 102.93  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA----GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05322     1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVAdeinAEYGEKAYGFGADATNEQSVIALSKGVDEIFKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllHKRSIVGLKGNSGq 155
Cdd:cd05322    81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDgIQGRIIQIN-------SKSGKVGSKHNSG- 152

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 156 svYSASKGGLVGFSRALAKEVARKKIRVN 184
Cdd:cd05322   153 --YSAAKFGGVGLTQSLALDLAEHGITVN 179
PRK06124 PRK06124
SDR family oxidoreductase;
3-188 1.20e-26

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 102.87  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06124   12 QVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALraaGGAAEALAFDIADEEAVAAAFARIDAEHGRLDI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGI-NRDGLLvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVY 158
Cdd:PRK06124   92 LVNNVGArDRRPLA-ELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAI----------TSIAGQVARAGDAVY 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06124  161 PAAKQGLTGLMRALAAEFGPHGITSNAIAP 190
PRK06947 PRK06947
SDR family oxidoreductase;
1-191 1.43e-26

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 102.19  E-value: 1.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK06947    1 MRKVVLITGASRGIGRATAVLAAARGWSVGInYARDAAAAEETADavrAAGGRACVVAGDVANEADVIAMFDAVQSAFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGL-LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ---GGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:PRK06947   81 LDALVNNAGIVAPSMpLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrGGAIVNVS----------SIASRLGS 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462599477 153 SGQSV-YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK06947  151 PNEYVdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLI 190
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 1-188 1.57e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 102.81  E-value: 1.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK08263    2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK08263   82 VNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQIS----------SIGGISAFPMSGIYHA 151

                         170       180
                  ....*....|....*....|....*...
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08263  152 SKWALEGMSEALAQEVAEFGIKVTLVEP 179
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
3-191 3.72e-26

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 101.24  E-value: 3.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV--------IARNLEGAKAaagdLGGDHLAFSCDVAKEHDVQNTFEELEKHL 74
Cdd:PRK12938    4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnsprRVKWLEDQKA----LGFDFIASEGNVGDWDSTKAAFDKVKAEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG 154
Cdd:PRK12938   80 GEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINIS----------SVNGQKGQFG 149

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462599477 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK12938  150 QTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYI 186
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-188 4.57e-26

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: 100.93  E-value: 4.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05345     4 EGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGI---NRDGLLVRTKTEDMVSQLhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:cd05345    84 VNNAGIthrNKPMLEVDEEEFDRVFAV--NVKSIYLSAQALVPHMEEQGGGVIINIA----------STAGLRPRPGLTW 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05345   152 YNASKGWVVTATKAMAVELAPRNIRVNCLCP 182
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 2-188 4.90e-26

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 101.52  E-value: 4.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08277   10 GKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIkaaGGEALAVKADVLDKESLEQARQQILEDFGPCD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINR---------DGLLVRTKT------EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhk 143
Cdd:PRK08277   90 ILINGAGGNHpkattdnefHELIEPTKTffdldeEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINIS--------- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462599477 144 rSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08277  161 -SMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAP 204
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 2-191 5.05e-26

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: 100.95  E-value: 5.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA------AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:cd05364     3 GKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEEtrqsclQAGVSEKKILLVVADLTEEEGQDRIISTTLAKFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQgGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05364    83 RLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVS----------SVAGGRSFPGV 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05364   152 LYYCISKAALDQFTRCTALELAPKGVRVNSVSPGVI 187
PRK07074 PRK07074
SDR family oxidoreductase;
1-188 9.72e-26

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 100.23  E-value: 9.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-LAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07074    1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARfVPVACDLTDAASLAAALANAAAERGPVDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGnSGQSVYS 159
Cdd:PRK07074   81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIG----------SVNGMAA-LGHPAYS 149

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07074  150 AAKAGLIHYTKLLAVEYGRFGIRANAVAP 178
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-194 1.66e-25

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 99.78  E-value: 1.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR-VN 78
Cdd:PRK08642    4 SEQTVLVTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGKpIT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAA-------GINRDGLLVRTkTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRremlLHKRSIVGLKG 151
Cdd:PRK08642   84 TVVNNAladfsfdGDARKKADDIT-WEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTN----LFQNPVVPYHD 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462599477 152 nsgqsvYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRT 194
Cdd:PRK08642  159 ------YTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTT 195
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 3-203 2.26e-25

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: 99.39  E-value: 2.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD--LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd08943     2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAaqGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllHKRSIVGLKGNSGqsvYS 159
Cdd:cd08943    82 VSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNA-------SKNAVAPGPNAAA---YS 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKG 203
Cdd:cd08943   152 AAKAAEAHLARCLALEGGEDGIRVNTVNPDAVFRGSKIWEGVWR 195
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 1-215 3.94e-25

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


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 98.81  E-value: 3.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDhLAFSC--DVAKEHDVQNTFEELEKHLG 75
Cdd:cd05332     2 QGKVVIITGASSGIGEELAYHLARLGARLVLSARReerLEEVKSECLELGAP-SPHVVplDMSDLEDAEQVVEEALKLFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05332    81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVS----------SIAGKIGVPFR 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRTVSIRK-------MEKGDRINVTLRSPEQ 215
Cdd:cd05332   151 TAYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNAlsgdgsmSAKMDDTTANGMSPEE 217
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-191 4.13e-25

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 101.45  E-value: 4.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAA----AGDLGGDHLAfsCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08261  211 KVALVTGAARGIGAAIAEVLARDGAH--VVCLDVPAAGEAlaavANRVGGTALA--LDITAPDAPARIAEHLAERHGGLD 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTE--DMVsqLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK08261  287 IVVHNAGITRDKTLANMDEArwDSV--LAVNLLAPLRITEALLAAGALGDGGRIVGVS----------SISGIAGNRGQT 354

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK08261  355 NYAASKAGVIGLVQALAPLLAERGITINAVAPGFI 389
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
2-188 8.31e-25

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 97.79  E-value: 8.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07067    6 GKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK07067   86 NNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMA----------SQAGRRGEALVSHYCA 155

                         170       180
                  ....*....|....*....|....*...
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07067  156 TKAAVISYTQSAALALIRHGINVNAIAP 183
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 1-188 1.15e-24

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: 97.40  E-value: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd08930     1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELtnlyKNRVIALELDITSKESIKELIESYLEKFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVR---TKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGL---- 149
Cdd:cd08930    81 IDILINNAYPSPKVWGSRfeeFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIA----------SIYGViapd 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462599477 150 ----KGNSGQS--VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08930   151 friyENTQMYSpvEYSVIKAGIIHLTKYLAKYYADTGIRVNAISP 195
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 2-202 1.15e-24

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: 97.75  E-value: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA-----AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05355    26 GKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAeetkkLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05355   106 LDILVNNAAYQHPQESIEDITTEQLEKtFRTNIFSMFYLTKAALPHL--KKGSSIINTT----------SVTAYKGSPHL 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP-----ELIPRTVSIRKMEK 202
Cdd:cd05355   174 LDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPgpiwtPLIPSSFPEEKVSE 225
PRK06181 PRK06181
SDR family oxidoreductase;
2-188 1.28e-24

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 97.36  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06181    1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNetrLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQgGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK06181   81 ILVNNAGITMWSRFDELTDLSVFERVmRVNYLGAVYCTHAALPHLKASR-GQIVVVS----------SLAGLTGVPTRSG 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06181  150 YAASKHALHGFFDSLRIELADDGVAVTVVCP 180
PRK08628 PRK08628
SDR family oxidoreductase;
2-188 1.37e-24

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 97.34  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK08628    7 DKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEElrALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINrDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMrTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK08628   87 LVNNAGVN-DGVGLEAGREAFVASLERNLIHYYVMAHYCL-PHLKASRGAIVNIS----------SKTALTGQGGTSGYA 154

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08628  155 AAKGAQLALTREWAVALAKDGVRVNAVIP 183
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-188 1.68e-24

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 97.27  E-value: 1.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK13394    8 KTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVAdeiNKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQ-QQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK13394   88 LVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMG----------SVHSHEASPLKSAY 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK13394  158 VTAKHGLLGLARVLAKEGAKHNVRSHVVCP 187
PRK05867 PRK05867
SDR family oxidoreductase;
7-191 4.33e-24

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 95.87  E-value: 4.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK05867   14 ITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIgtsGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDIAVCN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSV--YSA 160
Cdd:PRK05867   94 AGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTA----------SMSGHIINVPQQVshYCA 163

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK05867  164 SKAAVIHLTKAMAVELAPHKIRVNSVSPGYI 194
PRK06398 PRK06398
aldose dehydrogenase; Validated
 2-203 4.55e-24

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 96.05  E-value: 4.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGakaaagDLGGDHlaFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06398    6 DKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPS------YNDVDY--FKVDVSNKEQVIKGIDYVISKYGRIDILV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLLHKRSivglkgnsgqSVYSAS 161
Cdd:PRK06398   78 NNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNA----------AAYVTS 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 162 KGGLVGFSRALAKEVArKKIRVNVVAPELI--PRTVSIRKMEKG 203
Cdd:PRK06398  148 KHAVLGLTRSIAVDYA-PTIRCVAVCPGSIrtPLLEWAAELEVG 190
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 2-215 1.16e-23

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


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 94.21  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVqntFEELEKHLGR- 76
Cdd:cd05356     1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYgvetKTIAADFSAGDDI---YERIEKELEGl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 -VNFLVNAAGINRD--GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNS 153
Cdd:cd05356    78 dIGILVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNIS----------SFAGLIPTP 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599477 154 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIprtVSirKMEKGDRINVTLRSPEQ 215
Cdd:cd05356   148 LLATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLV---AT--KMSKIRKSSLFVPSPEQ 204
PRK05650 PRK05650
SDR family oxidoreductase;
9-188 1.21e-23

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 95.11  E-value: 1.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK05650    7 GAASGLGRAIALRWAREGWRLALADVNEEGGEETLkllREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVNNAG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGL 165
Cdd:PRK05650   87 VASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIA----------SMAGLMQGPAMSSYNVAKAGV 156

                         170       180
                  ....*....|....*....|...
gi 2462599477 166 VGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05650  157 VALSETLLVELADDEIGVHVVCP 179
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-212 1.24e-23

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 94.85  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06463    7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKGV--FTIKCDVGNRDQVKKSKEVVEKEFGRVDVLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGI-------NRDgllvRTKTEDMVSqlhTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGL-KGNS 153
Cdd:PRK06463   85 NNAGImylmpfeEFD----EEKYNKMIK---INLNGAIYTTYEFLPLLKLSKNGAIVNIA----------SNAGIgTAAE 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462599477 154 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPR--TVSIRKMEKGDRINVTLRS 212
Cdd:PRK06463  148 GTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETdmTLSGKSQEEAEKLRELFRN 208
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 2-188 2.15e-23

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: 94.14  E-value: 2.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG----GDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd08933     9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNragpGSCKFVPCDVTKEEDIKTLISVTVERFGRI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLV-RTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGgSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:cd08933    89 DCLVNNAGWHPPHQTTdETSAQEFRDLLNLNLISYFLASKYALPHLRKSQG-NIINLS----------SLVGSIGQKQAA 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08933   158 PYVATKGAITAMTKALAVDESRYGVRVNCISP 189
PRK08589 PRK08589
SDR family oxidoreductase;
2-191 2.39e-23

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 94.46  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKG-YRLAV-IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK08589    6 NKVAVITGASTGIGQASAIALAQEGaYVLAVdIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQqGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK08589   86 LFNNAGVDNAAGRIHEYPVDVFDKiMAVDMRGTFLMTKMLLPLMMEQ-GGSIINTS----------SFSGQAADLYRSGY 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK08589  155 NAAKGAVINFTKSIAIEYGRDGIRANAIAPGTI 187
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 4-183 2.73e-23

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: 93.60  E-value: 2.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA----AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEAllvdIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd05373    81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTG----------ATASLRGRAGFAAFA 150

                         170       180
                  ....*....|....*....|....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRV 183
Cdd:cd05373   151 GAKFALRALAQSMARELGPKGIHV 174
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
3-202 5.33e-23

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 93.33  E-value: 5.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA--GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK08226    7 KTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADelCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVG-LKGNSGQSVYS 159
Cdd:PRK08226   87 VNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMS----------SVTGdMVADPGETAYA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVSIRKMEK 202
Cdd:PRK08226  157 LTKAAIVGLTKSLAVEYAQSGIRVNAICPGYV-RTPMAESIAR 198
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 2-191 5.59e-23

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 93.25  E-value: 5.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR-NLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08936    7 GKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIkkaGGEAIAVKGDVTVESDVVNLIQTAVKEFGTL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGHRREML-----LHkrsivglkg 151
Cdd:PRK08936   87 DVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIpwplfVH--------- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462599477 152 nsgqsvYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK08936  158 ------YAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAI 191
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 9-197 5.88e-23

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: 92.73  E-value: 5.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAA 84
Cdd:cd05346     7 GASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFpvkvLPLQLDVSDRESIEAALENLPEEFRDIDILVNNA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  85 GINRdGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05346    87 GLAL-GLdpAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLG----------SIAGRYPYAGGNVYCATK 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAPELIPRTVSI 197
Cdd:cd05346   156 AAVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSL 190
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 7-191 7.13e-23

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: 92.51  E-value: 7.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHL-GRVNFLVN 82
Cdd:cd05329    11 VTGGTKGIGYAIVEELAGLGAEVYTCARNqkeLDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFgGKLNILVN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05329    91 NAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFIS----------SVAGVIAVPSGAPYGATK 160

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05329   161 GALNQLTRSLACEWAKDNIRVNAVAPWVI 189
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 3-188 9.69e-23

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: 92.15  E-value: 9.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELekhlGRVNFLVN 82
Cdd:cd05368     3 KVALITAAAQGIGRAIALAFAREGAN--VIATDINEEKLKELERGPGITTRVLDVTDKEQVAALAKEE----GRIDVLFN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVG-LKGNSGQSVYSAS 161
Cdd:cd05368    77 CAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMS----------SVASsIKGVPNRFVYSTT 146

                         170       180
                  ....*....|....*....|....*..
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05368   147 KAAVIGLTKSVAADFAQQGIRCNAICP 173
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 2-188 1.04e-22

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 92.38  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK08265    6 GKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFGRVDILV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 N-AAGINRDGLlvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK08265   86 NlACTYLDDGL--ASSRADWLAALDVNLVSAAMLAQAAHPHLA-RGGGAIVNFT----------SISAKFAQTGRWLYPA 152

                         170       180
                  ....*....|....*....|....*...
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08265  153 SKAAIRQLTRSMAMDLAPDGIRVNSVSP 180
PRK07856 PRK07856
SDR family oxidoreductase;
2-191 1.08e-22

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 92.30  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlegAKAAAGDLGGDHLAfsCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07856    6 GRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR---APETVDGRPAEFHA--ADVRDPDQVAALVDAIVERHGRLDVLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK07856   81 NNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQpGGGSIVNIG----------SVSGRRPSPGTAAYGA 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 161 SKGGLVGFSRALAKEVArKKIRVNVVAPELI 191
Cdd:PRK07856  151 AKAGLLNLTRSLAVEWA-PKVRVNAVVVGLV 180
PRK06114 PRK06114
SDR family oxidoreductase;
2-188 1.17e-22

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 92.15  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD----LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06114    8 GQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEhieaAGRRAIQIAADVTSKADLRAAVARTEAELGAL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRdgllvRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:PRK06114   88 TLAVNAAGIAN-----ANPAEEMEEEqwqtvMDINLTGVFLSCQAEARAMLENGGGSIVNIA----------SMSGIIVN 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462599477 153 SG--QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06114  153 RGllQAHYNASKAGVIHLSKSLAMEWVGRGIRVNSISP 190
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 3-188 1.17e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 92.27  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDhlafsCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06179    5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPGVELLE-----LDVTDDASVQAAVDEVIARAGRIDVLVN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:PRK06179   80 NAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINIS----------SVLGFLPAPYMALYAASK 149

                         170       180
                  ....*....|....*....|....*.
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06179  150 HAVEGYSESLDHEVRQFGIRVSLVEP 175
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 3-205 1.60e-22

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 92.05  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV---IARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07097   11 KIALITGASYGIGFAIAKAYAKAGATIVFndiNQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK07097   91 LVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINIC----------SMMSELGRETVSAYA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAPELI--PRTVSIR-KMEKGDR 205
Cdd:PRK07097  161 AAKGGLKMLTKNIASEYGEANIQCNGIGPGYIatPQTAPLReLQADGSR 209
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 2-188 1.67e-22

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: 92.14  E-value: 1.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd08935     5 NKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEItalGGRAIALAADVLDRASLERAREEIVAQFGTVD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINR-------DGLLVRTKT-------EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkr 144
Cdd:cd08935    85 ILINGAGGNHpdattdpEHYEPETEQnffdldeEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINIS---------- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 145 SIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08935   155 SMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAP 198
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 2-188 1.70e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 91.56  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR---NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07890    5 GKVVVVSGVGPGLGRTLAVRAARAGADVVLAARtaeRLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVN-AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQqGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK07890   85 ALVNnAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAES-GGSIVMIN----------SMVLRHSQPKYGA 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07890  154 YKMAKGALLAASQSLATELGPQGIRVNSVAP 184
PRK06914 PRK06914
SDR family oxidoreductase;
1-188 1.91e-22

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 92.01  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAK-----AAAGDLGGDHLAFSCDVAKEHDVQNtFEELEKHLG 75
Cdd:PRK06914    2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQEnllsqATQLNLQQNIKVQQLDVTDQNSIHN-FQLVLKEIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK06914   81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINIS----------SISGRVGFPGL 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06914  151 SPYVSSKYALEGFSESLRLELKPFGIDVALIEP 183
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 2-188 2.01e-22

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 91.44  E-value: 2.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG--DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08937     4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEilAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGinrdGLLVR-----TKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNsg 154
Cdd:cd08937    84 LINNVG----GTIWAkpyehYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVS----------SIATRGIY-- 147

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08937   148 RIPYSAAKGGVNALTASLAFEHARDGIRVNAVAP 181
PRK07774 PRK07774
SDR family oxidoreductase;
2-191 2.09e-22

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 91.34  E-value: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07774    6 DKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIvadGGTAIAVQVDVSDPDSAKAMADATVSAFGGID 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRD---GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNvghrremllhkRSIVGLKGNSGq 155
Cdd:PRK07774   86 YLVNNAAIYGGmklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVN-----------QSSTAAWLYSN- 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 156 sVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK07774  154 -FYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPI 188
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 7-191 3.72e-22

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: 90.49  E-value: 3.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05359     3 VTGGSRGIGKAIALRLAERGADVVInYRKSKDAAAEVAAEieeLGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVLVS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 --AAGINRDglLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:cd05359    83 naAAGAFRP--LSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAIS----------SLGSIRALPNYLAVGT 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05359   151 AKAALEALVRYLAVELGPRGIRVNAVSPGVI 181
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 2-191 4.51e-22

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: 90.76  E-value: 4.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05363     3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDILV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:cd05363    83 NNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMA----------SQAGRRGEALVGVYCA 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05363   153 TKAAVISLTQSAGLNLIRHGINVNAIAPGVV 183
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 6-203 5.00e-22

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: 89.82  E-value: 5.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   6 AVF--GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEEL-EKHLGRVNFLV 81
Cdd:cd08931     2 AIFitGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVvAGALDVTDRAAWAAALADFaAATGGRLDALF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:cd08931    82 NNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTA----------SSSAIYGQPDLAVYSAT 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVSIRKMEKG 203
Cdd:cd08931   152 KFAVRGLTEALDVEWARHGIRVADVWPWFV-DTPILTKGETG 192
PRK09242 PRK09242
SDR family oxidoreductase;
2-194 5.06e-22

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 90.58  E-value: 5.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK09242    9 GQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeefpEREVHGLAADVSDDEDRRAILDWVEDHWDG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINrdgllVRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKG 151
Cdd:PRK09242   89 LHILVNNAGGN-----IRKAAIDYTEDewrgiFETNLFSAFELSRYAHPLLKQHASSAIVNIG----------SVSGLTH 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462599477 152 NSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI--PRT 194
Cdd:PRK09242  154 VRSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIrtPLT 198
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 3-188 6.00e-22

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: 89.60  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKG-YRLAVIARNLEGAKAAAGDLGGDHL---AFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLRAEGLsvrFHQLDVTDDASIEAAADFVEEKYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGlkgnSGQSV 157
Cdd:cd05324    81 ILVNNAGIAFKGFDDSTPTREQAREtMKTNFFGTVDVTQALLPLLKKSPAGRIVNVS----------SGLG----SLTSA 146

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05324   147 YGVSKAALNALTRILAKELKETGIKVNACCP 177
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 2-195 6.21e-22

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 90.39  E-value: 6.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN--LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12823    8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSelVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGinrdGLlVRTK------TEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremlLHKRSIvglkgns 153
Cdd:PRK12823   88 LINNVG----GT-IWAKpfeeyeEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSS-----IATRGI------- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462599477 154 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP---ELIPRTV 195
Cdd:PRK12823  151 NRVPYSAAKGGVNALTASLAFEYAEHGIRVNAVAPggtEAPPRRV 195
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 2-191 1.01e-21

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: 89.89  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05330     3 DKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALleiapDAEVLLIKADVSDEAQVEAYVDATVEQFGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGIN-RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd05330    83 IDGFFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTA----------SVGGIRGVGNQ 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05330   153 SGYAAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAI 188
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 2-188 2.74e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 88.45  E-value: 2.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07478    6 GKVAIITGASSGIGRAAAKLFAREGAKVVVGARRqaeLDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGGLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGSIVN----VGHRremllhkrsiVGLKGNS 153
Cdd:PRK07478   86 IAFNNAGTLGEMGPVAEMSLEGWREtLATNLTSAFLGAKHQIPAMLARGGGSLIFtstfVGHT----------AGFPGMA 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462599477 154 gqsVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07478  156 ---AYAASKAGLIGLTQVLAAEYGAQGIRVNALLP 187
PRK07831 PRK07831
SDR family oxidoreductase;
13-190 2.80e-21

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 88.55  E-value: 2.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  13 GIGRAVAQLMARKGYRLAVI---ARNL-EGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGIN 87
Cdd:PRK07831   29 GIGSATARRALEEGARVVISdihERRLgETADELAAELGLGRVeAVVCDVTSEAQVDALIDAAVERLGRLDVLVNNAGLG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  88 RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMI-QQQGGSIVNvghrremllhKRSIVGLKGNSGQSVYSASKGGLV 166
Cdd:PRK07831  109 GQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRaRGHGGVIVN----------NASVLGWRAQHGQAHYAAAKAGVM 178

                         170       180
                  ....*....|....*....|....
gi 2462599477 167 GFSRALAKEVARKKIRVNVVAPEL 190
Cdd:PRK07831  179 ALTRCSALEAAEYGVRINAVAPSI 202
PRK08267 PRK08267
SDR family oxidoreductase;
6-191 3.02e-21

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 88.46  E-value: 3.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   6 AVF--GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHL-AFSCDVAKEHDVQNTFEELEKHL-GRVNFLV 81
Cdd:PRK08267    3 SIFitGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAwTGALDVTDRAAWDAALADFAAATgGRLDVLF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSAS 161
Cdd:PRK08267   83 NNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTS----------SASAIYGQPGLAVYSAT 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK08267  153 KFAVRGLTEALDLEWRRHGIRVADVMPLFV 182
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 3-188 4.26e-21

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 88.02  E-value: 4.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKaaagdlgGDHLA-FSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK08220    9 KTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQE-------DYPFAtFVLDVSDAAAVAQVCQRLLAETGPLDVLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGH------RREMllhkrsivglkgnsgq 155
Cdd:PRK08220   82 NAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSnaahvpRIGM---------------- 145

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08220  146 AAYGASKAALTSLAKCVGLELAPYGVRCNVVSP 178
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 7-188 4.97e-21

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: 87.52  E-value: 4.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAGdlgGDHL-AFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:cd05331     3 VTGAAQGIGRAVARHLLQAGAT--VIALDLPFVLLLEY---GDPLrLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGL 165
Cdd:cd05331    78 VLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVA----------SNAAHVPRISMAAYGASKAAL 147

                         170       180
                  ....*....|....*....|...
gi 2462599477 166 VGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05331   148 ASLSKCLGLELAPYGVRCNVVSP 170
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 1-188 7.30e-21

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 87.50  E-value: 7.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGyrlAVIARNLEGAKA--------AAGDLGGDHLAFSCDVAKEHDVQNTFEELEK 72
Cdd:cd08940     1 KGKVALVTGSTSGIGLGIARALAAAG---ANIVLNGFGDAAeieavragLAAKHGVKVLYHGADLSKPAAIEDMVAYAQR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  73 HLGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:cd08940    78 QFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIA----------SVHGLVAS 147

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08940   148 ANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICP 183
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-202 1.11e-20

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 87.10  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIA--RNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06935   16 KVAIVTGGNTGLGQGYAVALAKAGADIIITThgTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDIL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK06935   96 VNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIA----------SMLSFQGGKFVPAYTA 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVAPELIP--RTVSIRKMEK 202
Cdd:PRK06935  166 SKHGVAGLTKAFANELAAYNIQVNAIAPGYIKtaNTAPIRADKN 209
PRK12743 PRK12743
SDR family oxidoreductase;
1-188 1.30e-20

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 86.63  E-value: 1.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-ARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK12743    1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITwHSDEEGAKETAEEvrsHGVRAEIRQLDLSDLPEGAQALDKLIQRLGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGHRREmllHKRSIvglkgnsGQ 155
Cdd:PRK12743   81 IDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQgQGGRIINITSVHE---HTPLP-------GA 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12743  151 SAYTAAKHALGGLTKAMALELVEHGILVNAVAP 183
PRK07062 PRK07062
SDR family oxidoreductase;
2-184 1.50e-20

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 86.63  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK07062    8 GRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFpgarlLAARCDVLDEADVAAFAAAVEARFGG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK07062   88 VDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVN----------SLLALQPEPHMV 157

                         170       180
                  ....*....|....*....|....*...
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVN 184
Cdd:PRK07062  158 ATSAARAGLLNLVKSLATELAPKGVRVN 185
PLN02253 PLN02253
xanthoxin dehydrogenase
 3-205 1.59e-20

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 86.80  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLA--FSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PLN02253   19 KVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVcfFHCDVTVEDDVSRAVDFTVDKFGTLDIM 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PLN02253   99 VNNAGLTGPPCpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLC----------SVASAIGGLGPHAY 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKGDR 205
Cdd:PLN02253  169 TGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDER 215
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-187 1.66e-20

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 86.31  E-value: 1.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-ARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK08063    3 SGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEieaLGRKALAVKANVGDVEKIKEMFAQIDEEFGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVN--AAGINRDGLLVRTKTEDMVsqLHTNLLGSMLTCKAAMRTMIQQQGGSIVNV---GHRRemLLHKRSIVGlkg 151
Cdd:PRK08063   83 LDVFVNnaASGVLRPAMELEESHWDWT--MNINAKALLFCAQEAAKLMEKVGGGKIISLsslGSIR--YLENYTTVG--- 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 152 nsgqsvysASKGGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:PRK08063  156 --------VSKAALEALTRYLAVELAPKGIAVNAVS 183
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-191 1.97e-20

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 86.17  E-value: 1.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK12745    1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINDRpddeELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGI---NRDGLLvRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG------GSIVNVGhrremllhKRSIV 147
Cdd:PRK12745   81 IDCLVNNAGVgvkVRGDLL-DLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVS--------SVNAI 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 148 GLKGNSGQsvYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK12745  152 MVSPNRGE--YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLI 193
PRK07069 PRK07069
short chain dehydrogenase; Validated
 7-191 2.82e-20

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 85.53  E-value: 2.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARN-LEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK07069    4 ITGAAGGLGRAIARRMAEQGAKVFLTDINdAAGLDAFAAEINAAHgegvaFAAVQDVTDEAQWQALLAQAADAMGGLSVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK07069   84 VNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNIS----------SVAAFKAEPDYTAYNA 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 161 SKGGLVGFSRALAKEVARKK--IRVNVVAPELI 191
Cdd:PRK07069  154 SKAAVASLTKSIALDCARRGldVRCNSIHPTFI 186
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 2-191 3.19e-20

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: 85.64  E-value: 3.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05343     6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECqsagYPTLFPYQCDLSNEEQILSMFSAIRTQHQGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ--QGGSIVNV----GHRremllhkrsivgLKG 151
Cdd:cd05343    86 DVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERnvDDGHIINInsmsGHR------------VPP 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462599477 152 NSGQSVYSASKGGLVGFSRALAKEV--ARKKIRVNVVAPELI 191
Cdd:cd05343   154 VSVFHFYAATKHAVTALTEGLRQELreAKTHIRATSISPGLV 195
PRK07201 PRK07201
SDR family oxidoreductase;
3-181 4.36e-20

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 87.70  E-value: 4.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07201  372 KVVLITGASSGIGRATAIKVAEAGATVFLVARNgeaLDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDY 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGinRDgllVRTKTEDMVSQLH-------TNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrSIVGLKGN 152
Cdd:PRK07201  452 LVNNAG--RS---IRRSVENSTDRFHdyertmaVNYFGAVRLILGLLPHMRERRFGHVVNV-----------SSIGVQTN 515

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 153 SGQ-SVYSASKGGLVGFSRALAKEVARKKI 181
Cdd:PRK07201  516 APRfSAYVASKAALDAFSDVAASETLSDGI 545
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 9-192 7.38e-20

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: 84.44  E-value: 7.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINR 88
Cdd:COG3967    12 GGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLH-TIVLDVADPASIAALAEQVTAEFPDLNVLINNAGIMR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  89 DGLLVRTKT--EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLV 166
Cdd:COG3967    91 AEDLLDEAEdlADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVS----------SGLAFVPLAVTPTYSATKAALH 160

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 167 GFSRALakevaR---KKIRVNVVapELIP 192
Cdd:COG3967   161 SYTQSL-----RhqlKDTSVKVI--ELAP 182
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-191 7.68e-20

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 84.39  E-value: 7.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06077    6 DKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKkraeEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK06077   86 DILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIA----------SVAGIRPAYGLSI 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 158 YSASKGGLVGFSRALAKEVArKKIRVNVVAPELI 191
Cdd:PRK06077  154 YGAMKAAVINLTKYLALELA-PKIRVNAIAPGFV 186
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 9-188 1.07e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 84.04  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK08085   16 GSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLrqeGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVLINNAG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLlhkrsivglkGNSGQSVYSASKGGL 165
Cdd:PRK08085   96 IQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSEL----------GRDTITPYAASKGAV 165

                         170       180
                  ....*....|....*....|...
gi 2462599477 166 VGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08085  166 KMLTRGMCVELARHNIQVNGIAP 188
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 3-188 2.11e-19

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: 83.36  E-value: 2.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08945     4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELreaGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRT--MIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:cd08945    84 LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIA----------STGGKQGVVHAAP 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08945   154 YSASKHGVVGFTKALGLELARTGITVNAVCP 184
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-188 2.33e-19

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 82.70  E-value: 2.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAGDLGgdhlafscdvAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06550    4 MTKTVLITGAASGIGLAQARAFLAQGAQ--VYGVDKQDKPDLSGNFH----------FLQLDLSDDLEPLFDWVPSVDIL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGInRDGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVY 158
Cdd:PRK06550   72 CNTAGI-LDDYkpLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMC----------SIASFVAGGGGAAY 140

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 159 SASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06550  141 TASKHALAGFTKQLALDYAKDGIQVFGIAP 170
PRK07832 PRK07832
SDR family oxidoreductase;
3-188 2.53e-19

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 83.55  E-value: 2.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD---LGG---DHLAFscDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK07832    1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADaraLGGtvpEHRAL--DISDYDAVAAFAADIHAAHGS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK07832   79 MDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAgRGGHLVNVS----------SAAGLVALPWH 148

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07832  149 AAYSASKFGLRGLSEVLRFDLARHGIGVSVVVP 181
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 3-194 7.49e-19

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 82.41  E-value: 7.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV--IARNLEGAKAAAG----------DLGGDHLAFSCDVAKEHDVQNTFEEL 70
Cdd:PRK07791    7 RVVIVTGAGGGIGRAHALAFAAEGARVVVndIGVGLDGSASGGSaaqavvdeivAAGGEAVANGDDIADWDGAANLVDAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  71 EKHLGRVNFLVNAAGINRDGLLVRTKTE--DMVSQLHtnLLGSMLTCK-AAMRTMIQQQGGSIVNVghrreMLLHKRSIV 147
Cdd:PRK07791   87 VETFGGLDVLVNNAGILRDRMIANMSEEewDAVIAVH--LKGHFATLRhAAAYWRAESKAGRAVDA-----RIINTSSGA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462599477 148 GLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPelIPRT 194
Cdd:PRK07791  160 GLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP--AART 204
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 7-188 1.60e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 81.10  E-value: 1.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:PRK06523   14 VTGGTKGIGAATVARLLEAGARVVTTARS------RPDDLPEGVEFVAADLTTAEGCAAVARAVLERLGGVDILVHVLGG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 NR---DGLLVRTKtEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGH-RREMLLHKRSIVglkgnsgqsvYSASK 162
Cdd:PRK06523   88 SSapaGGFAALTD-EEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSiQRRLPLPESTTA----------YAAAK 156

                         170       180
                  ....*....|....*....|....*.
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06523  157 AALSTYSKSLSKEVAPKGVRVNTVSP 182
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 2-196 1.90e-18

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: 81.05  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFS---CDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:cd08936    10 NKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTgtvCHVGKAEDRERLVATAVNLHGGVD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINR-DGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:cd08936    90 ILVSNAAVNPfFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVS----------SVAAFHPFPGLGP 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRTVS 196
Cdd:cd08936   160 YNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFS 198
PRK05855 PRK05855
SDR family oxidoreductase;
2-191 2.03e-18

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 83.11  E-value: 2.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK05855  315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAeliRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPD 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK05855  395 IVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVA----------SAAAYAPSRSLPA 464

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK05855  465 YATSKAAVLMLSECLRAELAAAGIGVTAICPGFV 498
PRK07775 PRK07775
SDR family oxidoreductase;
7-188 3.14e-18

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 80.57  E-value: 3.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK07775   15 VAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIradGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLVSG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKG 163
Cdd:PRK07775   95 AGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVG----------SDVALRQRPHMGAYGAAKA 164

                         170       180
                  ....*....|....*....|....*
gi 2462599477 164 GLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07775  165 GLEAMVTNLQMELEGTGVRASIVHP 189
PRK06139 PRK06139
SDR family oxidoreductase;
2-177 4.46e-18

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 80.92  E-value: 4.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06139    7 GAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEecrALGAEVLVVPTDVTDADQVKALATQAASFGGRID 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNvghrreMLlhkrSIVGLKGNSGQSVY 158
Cdd:PRK06139   87 VWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFIN------MI----SLGGFAAQPYAAAY 156

                         170
                  ....*....|....*....
gi 2462599477 159 SASKGGLVGFSRALAKEVA 177
Cdd:PRK06139  157 SASKFGLRGFSEALRGELA 175
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 2-188 6.71e-18

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: 79.45  E-value: 6.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd08942     6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSayGECIAIPADLSSEEGIEALVARVAERSDRLDV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLL--VRTKTEDMVSQLHTNllgSMLTCKAAMRTMIQQQG-----GSIVNVGhrremllhkrSIVGLKGN 152
Cdd:cd08942    86 LVNNAGATWGAPLeaFPESGWDKVMDINVK---SVFFLTQALLPLLRAAAtaenpARVINIG----------SIAGIVVS 152

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462599477 153 SGQSV-YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd08942   153 GLENYsYGASKAAVHQLTRKLAKELAGEHITVNAIAP 189
PRK06128 PRK06128
SDR family oxidoreductase;
9-188 8.20e-18

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 79.90  E-value: 8.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA-----GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK06128   62 GADSGIGRATAIAFAREGADIALNYLPEEEQDAAEvvqliQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGLDILVNI 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  84 AG---INRDglLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK06128  142 AGkqtAVKD--IADITTEQFDATFKTNVYAMFWLCKAAIPHL--PPGASIINTG----------SIQSYQPSPTLLDYAS 207

                         170       180
                  ....*....|....*....|....*...
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06128  208 TKAAIVAFTKALAKQVAEKGIRVNAVAP 235
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-213 8.31e-18

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: 78.86  E-value: 8.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD----LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd05357     5 VTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDelnaLRNSAVLVQADLSDFAACADLVAAAFRAFGRCDVLVN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:cd05357    85 NASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINII----------DAMTDRPLTGYFAYCMSK 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462599477 163 GGLVGFSRALAKEVArKKIRVNVVAPELIPRTVsirKMEKGDRINVTLRSP 213
Cdd:cd05357   155 AALEGLTRSAALELA-PNIRVNGIAPGLILLPE---DMDAEYRENALRKVP 201
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 3-191 1.21e-17

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: 78.39  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLaVIARNLEGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd09761     2 KVAIVTGGGHGIGKQICLDFLEAGDKV-VFADIDEERGADFAEAEGPNLFFvHGDVADETLVKFVVYAMLEKLGRIDVLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqQQGGSIVNVGHRRemllhkrsivGLKGNSGQSVYSAS 161
Cdd:cd09761    81 NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELI-KNKGRIINIASTR----------AFQSEPDSEAYAAS 149

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 162 KGGLVGFSRALAKEVARkKIRVNVVAPELI 191
Cdd:cd09761   150 KGGLVALTHALAMSLGP-DIRVNCISPGWI 178
PRK07577 PRK07577
SDR family oxidoreductase;
2-188 1.25e-17

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 78.23  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaAAGDLGGDHLAfsCDVAKEHDVQNTFEELEKHlGRVNFLV 81
Cdd:PRK07577    3 SRTVLVTGATKGIGLALSLRLANLGHQVIGIARS------AIDDFPGELFA--CDLADIEQTAATLAQINEI-HPVDAIV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhKRSIVGLKgnsGQSVYSAS 161
Cdd:PRK07577   74 NNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNIC--------SRAIFGAL---DRTSYSAA 142

                         170       180
                  ....*....|....*....|....*..
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07577  143 KSALVGCTRTWALELAEYGITVNAVAP 169
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-188 1.32e-17

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 79.44  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV--IARNLEGAKAAA--GDLGGDHLAFSCDVAkEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07792   13 KVAVVTGAAAGLGRAEALGLARLGATVVVndVASALDASDVLDeiRAAGAKAVAVAGDIS-QRATADELVATAVGLGGLD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAM---RTMIQQQGGSIVNvghrreMLLHKRSIVGLKGNSGQ 155
Cdd:PRK07792   92 IVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAaywRAKAKAAGGPVYG------RIVNTSSEAGLVGPVGQ 165

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07792  166 ANYGAAKAGITALTLSAARALGRYGVRANAICP 198
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 2-185 1.43e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 79.24  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAF--SCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK05872    9 GKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDRVLtvVADVTDLAAMQAAAEEAVERFGGIDV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqqqggsivnvgHRREMLLHKRSIVGLKGNSGQSVYS 159
Cdd:PRK05872   89 VVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALI-----------ERRGYVLQVSSLAAFAAAPGMAAYC 157

                         170       180
                  ....*....|....*....|....*.
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNV 185
Cdd:PRK05872  158 ASKAGVEAFANALRLEVAHHGVTVGS 183
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 2-188 1.93e-17

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: 78.16  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:cd05348     4 GEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGKLDCFI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQL-----HTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrSIVGLKGNSGQS 156
Cdd:cd05348    84 GNAGIWDYSTSLVDIPEEKLDEAfdelfHINVKGYILGAKAALPALYATEGSVIFTV-----------SNAGFYPGGGGP 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 157 VYSASKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:cd05348   153 LYTASKHAVVGLVKQLAYELA-PHIRVNGVAP 183
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 2-200 2.05e-17

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: 78.42  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL----GGDHLAFS-CDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd05327     1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIkketGNAKVEVIqLDLSSLASVRQFAEEFLARFPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGInrdGLLVRTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVG---HRR-----EMLLHKRSiv 147
Cdd:cd05327    81 LDILINNAGI---MAPPRRLTKDgFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSsiaHRAgpidfNDLDLENN-- 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462599477 148 glKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVSIRKM 200
Cdd:cd05327   156 --KEYSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVV-RTELLRRN 205
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 7-188 6.02e-17

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: 76.02  E-value: 6.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGdhLAFSCDVAKEHDVQNTFEElekhLGRVNFLVNAAGI 86
Cdd:cd11730     3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGA--LARPADVAAELEVWALAQE----LGPLDLLVYAAGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIqqQGGSIVNVGHRREMllhkrsiVGLKGNSGqsvYSASKGGLV 166
Cdd:cd11730    77 ILGKPLARTKPAAWRRILDANLTGAALVLKHALALLA--AGARLVFLGAYPEL-------VMLPGLSA---YAAAKAALE 144

                         170       180
                  ....*....|....*....|..
gi 2462599477 167 GFSRALAKEVarKKIRVNVVAP 188
Cdd:cd11730   145 AYVEVARKEV--RGLRLTLVRP 164
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 4-188 1.33e-16

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 75.68  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGD---LGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAiqqAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 V-NAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:cd05365    81 VnNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNIS----------SMSSENKNVRIAAYG 150

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05365   151 SSKAAVNHMTRNLAFDLGPKGIRVNAVAP 179
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 2-191 1.36e-16

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 76.04  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK06113   11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVdeiQQLGGQAFACRCDITSEQELSALADFALSKLGKVD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINrdgllvRTKTEDM-----VSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNS 153
Cdd:PRK06113   91 ILVNNAGGG------GPKPFDMpmadfRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTIT----------SMAAENKNI 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462599477 154 GQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK06113  155 NMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAI 192
PRK08264 PRK08264
SDR family oxidoreductase;
2-183 6.73e-16

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 73.77  E-value: 6.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRA-VAQLMARKGYRLAVIARNLEGAKaaagDLGGDHLAFSCDVAKEHDVQntfeELEKHLGRVNFL 80
Cdd:PRK08264    6 GKVVLVTGANRGIGRAfVEQLLARGAAKVYAAARDPESVT----DLGPRVVPLQLDVTDPASVA----AAAEAASDVTIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYS 159
Cdd:PRK08264   78 VNNAGIFRTGSLLLEGDEDaLRAEMETNYFGPLAMARAFAPVLAANGGGAIVNV----------LSVLSWVNFPNLGTYS 147

                         170       180
                  ....*....|....*....|....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRV 183
Cdd:PRK08264  148 ASKAAAWSLTQALRAELAPQGTRV 171
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 4-191 1.16e-15

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: 73.27  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIAR----NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:cd05337     3 VAIVTGASRGIGRAIATELAARGFDIAINDLpdddQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGIN---RDGLLvrTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQGgsivnvghrREMLLHkRSIVGLKGNSGQ 155
Cdd:cd05337    83 LVNNAGIAvrpRGDLL--DLTEDSFDRLiAINLRGPFFLTQAVARRMVEQPD---------RFDGPH-RSIIFVTSINAY 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462599477 156 SV------YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05337   151 LVspnrgeYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLI 192
PRK09186 PRK09186
flagellin modification protein A; Provisional
 2-188 2.72e-15

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 72.33  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGD-----HLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK09186    4 GKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEfkskkLSLVELDITDQESLEEFLSKSAEKYGK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAginrdglLVRTKT----------EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSI 146
Cdd:PRK09186   84 IDGAVNCA-------YPRNKDygkkffdvslDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNIS----------SI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462599477 147 VGL--------KGNSGQSV--YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK09186  147 YGVvapkfeiyEGTSMTSPveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSP 198
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 2-188 2.89e-15

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 72.30  E-value: 2.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK06200    6 GQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCFV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGL-LVRTKTEDMVSQL----HTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrSIVGLKGNSGQS 156
Cdd:PRK06200   86 GNAGIWDYNTsLVDIPAETLDTAFdeifNVNVKGYLLGAKAALPALKASGGSMIFTL-----------SNSSFYPGGGGP 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 157 VYSASKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:PRK06200  155 LYTASKHAVVGLVRQLAYELA-PKIRVNGVAP 185
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 2-202 4.31e-15

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: 71.73  E-value: 4.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEgakaaagDLggDHLAFSC--------DVAkehDVQNTFEELEKH 73
Cdd:cd05351     7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQA-------DL--DSLVRECpgiepvcvDLS---DWDATEEALGSV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  74 lGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQ-GGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:cd05351    75 -GPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVS----------SQASQRAL 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462599477 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPeliprTVSIRKMEK 202
Cdd:cd05351   144 TNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNP-----TVVMTDMGR 188
PRK06500 PRK06500
SDR family oxidoreductase;
1-188 7.27e-15

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 71.14  E-value: 7.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK06500    5 QGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGRLDAV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTkTEDMVSQL-HTNLLGSMLTCKAAMRtmIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK06500   85 FINAGVAKFAPLEDW-DEAMFDRSfNTNVKGPYFLIQALLP--LLANPASIVLNG----------SINAHIGMPNSSVYA 151

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06500  152 ASKAALLSLAKTLSGELLPRGIRVNAVSP 180
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 7-188 3.28e-14

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 68.38  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNlegakaaagdlGGDHLafsCDVAKEHDVQNTFEElekhLGRVNFLVNAAGI 86
Cdd:cd11731     3 VIGATGTIGLAVAQLLSAHGHEVITAGRS-----------SGDYQ---VDITDEASIKALFEK----VGHFDAIVSTAGD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGGLV 166
Cdd:cd11731    65 AEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSITLTS----------GILAQRPIPGGAAAATVNGALE 132

                         170       180
                  ....*....|....*....|..
gi 2462599477 167 GFSRALAKEVARkKIRVNVVAP 188
Cdd:cd11731   133 GFVRAAAIELPR-GIRINAVSP 153
PRK06182 PRK06182
short chain dehydrogenase; Validated
 3-191 6.62e-14

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 68.83  E-value: 6.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAgDLGGDHLAFscDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLA-SLGVHPLSL--DVTDEASIKAAVDTIIAEEGRIDVLVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASK 162
Cdd:PRK06182   81 NAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINIS----------SMGGKIYTPLGAWYHATK 150

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK06182  151 FALEGFSDALRLEVAPFGIDVVVIEPGGI 179
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 7-188 7.21e-14

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: 68.10  E-value: 7.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:cd05370    10 ITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNIH-TIVLDVGDAESVEALAEALLSEYPNLDILINNAGI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 --NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGG 164
Cdd:cd05370    89 qrPIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVS----------SGLAFVPMAANPVYCATKAA 158

                         170       180
                  ....*....|....*....|....
gi 2462599477 165 LVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05370   159 LHSYTLALRHQLKDTGVEVVEIVP 182
PRK06482 PRK06482
SDR family oxidoreductase;
1-188 7.25e-14

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 68.60  E-value: 7.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLegakAAAGDLG---GDHL-AFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK06482    1 MSKTWFITGASSGFGRGMTERLLARGDRVAATVRRP----DALDDLKaryGDRLwVLQLDVTDSAAVRAVVDRAFAALGR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK06482   77 IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVS----------SEGGQIAYPGFS 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06482  147 LYHATKWGIEGFVEAVAQEVAPFGIEFTIVEP 178
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 7-206 7.80e-14

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 68.44  E-value: 7.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK05876   11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLraeGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFSN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGsivnvGHrremLLHKRSIVGLKGNSGQSVYSASKG 163
Cdd:PRK05876   91 AGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTG-----GH----VVFTASFAGLVPNAGLGAYGVAKY 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462599477 164 GLVGFSRALAKEVARKKIRVNVvapeLIPRTVSIRKMEKGDRI 206
Cdd:PRK05876  162 GVVGLAETLAREVTADGIGVSV----LCPMVVETNLVANSERI 200
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 4-188 1.02e-13

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 67.70  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   4 VCAVFGGSRGIGRAVAQLMARKGY--RLAVIARNLEGAKAAAGDL-GGDHLAF-SCDVAKEHDVQNTFEEL-EKHLGRVN 78
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEELrPGLRVTTvKADLSDAAGVEQLLEAIrKLDGERDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:cd05367    81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVS----------SGAAVNPFKGWGL 150

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEvaRKKIRVNVVAP 188
Cdd:cd05367   151 YCSSKAARDMFFRVLAAE--EPDVRVLSYAP 179
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 3-194 1.66e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 67.40  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK07677    2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTkekLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINrdgLLVRtkTEDMV-----SQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVghrremllhkrsIVGLKGNS 153
Cdd:PRK07677   82 LINNAAGN---FICP--AEDLSvngwnSVIDIVLNGTFYCSQAVGKYWIEKgIKGNIINM------------VATYAWDA 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462599477 154 GQSV-YSAS-KGGLVGFSRALAKEVARK-KIRVNVVAPELIPRT 194
Cdd:PRK07677  145 GPGViHSAAaKAGVLAMTRTLAVEWGRKyGIRVNAIAPGPIERT 188
PRK08251 PRK08251
SDR family oxidoreductase;
9-191 1.84e-13

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 67.27  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA 83
Cdd:PRK08251    9 GASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYpgikvAVAALDVNDHDQVFEVFAEFRDELGGLDRVIVN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  84 AGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG-QSVYSASK 162
Cdd:PRK08251   89 AGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLIS----------SVSAVRGLPGvKAAYAASK 158

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK08251  159 AGVASLGEGLRAELAKTPIKVSTIEPGYI 187
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 7-188 2.03e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 67.10  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH-----LAFscDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:PRK07523   15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGlsahaLAF--DVTDHDAVRAAIDAFEAEIGPIDILV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRdgllvRTKTEDMVSQ-----LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLlhkrsivglkGNSGQS 156
Cdd:PRK07523   93 NNAGMQF-----RTPLEDFPADaferlLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSAL----------ARPGIA 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07523  158 PYTATKGAVGNLTKGMATDWAKHGLQCNAIAP 189
PRK06949 PRK06949
SDR family oxidoreductase;
3-191 2.11e-13

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 67.09  E-value: 2.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06949   10 KVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIeaeGGAAHVVSLDVTDYQSIKAAVAHAETEAGTIDI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGS--------IVNVGhrremllhkrSIVGLKG 151
Cdd:PRK06949   90 LVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAKGAgntkpggrIINIA----------SVAGLRV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462599477 152 NSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK06949  160 LPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYI 199
PRK05866 PRK05866
SDR family oxidoreductase;
9-186 2.53e-13

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 67.46  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK05866   47 GASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRItraGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILINNAG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  86 INrdgllVRTKTEDMVSQLH-------TNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREmllhkrsivgLKGNSGQ-SV 157
Cdd:PRK05866  127 RS-----IRRPLAESLDRWHdvertmvLNYYAPLRLIRGLAPGMLERGDGHIINVATWGV----------LSEASPLfSV 191

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVV 186
Cdd:PRK05866  192 YNASKAALSAVSRVIETEWGDRGVHSTTL 220
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 2-188 2.66e-13

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: 66.66  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQ-LMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKehdvQNTFEELEKHLGRVNFL 80
Cdd:cd05354     3 DKTVLVTGANRGIGKAFVEsLLAHGAKKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTD----PESIKAAAAQAKDVDVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINR-DGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkRSIVGLKGNSGQSVYS 159
Cdd:cd05354    79 INNAGVLKpATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNL----------NSVASLKNFPAMGTYS 148

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05354   149 ASKSAAYSLTQGLRAELAAQGTLVLSVHP 177
PRK05693 PRK05693
SDR family oxidoreductase;
3-191 3.91e-13

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 66.74  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLE--GAKAAAGdlggdHLAFSCDVAKEHDVQNTFEELEKHLGRVNFL 80
Cdd:PRK05693    2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEdvEALAAAG-----FTAVQLDVNDGAALARLAEELEAEHGGLDVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLgSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSA 160
Cdd:PRK05693   77 INNAGYGAMGPLLDGGVEAMRRQFETNVF-AVVGVTRALFPLLRRSRGLVVNIG----------SVSGVLVTPFAGAYCA 145

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK05693  146 SKAAVHALSDALRLELAPFGVQVMEVQPGAI 176
PRK07814 PRK07814
SDR family oxidoreductase;
2-188 4.58e-13

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 66.34  E-value: 4.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG---DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK07814   10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEqirAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQG-GSIVNVghrremllhkRSIVGLKGNSGQSV 157
Cdd:PRK07814   90 IVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGgGSVINI----------SSTMGRLAGRGFAA 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:PRK07814  160 YGTAKAALAHYTRLAALDLC-PRIRVNAIAP 189
PRK09135 PRK09135
pteridine reductase; Provisional
 1-188 6.08e-13

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 65.72  E-value: 6.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN-LEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:PRK09135    5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELnalrPGSAAALQADLLDPDALPELVAACVAAFG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGinrdgLLVRTKTEDMVSQLHTNLLGSMLtcKA------AMRTMIQQQGGSIVNvghrremllhkrsIVGL 149
Cdd:PRK09135   85 RLDALVNNAS-----SFYPTPLGSITEAQWDDLFASNL--KApfflsqAAAPQLRKQRGAIVN-------------ITDI 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462599477 150 KGN---SGQSVYSASKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:PRK09135  145 HAErplKGYPVYCAAKAALEMLTRSLALELA-PEVRVNAVAP 185
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
7-214 6.95e-13

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 65.48  E-value: 6.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIAR--NLEGAKAAaGDLGGDHLAFSCDVAKEHDVQNTFEE----LEKHLGRVNFL 80
Cdd:PRK06924    6 ITGTSQGLGEAIANQLLEKGTHVISISRteNKELTKLA-EQYNSNLTFHSLDLQDVHELETNFNEilssIQEDNVSSIHL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAG----INRDGllvRTKTEDMVSQLHTNLLGSMLTCKAAM-RTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK06924   85 INNAGmvapIKPIE---KAESEELITNVHLNLLAPMILTSTFMkHTKDWKVDKRVINIS----------SGAAKNPYFGW 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVApeLIPRTV------SIRKMEKGDRINV----------TLRSPE 214
Cdd:PRK06924  152 SAYCSSKAGLDMFTQTVATEQEEEEYPVKIVA--FSPGVMdtnmqaQIRSSSKEDFTNLdrfitlkeegKLLSPE 224
PRK08219 PRK08219
SDR family oxidoreductase;
1-188 1.00e-12

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 64.57  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARkGYRLAVIARNLEGAKAAAGDLGGDHlAFSCDVAKEHDVQNTFEelekHLGRVNFL 80
Cdd:PRK08219    2 ERPTALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELAAELPGAT-PFPVDLTDPEAIAAAVE----QLGRLDVL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGSM-LTckAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK08219   76 VHNAGVADLGPVAESTVDEWRATLEVNVVAPAeLT--RLLLPALRAAHGHVVFIN----------SGAGLRANPGWGSYA 143

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEvARKKIRVNVVAP 188
Cdd:PRK08219  144 ASKFALRALADALREE-EPGNVRVTSVHP 171
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 7-188 1.19e-12

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: 64.62  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRA-VAQLMARKGYRLAVIARNLEGAKAAAGdLGGDHLAFSC---DVAKEhdVQNTFEELEKHLG--RVNFL 80
Cdd:cd05325     3 ITGASRGIGLElVRQLLARGNNTVIATCRDPSAATELAA-LGASHSRLHIlelDVTDE--IAESAEAVAERLGdaGLDVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKT-EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREmllhkrSIvGLKGNSGQSVYS 159
Cdd:cd05325    80 INNAGILHSYGPASEVDsEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVG------SI-GDNTSGGWYSYR 152

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05325   153 ASKAALNMLTKSLAVELKRDGITVVSLHP 181
PRK06194 PRK06194
hypothetical protein; Provisional
 3-192 1.72e-12

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 65.04  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLA---VIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK06194    7 KVAVITGAASGFGLAFARIGAALGMKLVladVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremLLHKRSIVGLKGNSGQSVYS 159
Cdd:PRK06194   87 LFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEKDPAYEGH----IVNTASMAGLLAPPAMGIYN 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462599477 160 ASKGGLVGFSRALAK--EVARKKIRVNVVAPELIP 192
Cdd:PRK06194  163 VSKHAVVSLTETLYQdlSLVTDQVGASVLCPYFVP 197
PRK05717 PRK05717
SDR family oxidoreductase;
3-201 1.80e-12

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 64.53  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK05717   11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALVC 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGIN--RDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMrTMIQQQGGSIVNVGHRREMllhkrsivglKGNSGQSVYSA 160
Cdd:PRK05717   91 NAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCA-PYLRAHNGAIVNLASTRAR----------QSEPDTEAYAA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462599477 161 SKGGLVGFSRALAKEVArKKIRVNVVAPELI-PRTVSIRKME 201
Cdd:PRK05717  160 SKGGLLALTHALAISLG-PEIRVNAVSPGWIdARDPSQRRAE 200
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-188 3.20e-12

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 63.77  E-value: 3.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGyrLAVIARNLEGA---KAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK12481    9 KVAIITGCNTGLGQGMAIGLAKAG--ADIVGVGVAEApetQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINR--DGLLVRTKTEDMVSQLHTNLLgSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK12481   87 LINNAGIIRrqDLLEFGNKDWDDVININQKTV-FFLSQAVAKQFVKQGNGGKIINIA----------SMLSFQGGIRVPS 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12481  156 YTASKSAVMGLTRALATELSQYNINVNAIAP 186
PRK07024 PRK07024
SDR family oxidoreductase;
7-188 4.11e-12

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 63.41  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VF--GGSRGIGRAVAQLMARKGYRLAVIARNLEG--AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK07024    5 VFitGASSGIGQALAREYARQGATLGLVARRTDAlqAFAARLPKAARVSVYAADVRDADALAAAAADFIAAHGLPDVVIA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRdGLLVRTkTED---MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK07024   85 NAGISV-GTLTEE-REDlavFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIA----------SVAGVRGLPGAGAYS 152

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07024  153 ASKAAAIKYLESLRVELRPAGVRVVTIAP 181
PRK07041 PRK07041
SDR family oxidoreductase;
7-191 4.81e-12

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 62.75  E-value: 4.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH--LAFSCDVAKEHDVQNTFEElekhLGRVNFLVNAA 84
Cdd:PRK07041    2 VVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGApvRTAALDITDEAAVDAFFAE----AGPFDHVVITA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  85 GINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAmrtmIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGG 164
Cdd:PRK07041   78 ADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAA----RIAPGGSLTFVS----------GFAAVRPSASGVLQGAINAA 143

                         170       180
                  ....*....|....*....|....*..
gi 2462599477 165 LVGFSRALAKEVArkKIRVNVVAPELI 191
Cdd:PRK07041  144 LEALARGLALELA--PVRVNTVSPGLV 168
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 3-191 5.48e-12

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: 63.25  E-value: 5.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHL-----AFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd09807     2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLnheviVRHLDLASLKSIRAFAAEFLAEEDRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRdglLVRTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremLLHKRSIVGLKG-NSGQ 155
Cdd:cd09807    82 DVLINNAGVMR---CPYSKTEDgFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSS----LAHKAGKINFDDlNSEK 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462599477 156 S-----VYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd09807   155 SyntgfAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVV 195
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 3-214 5.73e-12

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: 63.23  E-value: 5.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHL-GRV 77
Cdd:cd09763     4 KIALVTGASRGIGRGIALQLGEAGATVYITGRTilpqLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQqGRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAA-GINRDGLLVRTKT---------EDMVSqlhTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrSIV 147
Cdd:cd09763    84 DILVNNAyAAVQLILVGVAKPfweepptiwDDINN---VGLRAHYACSVYAAPLMVKAGKGLIVII-----------SST 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599477 148 GLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVSIRKMEKGDRINVTLRSPE 214
Cdd:cd09763   150 GGLEYLFNVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFV-RTELVLEMPEDDEGSWHAKERD 215
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 7-174 2.05e-11

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 62.38  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARK-GYRLAVIAR--------NLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd08953   210 VTGGAGGIGRALARALARRyGARLVLLGRsplppeeeWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYGAI 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSmltckAAMRTMIQQQggsivnvghRREMLLHKRSIVGLKGNSGQSV 157
Cdd:cd08953   290 DGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGL-----LNLAQALADE---------PLDFFVLFSSVSAFFGGAGQAD 355

                         170
                  ....*....|....*..
gi 2462599477 158 YSASKGGLVGFSRALAK 174
Cdd:cd08953   356 YAAANAFLDAFAAYLRQ 372
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-160 3.20e-11

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: 59.80  E-value: 3.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477    9 GGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAA------GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:smart00822   7 GGLGGLGRALARWLAERGARrLVLLSRSGPDAPGAAallaelEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSmltckaamrtmiqqqggsiVNVgHRremLLHKR---------SIVGLKGN 152
Cdd:smart00822  87 HAAGVLDDGVLASLTPERFAAVLAPKAAGA-------------------WNL-HE---LTADLpldffvlfsSIAGVLGS 143


                   ....*...
gi 2462599477  153 SGQSVYSA 160
Cdd:smart00822 144 PGQANYAA 151
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 9-188 3.21e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 60.83  E-value: 3.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH----LAFSCDVAKEHDVqntfEELEKHLGRVNFLVNAA 84
Cdd:PRK06125   14 GASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHgvdvAVHALDLSSPEAR----EQLAAEAGDIDILVNNA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  85 GINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrsiVGLKGNSGQSVY---SAS 161
Cdd:PRK06125   90 GAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV-------------IGAAGENPDADYicgSAG 156

                         170       180
                  ....*....|....*....|....*..
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK06125  157 NAALMAFTRALGGKSLDDGVRVVGVNP 183
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 3-188 3.77e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 60.74  E-value: 3.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV-- 77
Cdd:PRK07576   10 KNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVaqlQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPIdv 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 -------NFLVNAAGINRDGLlvRTKTEdmvsqlhTNLLGSMLTCKAAMRTMiQQQGGSIVNVGhrremllHKRSIVGLK 150
Cdd:PRK07576   90 lvsgaagNFPAPAAGMSANGF--KTVVD-------IDLLGTFNVLKAAYPLL-RRPGASIIQIS-------APQAFVPMP 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462599477 151 gnsGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07576  153 ---MQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSIVP 187
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-188 4.04e-11

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 60.66  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVI-----ARNLEGAKAaagdLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08993   11 KVAVVTGCDTGLGQGMALGLAEAGCDIVGInivepTETIEQVTA----LGRRFLSLTADLRKIDGIPALLERAVAEFGHI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQ-QGGSIVNVGhrremllhkrSIVGLKGNSGQS 156
Cdd:PRK08993   87 DILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIA----------SMLSFQGGIRVP 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08993  157 SYTASKSGVMGVTRLMANEWAKHNINVNAIAP 188
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 2-188 4.39e-11

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 60.28  E-value: 4.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAK------AAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLG 75
Cdd:cd05340     4 DRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRqvadhiNEEGGRQPQWFILDLLTCTSENCQQLAQRIAVNYP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVN-FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSG 154
Cdd:cd05340    84 RLDgVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTS----------SSVGRQGRAN 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 155 QSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd05340   154 WGAYAVSKFATEGL*QVLADEYQQRNLRVNCINP 187
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-160 4.97e-11

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: 59.11  E-value: 4.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYR-LAVIARNLEGAKAAAG------DLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:pfam08659   7 GGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAQAliaeleARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIRGVI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAGINRDGLLVRTKTEDMVSQLHTNLLGSM----LTCKAAMRTMIqqqggsivnvghrreMLlhkRSIVGLKGNSGQSV 157
Cdd:pfam08659  87 HAAGVLRDALLENMTDEDWRRVLAPKVTGTWnlheATPDEPLDFFV---------------LF---SSIAGLLGSPGQAN 148


                  ...
gi 2462599477 158 YSA 160
Cdd:pfam08659 149 YAA 151
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 3-188 5.57e-11

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: 60.17  E-value: 5.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMAR---KGYRLAVIARNL---EGAKAAAGDLGGDHLAF-SCDVAKEHDVQNTFEELEKhlG 75
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLASdpsKRFKVYATMRDLkkkGRLWEAAGALAGGTLETlQLDVCDSKSVAAAVERVTE--R 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGInrdGLL--VRTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGN 152
Cdd:cd09806    79 HVDVLVCNAGV---GLLgpLEALSEDaMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTS----------SVGGLQGL 145

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd09806   146 PFNDVYCASKFALEGLCESLAVQLLPFNVHLSLIEC 181
PRK08278 PRK08278
SDR family oxidoreductase;
9-214 6.25e-11

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 60.30  E-value: 6.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIAR------NLEG----AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVN 78
Cdd:PRK08278   13 GASRGIGLAIALRAARDGANIVIAAKtaephpKLPGtihtAAEEIEAAGGQALPLVGDVRDEDQVAAAVAKAVERFGGID 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAG-INRDGLL-VRTKTEDMVSQLhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMllhKRSIVGlkgnsGQS 156
Cdd:PRK08278   93 ICVNNASaINLTGTEdTPMKRFDLMQQI--NVRGTFLVSQACLPHLKKSENPHILTLSPPLNL---DPKWFA-----PHT 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599477 157 VYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKGDRINVTLRSPE 214
Cdd:PRK08278  163 AYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPRTTIATAAVRNLLGGDEAMRRSRTPE 220
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 76-188 9.38e-11

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: 58.68  E-value: 9.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:cd02266    31 RRDVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILIS----------SVAGLFGAPGL 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd02266   101 GGYAASKAALDGLAQQWASEGWGNGLPATAVAC 133
PRK09291 PRK09291
SDR family oxidoreductase;
1-188 1.47e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 59.24  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRL---AVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEElekhlgRV 77
Cdd:PRK09291    1 MSKTILITGAGSGFGREVALRLARKGHNViagVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDRAQAAEW------DV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:PRK09291   75 DVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTS----------SMAGLITGPFTGA 144

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK09291  145 YCASKHALEAIAEAMHAELKPFGIQVATVNP 175
PRK07985 PRK07985
SDR family oxidoreductase;
2-206 1.52e-10

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 59.24  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVI-----ARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK07985   49 DRKALVTGGDSGIGRAAAIAYAREGADVAISylpveEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALGG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRDGLLVRTKTEDMVSQLH-TNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK07985  129 LDIMALVAGKQVAIPDIADLTSEQFQKTFaINVFALFWLTQEAIPLL--PKGASIITTS----------SIQAYQPSPHL 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIPRTVSIRKMEKGDRI 206
Cdd:PRK07985  197 LDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISGGQTQDKI 247
PRK09134 PRK09134
SDR family oxidoreductase;
7-188 4.77e-10

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 57.63  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAA---GDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK09134   14 VTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAaeiRALGRRAVALQADLADEAEVRALVARASAALGPITLLVN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGI-NRDglLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREmllhkrsivgLKGNSGQSVYSA 160
Cdd:PRK09134   94 NASLfEYD--SAASFTRASWDRhMATNLRAPFVLAQAFARALPADARGLVVNMIDQRV----------WNLNPDFLSYTL 161

                         170       180
                  ....*....|....*....|....*...
gi 2462599477 161 SKGGLVGFSRALAKEVArKKIRVNVVAP 188
Cdd:PRK09134  162 SKAALWTATRTLAQALA-PRIRVNAIGP 188
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 3-191 5.00e-10

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: 57.33  E-value: 5.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNlEGAKAAAGDLGGDHlafSCDVAKEHDVqntFEELEKHLGRVNFLVN 82
Cdd:cd05334     2 RVVLVYGGRGALGSAVVQAFKSRGWWVASIDLA-ENEEADASIIVLDS---DSFTEQAKQV---VASVARLSGKVDALIC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAG-----INRDGLLVRTkTEDMVSQlhtNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGLKGNSGQSV 157
Cdd:cd05334    75 VAGgwaggSAKSKSFVKN-WDLMWKQ---NLWTSFIASHLATKHL--LSGGLLVLTG----------AKAALEPTPGMIG 138

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 158 YSASKGGLVGFSRALAKE--VARKKIRVNVVAPELI 191
Cdd:cd05334   139 YGAAKAAVHQLTQSLAAEnsGLPAGSTANAILPVTL 174
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-191 5.42e-10

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 57.46  E-value: 5.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLAFScDVAKEHDVQNTFEELEKHLGRVNF 79
Cdd:PRK05786    6 KKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNenkLKRMKKTLSKYGNIHYVVG-DVSSTESARNVIEKAAKVLNAIDG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 L-VNAAGINRDGLLVRTKTEDMvsqLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrSIVGL-KGNSGQSV 157
Cdd:PRK05786   85 LvVTVGGYVEDTVEEFSGLEEM---LTNHIKIPLYAVNASLRFL--KEGSSIVLVS----------SMSGIyKASPDQLS 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 158 YSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK05786  150 YAVAKAGLAKAVEILASELLGRGIRVNGIAPTTI 183
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 2-194 6.37e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 57.50  E-value: 6.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGR 76
Cdd:PRK05875    7 DRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIealkgAGAVRYEPADVTDEDQVARAVDAATAWHGR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRD-GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQ 155
Cdd:PRK05875   87 LHGVVHCAGGSETiGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGIS----------SIAASNTHRWF 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIpRT 194
Cdd:PRK05875  157 GAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLI-RT 194
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 5-214 1.53e-09

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: 55.91  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   5 CAVF--GGSRGIGRAVAQLMARKGYRLAVIARNLE----------GAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEK 72
Cdd:cd09762     4 KTLFitGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgtiyTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEKAVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  73 HLGRVNFLV-NAAGIN-RDGLLVRTKTEDMVSQLhtNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMllhkrsivGLK 150
Cdd:cd09762    84 KFGGIDILVnNASAISlTGTLDTPMKRYDLMMGV--NTRGTYLCSKACLPYLKKSKNPHILNLSPPLNL--------NPK 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462599477 151 GNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVvapeLIPRTV---SIRKMEKGDRINVTLRSPE 214
Cdd:cd09762   154 WFKNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNA----LWPRTAiatAAMNMLGGVDVAACCRKPE 216
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 3-213 4.67e-09

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site 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: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 54.90  E-value: 4.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFG--GSRGIGRAVAQLMARKGYRLAVIARN--LEG-AKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:cd05372     2 KRILITGiaNDRSIAWGIAKALHEAGAELAFTYQPeaLRKrVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGI-NRDGLLVRTktedmvsqLHTNLLGSMLT-----------CKAAMRTMiqQQGGSIVNVGHrremllhkrs 145
Cdd:cd05372    82 DGLVHSIAFaPKVQLKGPF--------LDTSRKGFLKAldisayslvslAKAALPIM--NPGGSIVTLSY---------- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462599477 146 IVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVS------IRKMEKGdrinVTLRSP 213
Cdd:cd05372   142 LGSERVVPGYNVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPI-KTLAasgitgFDKMLEY----SEQRAP 210
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-188 5.84e-09

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 54.41  E-value: 5.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSR--GIGRAVAQLMARKGYRL---------------------AVIARNLE--GAKAAAGDLggdhlafscDV 57
Cdd:PRK12859    7 KVAVVTGVSRldGIGAAICKELAEAGADIfftywtaydkempwgvdqdeqIQLQEELLknGVKVSSMEL---------DL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  58 AKEHDVQNTFEELEKHLGRVNFLVNAAGINRDgLLVRTKTEDMVSQLH-TNLLGSMLTCKAAMRTMIQQQGGSIVNVghr 136
Cdd:PRK12859   78 TQNDAPKELLNKVTEQLGYPHILVNNAAYSTN-NDFSNLTAEELDKHYmVNVRATTLLSSQFARGFDKKSGGRIINM--- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462599477 137 remllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12859  154 -------TSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINP 198
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 7-188 6.49e-09

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


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 54.26  E-value: 6.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFG--GSRGIGRAVAQLMARKGYRLAVIARN--LEG-AKAAAGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLV 81
Cdd:COG0623    10 ITGvaNDRSIAWGIAKALHEEGAELAFTYQGeaLKKrVEPLAEELGSA-LVLPCDVTDDEQIDALFDEIKEKWGKLDFLV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  82 NAAG-------------INRDGLLvrtKTEDmVS--QLHtnllgSMltCKAAMRTMiqQQGGSIVNV---GHRREMllhk 143
Cdd:COG0623    89 HSIAfapkeelggrfldTSREGFL---LAMD-ISaySLV-----AL--AKAAEPLM--NEGGSIVTLtylGAERVV---- 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462599477 144 rsivglkgnSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:COG0623   152 ---------PNYNVMGVAKAALEASVRYLAADLGPKGIRVNAISA 187
PRK12744 PRK12744
SDR family oxidoreductase;
2-188 7.79e-09

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 53.98  E-value: 7.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAG-------DLGGDHLAFSCDVAKEHDVQNTFEELEKHL 74
Cdd:PRK12744    8 GKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEetvaavkAAGAKAVAFQADLTTAAAVEKLFDDAKAAF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVghrremllhkrsIVGLKG--N 152
Cdd:PRK12744   88 GRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIVTL------------VTSLLGafT 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12744  154 PFYSAYAGSKAPVEHFTRAASKEFGARGISVTAVGP 189
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 2-188 1.44e-08

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 53.34  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN---LEGAKAAAGDLGGDHLA-FSCDV--AKEHDVQNTFEELEKHLG 75
Cdd:PRK08945   12 DRIILVTGAGDGIGREAALTYARHGATVILLGRTeekLEAVYDEIEAAGGPQPAiIPLDLltATPQNYQQLADTIEEQFG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  76 RVNFLVNAAGInrdgLLVRT----KTEDMVSQ-LHTNLLGS-MLTcKAAMRTMIQQQGGSIVnvghrremllHKRSIVGL 149
Cdd:PRK08945   92 RLDGVLHNAGL----LGELGpmeqQDPEVWQDvMQVNVNATfMLT-QALLPLLLKSPAASLV----------FTSSSVGR 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462599477 150 KGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08945  157 QGRANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINP 195
PRK12746 PRK12746
SDR family oxidoreductase;
3-188 1.69e-08

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 53.11  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFEELEKHL---- 74
Cdd:PRK12746    7 KVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIesnGGKAFLIEADLNSIDGVKKLVEQLKNELqirv 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  75 --GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGHRREMLlhkrsivglkGN 152
Cdd:PRK12746   87 gtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRL----------GF 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462599477 153 SGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12746  155 TGSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMP 190
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 4-191 1.86e-08

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: 52.99  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   4 VCAVFGGSRGIGRAVAQLMAR----KGYRLAVIARNLEGAKAAAGDLGGDHLA-----FSCDVAKEHDVQNTFEELEKhL 74
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERSGlrvvrVSLDLGAEAGLEQLLKALRE-L 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  75 GRVNFLVNAAGINRDGLLVRT-KTEDMVSQL-------HTNLLGSMLTCKAAMRTMIQQQGG--SIVNVGhrremllhkr 144
Cdd:TIGR01500  81 PRPKGLQRLLLINNAGTLGDVsKGFVDLSDStqvqnywALNLTSMLCLTSSVLKAFKDSPGLnrTVVNIS---------- 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462599477 145 SIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:TIGR01500 151 SLCAIQPFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVL 197
PRK08017 PRK08017
SDR family oxidoreductase;
1-188 5.06e-08

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 51.63  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAkAAAGDLGGDHLAFSCDVAKEHDvQNTFEELEKHLGRVNFL 80
Cdd:PRK08017    1 MQKSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDV-ARMNSLGFTGILLDLDDPESVE-RAADEVIALTDNRLYGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQLHTNLLGS-MLTCkAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK08017   79 FNNAGFGVYGPLSTISRQQMEQQFSTNFFGThQLTM-LLLPAMLPHGEGRIVMTS----------SVMGLISTPGRGAYA 147

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK08017  148 ASKYALEAWSDALRMELRHSGIKVSLIEP 176
PRK08703 PRK08703
SDR family oxidoreductase;
2-188 5.25e-08

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 51.47  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKA------AAGdlGGDHLAFSCDVAKEHDvqNTFEEL----- 70
Cdd:PRK08703    6 DKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKvydaivEAG--HPEPFAIRFDLMSAEE--KEFEQFaatia 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  71 EKHLGRVNFLVNAAGINRDGLLVRTKT-EDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRRemllhkrsivGL 149
Cdd:PRK08703   82 EATQGKLDGIVHCAGYFYALSPLDFQTvAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESH----------GE 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462599477 150 KGNSGQSVYSASKGGLVGFSRALAKEVAR-KKIRVNVVAP 188
Cdd:PRK08703  152 TPKAYWGGFGASKAALNYLCKVAADEWERfGNLRANVLVP 191
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-188 5.94e-08

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 51.61  E-value: 5.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSR--GIGRAVAQLMARKGYR------------LAVIARNLEGA--KAAAGDLGGDHLAFSCDVAKEHDVQ 64
Cdd:PRK12748    4 MKKIALVTGASRlnGIGAAVCRRLAAKGIDifftywspydktMPWGMHDKEPVllKEEIESYGVRCEHMEIDLSQPYAPN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  65 NTFEELEKHLGRVNFLVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkr 144
Cdd:PRK12748   84 RVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINL----------- 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462599477 145 sivglkgNSGQSV--------YSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12748  153 -------TSGQSLgpmpdelaYAATKGAIEAFTKSLAPELAEKGITVNAVNP 197
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 5-188 1.18e-07

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: 50.74  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   5 CAVF--GGSRGIGRAVAQLMARKGYRL--AVIARNLEGAK----AAAGDLGGDHLafscDVAKEHDVQNTFEELEKHLGR 76
Cdd:cd09805     1 KAVLitGCDSGFGNLLAKKLDSLGFTVlaGCLTKNGPGAKelrrVCSDRLRTLQL----DVTKPEQIKRAAQWVKEHVGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNF--LVNAAGIN---RDGLLvrTKTEDMVSQLHTNLLGSMLTCKAaMRTMIQQQGGSIVNVGhrremllhkrSIVGLKG 151
Cdd:cd09805    77 KGLwgLVNNAGILgfgGDEEL--LPMDDYRKCMEVNLFGTVEVTKA-FLPLLRRAKGRVVNVS----------SMGGRVP 143

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462599477 152 NSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:cd09805   144 FPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEP 180
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 4-190 1.29e-07

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 50.70  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   4 VCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAK---AAAGDLGGDHLAFSC--DVAKEHDVQNTFEEL----EKHL 74
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAAstlAAELNARRPNSAVTCqaDLSNSATLFSRCEAIidacFRAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  75 GRVNFLVNAAGINRDGLLVRTKTEDMVSQLHT------NLLGSMLTCKAAM-RTMIQQQGGSivnvghRREMLLHKRSIV 147
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPLLRGDAGEGVGDKKSlevqvaELFGSNAIAPYFLiKAFAQRQAGT------RAEQRSTNLSIV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462599477 148 GL------KGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPEL 190
Cdd:TIGR02685 157 NLcdamtdQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL 205
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 9-172 1.68e-07

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: 50.85  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYR-LAVIARN-----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKhLGRVNFLVN 82
Cdd:cd05274   157 GGLGGLGLLVARWLAARGARhLVLLSRRgpaprAAARAALLRAGGARVSVVRCDVTDPAALAALLAELAA-GGPLAGVIH 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCkAAMRtmiqqqggsivnvGHRREMLLHKRSIVGLKGNSGQSVYSASK 162
Cdd:cd05274   236 AAGVLRDALLAELTPAAFAAVLAAKVAGALNLH-ELTP-------------DLPLDFFVLFSSVAALLGGAGQAAYAAAN 301

                         170
                  ....*....|
gi 2462599477 163 GGLVGFSRAL 172
Cdd:cd05274   302 AFLDALAAQR 311
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 7-194 2.07e-07

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 50.14  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGI 86
Cdd:PRK10538    5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAGL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 NRdGL--LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYSASKGG 164
Cdd:PRK10538   85 AL-GLepAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIG----------STAGSWPYAGGNVYGATKAF 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 2462599477 165 LVGFSRALAKEVARKKIRVNVVAPELIPRT 194
Cdd:PRK10538  154 VRQFSLNLRTDLHGTAVRVTDIEPGLVGGT 183
PRK07806 PRK07806
SDR family oxidoreductase;
2-85 1.83e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 47.02  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARN----LEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK07806    6 GKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkaprANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGL 85


                  ....*....
gi 2462599477  78 NFLV-NAAG 85
Cdd:PRK07806   86 DALVlNASG 94
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 3-191 2.57e-06

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 46.99  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAV-IARNLEGAKAAAGDL---GGDHLAFSCDVAKEHDVQNTFE----ELEKHL 74
Cdd:PRK12747    5 KVALVTGASRGIGRAIAKRLANDGALVAIhYGNRKEEAEETVYEIqsnGGSAFSIGANLESLHGVEALYSsldnELQNRT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  75 GRVNF--LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGHRREMLLHKRSIvglkgn 152
Cdd:PRK12747   85 GSTKFdiLINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFI------ 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462599477 153 sgqsVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK12747  157 ----AYSMTKGAINTMTFTLAKQLGARGITVNAILPGFI 191
PRK07023 PRK07023
SDR family oxidoreductase;
7-188 8.61e-06

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 45.00  E-value: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGA-KAAAGDLGGDHLafsCDVAKEHDVQ-----NTFEELEKHLGRVnFL 80
Cdd:PRK07023    6 VTGHSRGLGAALAEQLLQPGIAVLGVARSRHPSlAAAAGERLAEVE---LDLSDAAAAAawlagDLLAAFVDGASRV-LL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  81 VNAAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCKAAMRTMIQQQggsivnvgHRRemLLHKRSIVGLKGNSGQSVYS 159
Cdd:PRK07023   82 INNAGTVEPIGPLATLDAAAIARaVGLNVAAPLMLTAALAQAASDAA--------ERR--ILHISSGAARNAYAGWSVYC 151

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEvARKKIRVNVVAP 188
Cdd:PRK07023  152 ATKAALDHHARAVALD-ANRALRIVSLAP 179
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 7-199 9.29e-06

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 45.24  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH---------LAFSCDVAKE-HDVQNTFEELEkhlgr 76
Cdd:PLN02780   58 VTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYsktqiktvvVDFSGDIDEGvKRIKETIEGLD----- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  77 VNFLVNAAGINRD-GLLVRTKTEDMVSQL-HTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHRREMLLHKRSIVglkgnsg 154
Cdd:PLN02780  133 VGVLINNVGVSYPyARFFHEVDEELLKNLiKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSDPLY------- 205

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462599477 155 qSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELIP-RTVSIRK 199
Cdd:PLN02780  206 -AVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVAtKMASIRR 250
PRK12742 PRK12742
SDR family oxidoreductase;
7-188 1.08e-05

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 44.75  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLA-VIARNLEGAKAAAGDLGGDhlAFSCDVAKEHDVQNTFEELekhlGRVNFLVNAAG 85
Cdd:PRK12742   11 VLGGSRGIGAAIVRRFVTDGANVRfTYAGSKDAAERLAQETGAT--AVQTDSADRDAVIDVVRKS----GALDILVVNAG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGhrremllhkrsivGLKGN----SGQSVYSAS 161
Cdd:PRK12742   85 IAVFGDALELDADDIDRLFKINIHAPYHASVEAARQM--PEGGRIIIIG-------------SVNGDrmpvAGMAAYAAS 149

                         170       180
                  ....*....|....*....|....*..
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK12742  150 KSALQGMARGLARDFGPRGITINVVQP 176
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 60-191 1.18e-05

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 44.87  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  60 EHDVQNTFEELEKHLGRVNFLVNAAGINRD-GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrre 138
Cdd:cd05361    56 EQKPEELVDAVLQAGGAIDVLVSNDYIPRPmNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFI----- 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462599477 139 mllhkRSIVGLKGNSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVAPELI 191
Cdd:cd05361   131 -----TSAVPKKPLAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFF 178
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
12-198 1.28e-05

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 44.72  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  12 RGIGRAVAQLMARKGYRLAVI---ARNLEGAKAAAGDLGG-DHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNA-AGI 86
Cdd:PRK08594   19 RSIAWGIARSLHNAGAKLVFTyagERLEKEVRELADTLEGqESLLLPCDVTSDEEITACFETIKEEVGVIHGVAHCiAFA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 NRD---GLLVRTKTEDMVsqLHTNLLGSMLT--CKAAMRTMiqQQGGSIVNVGHrremllhkrsIVGLKGNSGQSVYSAS 161
Cdd:PRK08594   99 NKEdlrGEFLETSRDGFL--LAQNISAYSLTavAREAKKLM--TEGGSIVTLTY----------LGGERVVQNYNVMGVA 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAPELIpRTVSIR 198
Cdd:PRK08594  165 KASLEASVKYLANDLGKDGIRVNAISAGPI-RTLSAK 200
PRK08862 PRK08862
SDR family oxidoreductase;
10-190 1.78e-05

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 44.33  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  10 GSRgIGRAVAQLMARKGYRLAVIARNLEGAKA---AAGDLGGDHLAFSCDVAKEHDVQNTFEELEKHLGRV-NFLVNAAG 85
Cdd:PRK08862   14 GSV-LGRTISCHFARLGATLILCDQDQSALKDtyeQCSALTDNVYSFQLKDFSQESIRHLFDAIEQQFNRApDVLVNNWT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  86 INRDGLLVRTKTEDMVSQLHTNLLGSMLT----CKAAMRTmiQQQGGSIVNVGHRREmlLHKRSIVglkgnsgqsvySAS 161
Cdd:PRK08862   93 SSPLPSLFDEQPSESFIQQLSSLASTLFTygqvAAERMRK--RNKKGVIVNVISHDD--HQDLTGV-----------ESS 157

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 162 KGGLVGFSRALAKEVARKKIRVNVVAPEL 190
Cdd:PRK08862  158 NALVSGFTHSWAKELTPFNIRVGGVVPSI 186
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-120 2.07e-05

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 44.20  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLafscdvakEHDVQNtFEELEKHLGRVNFLVNAAGI 86
Cdd:COG0451     4 VTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFV--------RGDLRD-PEALAAALAGVDAVVHLAAP 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462599477  87 nrdgllVRTKTEDMVSQLHTNLLGSMLTCKAAMR 120
Cdd:COG0451    75 ------AGVGEEDPDETLEVNVEGTLNLLEAARA 102
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 11-191 2.37e-05

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 44.08  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  11 SRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGG----DHLAFSCDVAKEHDVQNTFEELeKHLGRVNFLVNAAGI 86
Cdd:PRK08339   17 SKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSesnvDVSYIVADLTKREDLERTVKEL-KNIGEPDIFFFSTGG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVnvghRREMLLHKRSIVGLkgnSGQSVYSASKGGLV 166
Cdd:PRK08339   96 PKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRII----YSTSVAIKEPIPNI---ALSNVVRISMAGLV 168

                         170       180
                  ....*....|....*....|....*
gi 2462599477 167 gfsRALAKEVARKKIRVNVVAPELI 191
Cdd:PRK08339  169 ---RTLAKELGPKGITVNGIMPGII 190
PRK08340 PRK08340
SDR family oxidoreductase;
7-85 2.63e-05

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 44.03  E-value: 2.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLG--GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAA 84
Cdd:PRK08340    5 VTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKeyGEVYAVKADLSDKDDLKNLVKEAWELLGGIDALVWNA 84


                  .
gi 2462599477  85 G 85
Cdd:PRK08340   85 G 85
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 9-192 4.10e-05

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 43.25  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   9 GGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDVQNTFEELEKhLGRVNFLVNAAGINR 88
Cdd:cd08951    14 GSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNA-IGRFDAVIHNAGILS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  89 DGlLVRTKTEDMVSQLHTNLLGS-MLTCKAA-------MRTMIQQQGGSIVNvghrrEMLLHKRsivglkGNSGQSVYSA 160
Cdd:cd08951    93 GP-NRKTPDTGIPAMVAVNVLAPyVLTALIRrpkrliyLSSGMHRGGNASLD-----DIDWFNR------GENDSPAYSD 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462599477 161 SKgglvGFSRALAKEVAR--KKIRVNVVAPELIP 192
Cdd:cd08951   161 SK----LHVLTLAAAVARrwKDVSSNAVHPGWVP 190
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
11-184 4.66e-05

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 43.03  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  11 SRGIGRAVAQLMARKGYRLA---VIARNLEGAKAAAGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGIN 87
Cdd:PRK08690   17 ERSIAYGIAKACREQGAELAftyVVDKLEERVRKMAAELDSE-LVFRCDVASDDEINQVFADLGKHWDGLDGLVHSIGFA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  88 -RDGL---LVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGHrremLLHKRSIvglkgnSGQSVYSASKG 163
Cdd:PRK08690   96 pKEALsgdFLDSISREAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSY----LGAVRAI------PNYNVMGMAKA 165

                         170       180
                  ....*....|....*....|.
gi 2462599477 164 GLVGFSRALAKEVARKKIRVN 184
Cdd:PRK08690  166 SLEAGIRFTAACLGKEGIRCN 186
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
43-187 6.58e-05

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 42.82  E-value: 6.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  43 AGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAGINR----DGLLVRTKTEDMVSQLHTNLLGSMLTCKAA 118
Cdd:PRK08159   56 AAELGAF-VAGHCDVTDEASIDAVFETLEKKWGKLDFVVHAIGFSDkdelTGRYVDTSRDNFTMTMDISVYSFTAVAQRA 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462599477 119 MRTMiqQQGGSIVNV---GHRREMllhkrsivglkgnSGQSVYSASKGGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:PRK08159  135 EKLM--TDGGSILTLtyyGAEKVM-------------PHYNVMGVAKAALEASVKYLAVDLGPKNIRVNAIS 191
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 10-94 6.70e-05

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 41.04  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  10 GSRGIGRAVAQLMARKG--YRLAVIARNLEGAKAAAGDLGGDHLafscdVAKEHDVQNTFEELEKHLGRVNFLVNAAGIN 87
Cdd:pfam03435   5 GAGSVGQGVAPLLARHFdvDRITVADRTLEKAQALAAKLGGVRF-----IAVAVDADNYEAVLAALLKEGDLVVNLSPPT 79


                  ....*..
gi 2462599477  88 RDGLLVR 94
Cdd:pfam03435  80 LSLDVLK 86
PRK08416 PRK08416
enoyl-ACP reductase;
3-187 1.08e-04

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 42.07  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLA-VIARNLEGAKAAAGDL----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK08416    9 KTLVISGGTRGIGKAIVYEFAQSGVNIAfTYNSNVEEANKIAEDLeqkyGIKAKAYPLNILEPETYKELFKKIDEDFDRV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  78 NFLVNAAGINRD------GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVghrremllhkrsivglkG 151
Cdd:PRK08416   89 DFFISNAIISGRavvggyTKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISL-----------------S 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462599477 152 NSGQSVY-------SASKGGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:PRK08416  152 STGNLVYienyaghGTSKAAVETMVKYAATELGEKNIRVNAVS 194
PRK06196 PRK06196
oxidoreductase; Provisional
 3-137 1.26e-04

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 41.98  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAfSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:PRK06196   27 KTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDGVEVV-MLDLADLESVRAFAERFLDSGRRIDILIN 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462599477  83 AAGINRDGLlvrTKTED-MVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNV---GHRR 137
Cdd:PRK06196  106 NAGVMACPE---TRVGDgWEAQFATNHLGHFALVNLLWPALAAGAGARVVALssaGHRR 161
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 6-213 1.60e-04

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: 41.33  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   6 AVFGGSRGIGRAVAQLMARKGYRlaVIARNLEGAKAAAgDLGgdhlafscdvAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:cd05328     3 VITGAASGIGAATAELLEDAGHT--VIGIDLREADVIA-DLS----------TPEGRAAAIADVLARCSGVLDGLVNCAG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  86 INrdgllVRTKTEDMVSqlhTNLLGSMLTCKAAMRTMIQQQGGSIVNVG-------HRREMLLHK----------RSIVG 148
Cdd:cd05328    70 VG-----GTTVAGLVLK---VNYFGLRALMEALLPRLRKGHGPAAVVVSsiagagwAQDKLELAKalaagtearaVALAE 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599477 149 LKGNSGQSVYSASKGGLVGFSRALAKE-VARKKIRVNVVAPELI--PRTVSIRKMEKGDRINVTLRSP 213
Cdd:cd05328   142 HAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVetPILQAFLQDPRGGESVDAFVTP 209
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 3-89 1.70e-04

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. 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: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 41.46  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAA--AGDLGGdHLAFSCDVAkehdvqnTFEELEKHLGRVNFL 80
Cdd:cd05271     1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEAYARRLlvMGDLGQ-VLFVEFDLR-------DDESIRKALEGSDVV 72


                  ....*....
gi 2462599477  81 VNAAGINRD 89
Cdd:cd05271    73 INLVGRLYE 81
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 7-116 1.76e-04

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 41.73  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIA-RNLEGAKAAAGDLG---GDHLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVN 82
Cdd:cd09810     6 ITGASSGLGLAAAKALARRGEWHVVMAcRDFLKAEQAAQEVGmpkDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDALVC 85

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462599477  83 AAGINRDGLLVRTKTEDMVSQ-LHTNLLGSMLTCK 116
Cdd:cd09810    86 NAAVYLPTAKEPRFTADGFELtVGVNHLGHFLLTN 120
PRK07102 PRK07102
SDR family oxidoreductase;
7-188 1.80e-04

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 41.45  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL---GGDHLAFScdvakEHDVqNTFEE----LEKHLGRVNF 79
Cdd:PRK07102    6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLrarGAVAVSTH-----ELDI-LDTAShaafLDSLPALPDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  80 LVNAAGINRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMIQQQGGSIVNVGhrremllhkrSIVGLKGNSGQSVYS 159
Cdd:PRK07102   80 VLIAVGTLGDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGIS----------SVAGDRGRASNYVYG 149

                         170       180
                  ....*....|....*....|....*....
gi 2462599477 160 ASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK07102  150 SAKAALTAFLSGLRNRLFKSGVHVLTVKP 178
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 3-136 2.00e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 41.55  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   3 KVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDL-----GGDHLAFSCDVAKEHDVQNTFEELEKHLGRV 77
Cdd:PRK06197   17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARItaatpGADVTLQELDLTSLASVRAAADALRAAYPRI 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462599477  78 NFLVNAAGINrdgLLVRTKTEDMVS-QLHTNLLGSMLTCKAAMRTMIQQQGGSIVNV---GHR 136
Cdd:PRK06197   97 DLLINNAGVM---YTPKQTTADGFElQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVssgGHR 156
PRK05993 PRK05993
SDR family oxidoreductase;
1-188 4.25e-04

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 40.40  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   1 MDKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAaagdLGGDHL-AFSCDVAKEHDVQNTFEE-LEKHLGRVN 78
Cdd:PRK05993    3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAA----LEAEGLeAFQLDYAEPESIAALVAQvLELSGGRLD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  79 FLVNAAGINRDGLLVRTKTEDMVSQLHTNLLG-SMLTCKA--AMRTmiqQQGGSIVnvghrremllHKRSIVGLKGNSGQ 155
Cdd:PRK05993   79 ALFNNGAYGQPGAVEDLPTEALRAQFEANFFGwHDLTRRVipVMRK---QGQGRIV----------QCSSILGLVPMKYR 145

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462599477 156 SVYSASKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05993  146 GAYNASKFAIEGLSLTLRMELQGSGIHVSLIEP 178
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
14-187 4.81e-04

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 39.99  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  14 IGRAVAQLMARKG------YRLAVIARNLegaKAAAGDLGGDHLAfSCDVAKEHDVQNTFEELEKHLGRVNFLVNA-AGI 86
Cdd:PRK06603   22 ISWAIAQLAKKHGaelwftYQSEVLEKRV---KPLAEEIGCNFVS-ELDVTNPKSISNLFDDIKEKWGSFDFLLHGmAFA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 NRD---GLLVRTKTEDMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVGHR-REMLLHKRSIVGLkgnsgqsvysaSK 162
Cdd:PRK06603   98 DKNelkGRYVDTSLENFHNSLHISCYSLLELSRSAEALM--HDGGSIVTLTYYgAEKVIPNYNVMGV-----------AK 164

                         170       180
                  ....*....|....*....|....*
gi 2462599477 163 GGLVGFSRALAKEVARKKIRVNVVA 187
Cdd:PRK06603  165 AALEASVKYLANDMGENNIRVNAIS 189
PRK05884 PRK05884
SDR family oxidoreductase;
7-188 1.83e-03

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 38.25  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDhlAFSCDVAKEHDVQNTFEELEKHLgrvNFLVN---- 82
Cdd:PRK05884    5 VTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVD--AIVCDNTDPASLEEARGLFPHHL---DTIVNvpap 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  83 --AAGINRDGLLVRTKTEdMVSQLHTNLLGSMLTCKAAMRTMiqQQGGSIVNVghrremllhkrsiVGLKGNSGqSVYSA 160
Cdd:PRK05884   80 swDAGDPRTYSLADTANA-WRNALDATVLSAVLTVQSVGDHL--RSGGSIISV-------------VPENPPAG-SAEAA 142

                         170       180
                  ....*....|....*....|....*...
gi 2462599477 161 SKGGLVGFSRALAKEVARKKIRVNVVAP 188
Cdd:PRK05884  143 IKAALSNWTAGQAAVFGTRGITINAVAC 170
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
6-46 2.12e-03

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


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 37.91  E-value: 2.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462599477   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARN-------LEGAKAAAGDL 46
Cdd:COG2910     3 AVIGATGRVGSLIVREALARGHEVTALVRNpeklpdeHPGLTVVVGDV 50
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 2-43 4.13e-03

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 36.99  E-value: 4.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462599477   2 DKVCAVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAA 43
Cdd:cd01078    28 GKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAA 69
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
6-50 5.19e-03

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 37.13  E-value: 5.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462599477   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDH 50
Cdd:COG5322   155 AVVGATGSIGSVCARLLAREVKRLTLVARNLERLEELAEEILRNP 199
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 6-63 5.30e-03

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 37.27  E-value: 5.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599477   6 AVFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAKAAAGDLGGDHLAFSCDVAKEHDV 63
Cdd:PRK08655    4 SIIGGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEYANDNIDAAKDADI 61
PRK06953 PRK06953
SDR family oxidoreductase;
7-165 5.78e-03

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 36.59  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477   7 VFGGSRGIGRAVAQLMARKGYRLAVIARNLEGAkAAAGDLGGDhlAFSCDVAKEHDVQNTFEELEKHlgRVNFLVNAAGI 86
Cdd:PRK06953    6 IVGASRGIGREFVRQYRADGWRVIATARDAAAL-AALQALGAE--ALALDVADPASVAGLAWKLDGE--ALDAAVYVAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462599477  87 --NRDGLLVRTKTEDMVSQLHTNLLGSMLTCKAAMrTMIQQQGGSIVNVGHRREmllhkrSIVGLKGNSGQsVYSASKGG 164
Cdd:PRK06953   81 ygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILL-PLVEAAGGVLAVLSSRMG------SIGDATGTTGW-LYRASKAA 152


                  .
gi 2462599477 165 L 165
Cdd:PRK06953  153 L 153
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
11-85 6.12e-03

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 36.72  E-value: 6.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462599477  11 SRGIGRAVAQLMARKGYRLA---VIARNLEGAKAAAGDLGGDhLAFSCDVAKEHDVQNTFEELEKHLGRVNFLVNAAG 85
Cdd:PRK06997   17 NRSIAYGIAKACKREGAELAftyVGDRFKDRITEFAAEFGSD-LVFPCDVASDEQIDALFASLGQHWDGLDGLVHSIG 93
 
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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