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Conserved domains on  [gi|1993940993|ref|XP_039599779|]
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carbonyl reductase [NADPH] 1 [Polypterus senegalus]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143144)

SDR family NAD(P)-dependent oxidoreductase with similarity to mammalian carbonyl reductase, which catalyzes the NADPH-dependent reduction of a wide range of substrates including quinones, prostaglandins, and other carbonyl-containing compounds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 5-276 4.72e-113

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: 324.58  E-value: 4.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFKVADT-TPFGNQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGSMAlrqcsqslkekfrsed 161
Cdd:cd05324    81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKSpaGRIVNVSSGLGSLT---------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 162 iteeelvelmenfvedakkgvhtqkgwpnWAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDMAGPHATK 241
Cdd:cd05324   145 -----------------------------SAYGVSKAALNALTRILAKELK----ETGIKVNACCPGWVKTDMGGGKAPK 191

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1993940993 242 TPDEGAITPVYLALLsEEDIEPHGQFVCEKKTQSW 276
Cdd:cd05324   192 TPEEGAETPVYLALL-PPDGEPTGKFFSDKKVVPW 225
 
Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 5-276 4.72e-113

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: 324.58  E-value: 4.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFKVADT-TPFGNQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGSMAlrqcsqslkekfrsed 161
Cdd:cd05324    81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKSpaGRIVNVSSGLGSLT---------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 162 iteeelvelmenfvedakkgvhtqkgwpnWAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDMAGPHATK 241
Cdd:cd05324   145 -----------------------------SAYGVSKAALNALTRILAKELK----ETGIKVNACCPGWVKTDMGGGKAPK 191

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1993940993 242 TPDEGAITPVYLALLsEEDIEPHGQFVCEKKTQSW 276
Cdd:cd05324   192 TPEEGAETPVYLALL-PPDGEPTGKFFSDKKVVPW 225
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 5-259 2.59e-46

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: 155.33  E-value: 2.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:COG1028     7 KVALVTGGSSGIGRAIARALAAEGA-RVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAF--KVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGsmalrqcsqslkekfrse 160
Cdd:COG1028    86 ILVNNAGITPpgPLEELTE--EDWDRVLDVNLKGPFLLTRAALPHMRERggGRIVNISSIAG------------------ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 161 diteeelvelmenfvedakkgvhtQKGWPNW-AYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGPHA 239
Cdd:COG1028   146 ------------------------LRGSPGQaAYAASKAAVVGLTRSLALEL----APRGIRVNAVAPGPIDTPMTRALL 197

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1993940993 240 TK-----------------TPDEGAitPVYLALLSEE 259
Cdd:COG1028   198 GAeevrealaariplgrlgTPEEVA--AAVLFLASDA 232
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 5-237 6.13e-40

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 137.36  E-value: 6.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGA-KVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIafkvADTTPFGNQAEE----TLRTNFFATRDICRELLP--IIKPSGRVVNIASIAGsmalrqcsqslkekfr 158
Cdd:pfam00106  80 ILVNNAGI----TGLGPFSELSDEdwerVIDVNLTGVFNLTRAVLPamIKGSGGRIVNISSVAG---------------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmenfvedakkgvhtQKGWPNW-AYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGP 237
Cdd:pfam00106 140 --------------------------LVPYPGGsAYSASKAAVIGFTRSLALEL----APHGIRVNAVAPGGVDTDMTKE 189
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
5-234 9.99e-30

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 112.18  E-value: 9.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK05653    6 KTALVTGASRGIGRAIALRLAADGA-KVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIafkvADTTPFGNQAEE----TLRTN---FFATrdiCRELLPIIKPS--GRVVNIASIAGSMalrqcsqslke 155
Cdd:PRK05653   85 ILVNNAGI----TRDALLPRMSEEdwdrVIDVNltgTFNV---VRAALPPMIKAryGRIVNISSVSGVT----------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 156 kfrsediteeelvelmenfvedakkgvhtqkGWPNWA-YGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDM 234
Cdd:PRK05653  147 -------------------------------GNPGQTnYSAAKAGVIGFTKALALEL----ASRGITVNAVAPGFIDTDM 191
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-112 2.13e-08

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: 52.87  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993    9 VTGANKGIGLAIVRALCRQFAGHVYLTAR---DEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDV 85
Cdd:smart00822   5 ITGGLGGLGRALARWLAERGARRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTG 84

                           90       100
                   ....*....|....*....|....*..
gi 1993940993   86 LVNNAAiafkVADTTPFGNQAEETLRT 112
Cdd:smart00822  85 VIHAAG----VLDDGVLASLTPERFAA 107
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 4-146 1.22e-05

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


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 45.39  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQF------------AGHVY-LTARDEgrgMAAVQTLQNEGLDPHFhqLDITDLSSIR 70
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGwrvvavdlcaddPAVGYpLATRAE---LDAVAAACPDQVLPVI--ADVRDPAALA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  71 RIRDFMRDKYGGVDVLVNNAAIafkVADTTPFGNQAEETLRT----NFFATRDICRELLPII----KP-SGRVVNIASIA 141
Cdd:TIGR04504  76 AAVALAVERWGRLDAAVAAAGV---IAGGRPLWETTDAELDLlldvNLRGVWNLARAAVPAMlarpDPrGGRFVAVASAA 152


                  ....*
gi 1993940993 142 GSMAL 146
Cdd:TIGR04504 153 ATRGL 157
 
Name Accession Description Interval E-value
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 5-276 4.72e-113

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: 324.58  E-value: 4.72e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFKVADT-TPFGNQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGSMAlrqcsqslkekfrsed 161
Cdd:cd05324    81 ILVNNAGIAFKGFDDsTPTREQARETMKTNFFGTVDVTQALLPLLKKSpaGRIVNVSSGLGSLT---------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 162 iteeelvelmenfvedakkgvhtqkgwpnWAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDMAGPHATK 241
Cdd:cd05324   145 -----------------------------SAYGVSKAALNALTRILAKELK----ETGIKVNACCPGWVKTDMGGGKAPK 191

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1993940993 242 TPDEGAITPVYLALLsEEDIEPHGQFVCEKKTQSW 276
Cdd:cd05324   192 TPEEGAETPVYLALL-PPDGEPTGKFFSDKKVVPW 225
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 5-259 2.59e-46

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: 155.33  E-value: 2.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:COG1028     7 KVALVTGGSSGIGRAIARALAAEGA-RVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAF--KVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGsmalrqcsqslkekfrse 160
Cdd:COG1028    86 ILVNNAGITPpgPLEELTE--EDWDRVLDVNLKGPFLLTRAALPHMRERggGRIVNISSIAG------------------ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 161 diteeelvelmenfvedakkgvhtQKGWPNW-AYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGPHA 239
Cdd:COG1028   146 ------------------------LRGSPGQaAYAASKAAVVGLTRSLALEL----APRGIRVNAVAPGPIDTPMTRALL 197

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1993940993 240 TK-----------------TPDEGAitPVYLALLSEE 259
Cdd:COG1028   198 GAeevrealaariplgrlgTPEEVA--AAVLFLASDA 232
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 7-268 3.86e-44

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: 149.36  E-value: 3.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQtLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDVL 86
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGA-KVVLADRNEEALAELAA-IEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  87 VNNAAIA--FKVADTTPfgNQAEETLRTNFFATRDICRELLPIIK--PSGRVVNIASIAGsmalrqcsqslkekfrsedi 162
Cdd:cd05233    79 VNNAGIArpGPLEELTD--EDWDRVLDVNLTGVFLLTRAALPHMKkqGGGRIVNISSVAG-------------------- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 163 teeelvelmenfvedakkgvhtQKGWPNW-AYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMA------ 235
Cdd:cd05233   137 ----------------------LRPLPGQaAYAASKAALEGLTRSLALEL----APYGIRVNAVAPGLVDTPMLaklgpe 190

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1993940993 236 ---GPHATKTPDEGAITP-----VYLALLSEEDIEPHGQFV 268
Cdd:cd05233   191 eaeKELAAAIPLGRLGTPeevaeAVVFLASDEASYITGQVI 231
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4-250 9.00e-44

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 148.86  E-value: 9.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:COG0300     5 GKTVLITGASSGIGRALARALAARGA-RVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAF--KVADTTPfgNQAEETLRTNFFATRDICRELLPIIK--PSGRVVNIASIAGSMalrqcsqslkekfrs 159
Cdd:COG0300    84 DVLVNNAGVGGggPFEELDL--EDLRRVFEVNVFGPVRLTRALLPLMRarGRGRIVNVSSVAGLR--------------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 160 editeeelvelmenfvedakkgvhtqkGWPNW-AYGVSKIGVIVLSRIQAKELSHkrgqSKILLNSCCPGWVKTDMAGpH 238
Cdd:COG0300   147 ---------------------------GLPGMaAYAASKAALEGFSESLRAELAP----TGVRVTAVCPGPVDTPFTA-R 194

                         250
                  ....*....|..
gi 1993940993 239 ATKTPDEGAITP 250
Cdd:COG0300   195 AGAPAGRPLLSP 206
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 5-237 6.13e-40

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 137.36  E-value: 6.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGA-KVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIafkvADTTPFGNQAEE----TLRTNFFATRDICRELLP--IIKPSGRVVNIASIAGsmalrqcsqslkekfr 158
Cdd:pfam00106  80 ILVNNAGI----TGLGPFSELSDEdwerVIDVNLTGVFNLTRAVLPamIKGSGGRIVNISSVAG---------------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmenfvedakkgvhtQKGWPNW-AYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGP 237
Cdd:pfam00106 140 --------------------------LVPYPGGsAYSASKAAVIGFTRSLALEL----APHGIRVNAVAPGGVDTDMTKE 189
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 5-275 1.25e-35

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: 128.50  E-value: 1.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDP--HFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:cd05327     2 KVVVITGANSGIGKETARELAKRGA-HVIIACRNEEKGEEAAAEIKKETGNAkvEVIQLDLSSLASVRQFAEEFLARFPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIAFKVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGSMAlrqcsqslkeKFRSE 160
Cdd:cd05327    81 LDILINNAGIMAPPRRLTK--DGFELQFAVNYLGHFLLTNLLLPVLKASapSRIVNVSSIAHRAG----------PIDFN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 161 DITEEELVELmenfvedakkgvhtqkgWPNWAYGVSKIGVIVLsriqAKELSHKRGQSKILLNSCCPGWVKTDM------ 234
Cdd:cd05327   149 DLDLENNKEY-----------------SPYKAYGQSKLANILF----TRELARRLEGTGVTVNALHPGVVRTELlrrngs 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1993940993 235 -------AGPHATKTPDEGAITPVYLALLSEEDIEPHGQFVCEKKTQS 275
Cdd:cd05327   208 ffllyklLRPFLKKSPEQGAQTALYAATSPELEGVSGKYFSDCKIKMS 255
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 5-261 7.03e-35

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 125.68  E-value: 7.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRqfAGH-VYLTARDEGRGMAAVQTLqneGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:COG4221     6 KVALITGASSGIGAATARALAA--AGArVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFGRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAF--KVADTTPfgNQAEETLRTNFFATRDICRELLPIIKP--SGRVVNIASIAGsmalrqcsqslkekfrs 159
Cdd:COG4221    81 DVLVNNAGVALlgPLEELDP--EDWDRMIDVNVKGVLYVTRAALPAMRArgSGHIVNISSIAG----------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 160 editeeelvelmenfvedakkgvhtQKGWPNWA-YGVSKIGVIVLSRIQAKELSHKRGQSKILlnscCPGWVKTDMAGPH 238
Cdd:COG4221   142 -------------------------LRPYPGGAvYAATKAAVRGLSESLRAELRPTGIRVTVI----EPGAVDTEFLDSV 192

                         250       260
                  ....*....|....*....|...
gi 1993940993 239 ATKTPDEGAITPVYLALLSEEDI 261
Cdd:COG4221   193 FDGDAEAAAAVYEGLEPLTPEDV 215
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 5-256 2.78e-31

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: 115.92  E-value: 2.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDegrgMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGY-RVSLGLRN----PEDLAALSASGGDVEAVPYDARDPEDARALVDALRDRFGRID 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFKVadTTPFGNQA--EETLRTNFFATRDICRELLP--IIKPSGRVVNIASIAGSMALRqcsqslkekFRSe 160
Cdd:cd08932    76 VLVHNAGIGRPT--TLREGSDAelEAHFSINVIAPAELTRALLPalREAGSGRVVFLNSLSGKRVLA---------GNA- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 161 diteeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDMAGPHA- 239
Cdd:cd08932   144 -------------------------------GYSASKFALRALAHALRQEGWDH----GVRVSAVCPGFVDTPMAQGLTl 188

                         250
                  ....*....|....*...
gi 1993940993 240 -TKTPDEGAITPVYLALL 256
Cdd:cd08932   189 vGAFPPEEMIQPKDIANL 206
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 11-259 1.35e-30

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: 114.06  E-value: 1.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  11 GA--NKGIGLAIVRALCRQFAgHVYLTARDEgRGMAAVQTLQNEgLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDVLVN 88
Cdd:pfam13561   1 GAanESGIGWAIARALAEEGA-EVVLTDLNE-ALAKRVEELAEE-LGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  89 NAAIAFK----VADTTPfgNQAEETLRTNFFATRDICRELLPIIKPSGRVVNIASIAGsmalrqcsqslkekfrsedite 164
Cdd:pfam13561  78 NAGFAPKlkgpFLDTSR--EDFDRALDVNLYSLFLLAKAALPLMKEGGSIVNLSSIGA---------------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 165 eelvelmenfvedakkgvhtQKGWPN-WAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGP------ 237
Cdd:pfam13561 134 --------------------ERVVPNyNAYGAAKAALEALTRYLAVEL----GPRGIRVNAISPGPIKTLAASGipgfde 189

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1993940993 238 ----HATKTPDEGAITP-----VYLALLSEE 259
Cdd:pfam13561 190 llaaAEARAPLGRLGTPeevanAAAFLASDL 220
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
5-234 9.99e-30

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 112.18  E-value: 9.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK05653    6 KTALVTGASRGIGRAIALRLAADGA-KVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIafkvADTTPFGNQAEE----TLRTN---FFATrdiCRELLPIIKPS--GRVVNIASIAGSMalrqcsqslke 155
Cdd:PRK05653   85 ILVNNAGI----TRDALLPRMSEEdwdrVIDVNltgTFNV---VRAALPPMIKAryGRIVNISSVSGVT----------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 156 kfrsediteeelvelmenfvedakkgvhtqkGWPNWA-YGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDM 234
Cdd:PRK05653  147 -------------------------------GNPGQTnYSAAKAGVIGFTKALALEL----ASRGITVNAVAPGFIDTDM 191
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 7-268 1.48e-29

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: 111.62  E-value: 1.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGrGMAAVQTLQNEGLDPHFHQLDITDL--SSIRRIRDfmRDKYGGVD 84
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPS-AATELAALGASHSRLHILELDVTDEiaESAEAVAE--RLGDAGLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIA--FKVADTTPFGNqAEETLRTNFFATRDICRELLPIIKPSGR--VVNIASIAGSMALRqcsqslkekfrse 160
Cdd:cd05325    78 VLINNAGILhsYGPASEVDSED-LLEVFQVNVLGPLLLTQAFLPLLLKGARakIINISSRVGSIGDN------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 161 diteeelvelmenfvedakkgvhTQKGWpnWAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGPHAT 240
Cdd:cd05325   144 -----------------------TSGGW--YSYRASKAALNMLTKSLAVEL----KRDGITVVSLHPGWVRTDMGGPFAK 194

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1993940993 241 ktpDEGAITPVY-----LALLSEEDIEPHGQFV 268
Cdd:cd05325   195 ---NKGPITPEEsvaglLKVIDNLNEEDSGKFL 224
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 5-146 1.66e-28

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: 109.24  E-value: 1.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfaGH-VYLTARDEgrgmAAVQTLQNEgLDPHFH--QLDITDLSSIRRIRDFMRDKYG 81
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQ--GYrVIATARNP----DKLESLGEL-LNDNLEvlELDVTDEESIKAAVKEVIERFG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  82 GVDVLVNNAAIAFK--VADTTPfgNQAEETLRTNFFATRDICRELLPIIK--PSGRVVNIASIAGSMAL 146
Cdd:cd05374    74 RIDVLVNNAGYGLFgpLEETSI--EEVRELFEVNVFGPLRVTRAFLPLMRkqGSGRIVNVSSVAGLVPT 140
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 5-234 5.45e-28

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 107.59  E-value: 5.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK05557    6 KVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIA-------FKVADttpFgnqaEETLRTN----FFATRDICRELLPiiKPSGRVVNIASIAGSMalrqcsqsl 153
Cdd:PRK05557   86 ILVNNAGITrdnllmrMKEED---W----DRVIDTNltgvFNLTKAVARPMMK--QRSGRIINISSVVGLM--------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 154 kekfrsediteeelvelmenfvedakkgvhtqkGWPNWA-YGVSKIGVIVLSRIQAKELShKRGqskILLNSCCPGWVKT 232
Cdd:PRK05557  148 ---------------------------------GNPGQAnYAASKAGVIGFTKSLARELA-SRG---ITVNAVAPGFIET 190


                  ..
gi 1993940993 233 DM 234
Cdd:PRK05557  191 DM 192
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 5-234 6.82e-28

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 107.36  E-value: 6.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK12939    8 KRALVTGAARGLGAAFAEALAEAGA-TVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAfKVADTTPFGNQA-EETLRTNFFATRDICRELLPIIK--PSGRVVNIASiagSMALrqcsqslkekfrsed 161
Cdd:PRK12939   87 GLVNNAGIT-NSKSATELDIDTwDAVMNVNVRGTFLMLRAALPHLRdsGRGRIVNLAS---DTAL--------------- 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993 162 iteeelvelmenfvedakkgvhtqKGWPNW-AYGVSKIGVIVLSRIQAKELSHKRgqskILLNSCCPGWVKTDM 234
Cdd:PRK12939  148 ------------------------WGAPKLgAYVASKGAVIGMTRSLARELGGRG----ITVNAIAPGLTATEA 193
PRK08264 PRK08264
SDR family oxidoreductase;
5-142 4.53e-26

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 102.27  E-value: 4.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGR---GMAAVQTLqnegldphfhQLDITDLSSIRRIRDFMRDkyg 81
Cdd:PRK08264    7 KVVLVTGANRGIGRAFVEQLLARGAAKVYAAARDPESvtdLGPRVVPL----------QLDVTDPASVAAAAEAASD--- 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993  82 gVDVLVNNAAIAfkvADTTPFGNQAEETLR----TNFFATRDICRELLPIIK--PSGRVVNIASIAG 142
Cdd:PRK08264   74 -VTILVNNAGIF---RTGSLLLEGDEDALRaemeTNYFGPLAMARAFAPVLAanGGGAIVNVLSVLS 136
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 5-234 2.71e-25

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: 100.31  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGA-KVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIafkVADTTpFGNQAEE----TLRTNFFATRDICRELLPII--KPSGRVVNIASIAGsmalrqcsqslkekfr 158
Cdd:cd05333    80 ILVNNAGI---TRDNL-LMRMSEEdwdaVINVNLTGVFNVTQAVIRAMikRRSGRIINISSVVG---------------- 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993 159 sediteeelveLMENFvedakkgvhtqkGWPNwaYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDM 234
Cdd:cd05333   140 -----------LIGNP------------GQAN--YAASKAGVIGFTKSLAKELASR----GITVNAVAPGFIDTDM 186
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 5-268 6.53e-25

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: 99.83  E-value: 6.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNE-GLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd08940     3 KVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKhGVKVLYHGADLSKPAAIEDMVAYAQRQFGGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAFkVADTTPFGNQAEE-----TLRTNFFATRDIcrelLPIIKPS--GRVVNIASIAGsmalrqcsqslkek 156
Cdd:cd08940    83 DILVNNAGIQH-VAPIEDFPTEKWDaiialNLSAVFHTTRLA----LPHMKKQgwGRIINIASVHG-------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 157 frsediteeelvelmenFVEDAKKGvhtqkgwpnwAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDM-- 234
Cdd:cd08940   144 -----------------LVASANKS----------AYVAAKHGVVGLTKVVALETA----GTGVTCNAICPGWVLTPLve 192

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1993940993 235 ----AGPHATKTPDEGAITpvylALLSEEdiEPHGQFV 268
Cdd:cd08940   193 kqisALAQKNGVPQEQAAR----ELLLEK--QPSKQFV 224
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-239 1.36e-24

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 98.79  E-value: 1.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK12825    7 RVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRID 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAF--KVADTTPfgNQAEETLRTN---FFATrdiCRELLPIIKPS--GRVVNIASIAGSmalrqcsqslkekf 157
Cdd:PRK12825   87 ILVNNAGIFEdkPLADMSD--DEWDEVIDVNlsgVFHL---LRAVVPPMRKQrgGRIVNISSVAGL-------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 158 rsediteeelvelmenfvedakkgvhtqKGWP-NWAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAG 236
Cdd:PRK12825  148 ----------------------------PGWPgRSNYAAAKAGLVGLTKALAREL----AEYGITVNMVAPGDIDTDMKE 195


                  ...
gi 1993940993 237 PHA 239
Cdd:PRK12825  196 ATI 198
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 5-261 2.02e-24

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: 98.50  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05344     2 KVALVTAASSGIGLAIARALAREGA-RVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNA----AIAFkvADTTPfgNQAEETLRTNFFATRDICRELLPIIKP--SGRVVNIASIAGsmalrqcsqslkekfr 158
Cdd:cd05344    81 ILVNNAggppPGPF--AELTD--EDWLEAFDLKLLSVIRIVRAVLPGMKErgWGRIVNISSLTV---------------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelVELMENFVedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELShKRGqskILLNSCCPGWVKTDMAGPH 238
Cdd:cd05344   141 ---------KEPEPNLV----------------LSNVARAGLIGLVKTLSRELA-PDG---VTVNSVLPGYIDTERVRRL 191

                         250       260
                  ....*....|....*....|...
gi 1993940993 239 ATKTPDEGAITPVYLALLSEEDI 261
Cdd:cd05344   192 LEARAEKEGISVEEAEKEVASQI 214
PRK12826 PRK12826
SDR family oxidoreductase;
5-237 2.16e-24

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 98.06  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfaGH-VYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK12826    7 RVALVTGAARGIGRAIAVRLAAD--GAeVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIafkvADTTPFGNQAEETLR----TNFFATRDICRELLPIIKPS--GRVVNIASIAGSmalrqcsqslkekf 157
Cdd:PRK12826   85 DILVANAGI----FPLTPFAEMDDEQWErvidVNLTGTFLLTQAALPALIRAggGRIVLTSSVAGP-------------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 158 rsediteeelvelmenfvedakkgvhtQKGWPNWA-YGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAG 236
Cdd:PRK12826  147 ---------------------------RVGYPGLAhYAASKAGLVGFTRALALEL----AARNITVNSVHPGGVDTPMAG 195


                  .
gi 1993940993 237 P 237
Cdd:PRK12826  196 N 196
FabG-like PRK07231
SDR family oxidoreductase;
5-235 4.27e-24

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 97.59  E-value: 4.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGlDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07231    6 KVAIVTGASSGIGEGIARRFAAEGA-RVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERFGSVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFK---VADTTPfgNQAEETLRTN----FFATrdicRELLPIIKPS--GRVVNIASIAGsmaLRQcsqslke 155
Cdd:PRK07231   84 ILVNNAGTTHRngpLLDVDE--AEFDRIFAVNvkspYLWT----QAAVPAMRGEggGAIVNVASTAG---LRP------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 156 kfrSEDITeeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMA 235
Cdd:PRK07231  148 ---RPGLG----------------------------WYNASKGAVITLTKALAAEL----GPDKIRVNAVAPVVVETGLL 192
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-234 5.73e-24

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 96.83  E-value: 5.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK05565    6 KVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKID 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIA-FK-VADTTpfGNQAEETLRTNFFATRDICRELLPII--KPSGRVVNIASIAGSMAlrqcsqslkekfrse 160
Cdd:PRK05565   86 ILVNNAGISnFGlVTDMT--DEEWDRVIDVNLTGVMLLTRYALPYMikRKSGVIVNISSIWGLIG--------------- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993 161 diteeelvelmenfvedAKKGVhtqkgwpnwAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDM 234
Cdd:PRK05565  149 -----------------ASCEV---------LYSASKGAVNAFTKALAKELA----PSGIRVNAVAPGAIDTEM 192
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 5-146 1.02e-23

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: 95.94  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDegrgMAAVQTLQNEGLDP-HFHQLDITDLSSIRRIRDFMRDkyggV 83
Cdd:cd05354     4 KTVLVTGANRGIGKAFVESLLAHGAKKVYAAVRD----PGSAAHLVAKYGDKvVPLRLDVTDPESIKAAAAQAKD----V 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  84 DVLVNNAAIaFKVAdtTPFGNQAEETLR----TNFFATRDICRELLPIIKPSGR--VVNIASIAGSMAL 146
Cdd:cd05354    76 DVVINNAGV-LKPA--TLLEEGALEALKqemdVNVFGLLRLAQAFAPVLKANGGgaIVNLNSVASLKNF 141
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 5-235 1.37e-22

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: 93.76  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfaGH-VYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd08945     4 EVALVTGATSGIGLAIARRLGKE--GLrVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNA------AIAfKVADTTPFgNQAEETLRTNFFATRDICRELLPIIKPSGRVVNIASIAGsmalrqcsqslkekf 157
Cdd:cd08945    82 DVLVNNAgrsgggATA-ELADELWL-DVVETNLTGVFRVTKEVLKAGGMLERGTGRIINIASTGG--------------- 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993 158 rsediteeelvelmenfvedaKKGVhtQKGWPnwaYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDMA 235
Cdd:cd08945   145 ---------------------KQGV--VHAAP---YSASKHGVVGFTKALGLELA----RTGITVNAVCPGFVETPMA 192
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 5-237 1.86e-22

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: 92.81  E-value: 1.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05347     6 KVALVTGASRGIGFGIASGLAEAGA-NIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKID 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAfKVADTTPFGNQA-EETLRTNFFATRDICRELLPIIKPS--GRVVNIASIagsmalrqcsQSlkekfrsed 161
Cdd:cd05347    85 ILVNNAGII-RRHPAEEFPEAEwRDVIDVNLNGVFFVSQAVARHMIKQghGKIINICSL----------LS--------- 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993 162 iteeelvelmenfvedakkgvhTQKGWPNWAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGP 237
Cdd:cd05347   145 ----------------------ELGGPPVPAYAASKGGVAGLTKALATEW----ARHGIQVNAIAPGYFATEMTEA 194
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 5-266 7.74e-22

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: 91.21  E-value: 7.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGA-KVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIA--FKVADTTPFGNQAEETLRTNFFATrdiCRELLPII--------KPSGRVVNIASIAGSMALRQCSqslk 154
Cdd:cd05323    80 ILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGV---INTTYLALhymdknkgGKGGVIVNIGSVAGLYPAPQFP---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 155 ekfrsediteeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELSHKRGqskILLNSCCPGWVKT-- 232
Cdd:cd05323   153 -------------------------------------VYSASKHGVVGFTRSLADLLEYKTG---VRVNAICPGFTNTpl 192

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1993940993 233 ---------DMAGPHATKTPDEGAITPVYLAllseEDIEPHGQ 266
Cdd:cd05323   193 lpdlvakeaEMLPSAPTQSPEVVAKAIVYLI----EDDEKNGA 231
PRK07326 PRK07326
SDR family oxidoreductase;
5-268 1.12e-21

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 90.46  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGhVYLTARDEGRGMAAVQTLQNEGlDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07326    7 KVALITGGSKGIGFAIAEALLAEGYK-VAITARDQKELEEAAAELNNKG-NVLGLAADVRDEADVQRAVDAIVAAFGGLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIA-FK-VADTTPfgNQAEETLRTNFFATRDICRELLPIIKPS-GRVVNIASIAGSmalrqcsqslkekfrsed 161
Cdd:PRK07326   85 VLIANAGVGhFApVEELTP--EEWRLVIDTNLTGAFYTIKAAVPALKRGgGYIINISSLAGT------------------ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 162 iteeelvelmeNFVEDAKkgvhtqkgwpnwAYGVSKIGVIVLSriQAKELSHKrgQSKILLNSCCPGWVKTDMAGpHATK 241
Cdd:PRK07326  145 -----------NFFAGGA------------AYNASKFGLVGFS--EAAMLDLR--QYGIKVSTIMPGSVATHFNG-HTPS 196

                         250       260
                  ....*....|....*....|....*..
gi 1993940993 242 TPDEGAITPvylallseEDIephGQFV 268
Cdd:PRK07326  197 EKDAWKIQP--------EDI---AQLV 212
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 5-259 1.16e-21

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: 90.91  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLqneGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05341     6 KVAIVTGGARGLGLAHARLLVAEGA-KVVLSDILDEEGQAAAAEL---GDAARFFHLDVTDEDGWTAVVDTAREAFGRLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAF--KVADTTpfgnqAEE---TLRTNFFATRDICRELLPIIKPSGR--VVNIASIAGSMALRQCSqslkekf 157
Cdd:cd05341    82 VLVNNAGILTggTVETTT-----LEEwrrLLDINLTGVFLGTRAVIPPMKEAGGgsIINMSSIEGLVGDPALA------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 158 rsediteeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELshKRGQSKILLNSCCPGWVKTDM--- 234
Cdd:cd05341   150 ----------------------------------AYNASKGAVRGLTKSAALEC--ATQGYGIRVNSVHPGYIYTPMtde 193

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1993940993 235 -----AGPHA-TKTPDEGAITPVYLA-----LLSEE 259
Cdd:cd05341   194 lliaqGEMGNyPNTPMGRAGEPDEIAyavvyLASDE 229
PRK05650 PRK05650
SDR family oxidoreductase;
8-243 2.33e-21

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 90.48  E-value: 2.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   8 MVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDVLV 87
Cdd:PRK05650    4 MITGAASGLGRAIALRWAREGW-RLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  88 NNAAIAfkvadttPFGNQAEETLR-------TNFFATRDICRELLPIIKPS--GRVVNIASIAGSMalrqcsqslkekfr 158
Cdd:PRK05650   83 NNAGVA-------SGGFFEELSLEdwdwqiaINLMGVVKGCKAFLPLFKRQksGRIVNIASMAGLM-------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeeLVELMENfvedakkgvhtqkgwpnwaYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDMAGPH 238
Cdd:PRK05650  142 --------QGPAMSS-------------------YNVAKAGVVALSETLLVELA----DDEIGVHVVCPSFFQTNLLDSF 190


                  ....*
gi 1993940993 239 ATKTP 243
Cdd:PRK05650  191 RGPNP 195
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 5-269 3.91e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 89.73  E-value: 3.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGrgmAAVQTL-QNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK12829   12 LRVLVTGGASGIGRAIAEAFAEAGA-RVHVCDVSEA---ALAATAaRLPGAKVTATVADVADPAQVERVFDTAVERFGGL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIA---FKVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPSGR---VVNIASIAGsmalrqcsqslkekf 157
Cdd:PRK12829   88 DVLVNNAGIAgptGGIDEITP--EQWEQTLAVNLNGQFYFARAAVPLLKASGHggvIIALSSVAG--------------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 158 rsediteeelvelmenfvedakkgvhtQKGWPNWA-YGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKT---- 232
Cdd:PRK12829  151 ---------------------------RLGYPGRTpYAASKWAVVGLVKSLAIEL----GPLGIRVNAILPGIVRGprmr 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1993940993 233 -DMAGPHATKTPDEGAITPVYLA------LLSEEDIEPHGQFVC 269
Cdd:PRK12829  200 rVIEARAQQLGIGLDEMEQEYLEkislgrMVEPEDIAATALFLA 243
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 5-234 5.06e-21

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 89.03  E-value: 5.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK12937    6 KVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRID 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAF--KVADTT--PFgnqaEETLRTNFFATRDICRELLPIIKPSGRVVNIASIAGSMAlrqcsqslkekfrse 160
Cdd:PRK12937   86 VLVNNAGVMPlgTIADFDleDF----DRTIATNLRGAFVVLREAARHLGQGGRIINLSTSVIALP--------------- 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993 161 diteeelvelmenfvedakkgvhtqkgWPNW-AYGVSKIGVIVLSRIQAKELshkRGQSkILLNSCCPGWVKTDM 234
Cdd:PRK12937  147 ---------------------------LPGYgPYAASKAAVEGLVHVLANEL---RGRG-ITVNAVAPGPVATEL 190
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 5-243 5.07e-21

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


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 88.87  E-value: 5.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHV--YLTARDEGRgmAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:cd05362     4 KVALVTGASRGIGRAIAKRLARDGASVVvnYASSKAAAE--EVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIAFK--VADTTP--FGNQAEETLRTNFFAtrdiCRELLPIIKPSGRVVNIASIAGSMALrqcsqslkekfr 158
Cdd:cd05362    82 VDILVNNAGVMLKkpIAETSEeeFDRMFTVNTKGAFFV----LQEAAKRLRDGGRIINISSSLTAAYT------------ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmenfvedakkgvhtqkgwPNW-AYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDMAgp 237
Cdd:cd05362   146 ------------------------------PNYgAYAGSKAAVEAFTRVLAKELGGR----GITVNAVAPGPVDTDMF-- 189


                  ....*.
gi 1993940993 238 HATKTP 243
Cdd:cd05362   190 YAGKTE 195
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 5-232 1.09e-20

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 88.40  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK12429    5 KVALVTGAASGIGLEIALALAKEGA-KVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFkVADTTPFGNQAEET-----LRTNFFATRDIcrelLPIIKPS--GRVVNIASIAGSMAlrqcsqslkekf 157
Cdd:PRK12429   84 ILVNNAGIQH-VAPIEDFPTEKWKKmiaimLDGAFLTTKAA----LPIMKAQggGRIINMASVHGLVG------------ 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993 158 rsediteeelvelmenFVEDAkkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKElshkRGQSKILLNSCCPGWVKT 232
Cdd:PRK12429  147 ----------------SAGKA-------------AYVSAKHGLIGLTKVVALE----GATHGVTVNAICPGYVDT 188
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-234 1.37e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 91.06  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06484    6 RVVLVTGAAGGIG----RAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAI----AFKVADTTPfgNQAEETLRTNFFATRDICRELLPII---KPSGRVVNIASIAGSMALrqcsqslkekf 157
Cdd:PRK06484   82 VLVNNAGVtdptMTATLDTTL--EEFARLQAINLTGAYLVAREALRLMieqGHGAAIVNVASGAGLVAL----------- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993 158 rsediteeelvelmenfvedAKKGvhtqkgwpnwAYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDM 234
Cdd:PRK06484  149 --------------------PKRT----------AYSASKAAVISLTRSLACEWAAK----GIRVNAVLPGYVRTQM 191
PRK06914 PRK06914
SDR family oxidoreductase;
4-171 1.89e-20

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 88.16  E-value: 1.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRqfAGH-VYLTARD-EGRGMAAVQTLQNEGLDP-HFHQLDITDLSSIRRIRDFMRdKY 80
Cdd:PRK06914    3 KKIAIVTGASSGFGLLTTLELAK--KGYlVIATMRNpEKQENLLSQATQLNLQQNiKVQQLDVTDQNSIHNFQLVLK-EI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  81 GGVDVLVNNAAIAfkvadttpFGNQAEE----TLR----TNFFATRDICRELLPIIKP--SGRVVNIASIAGSMALRQCS 150
Cdd:PRK06914   80 GRIDLLVNNAGYA--------NGGFVEEipveEYRkqfeTNVFGAISVTQAVLPYMRKqkSGKIINISSISGRVGFPGLS 151

                         170       180
                  ....*....|....*....|.
gi 1993940993 151 QSLKEKFRSEDITEEELVELM 171
Cdd:PRK06914  152 PYVSSKYALEGFSESLRLELK 172
PRK09242 PRK09242
SDR family oxidoreductase;
5-142 2.29e-20

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 87.50  E-value: 2.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRqFAGHVYLTARDEgrgmAAVQTLQNE------GLDPHFHQLDITDLSSIRRIRDFMRD 78
Cdd:PRK09242   10 QTALITGASKGIGLAIAREFLG-LGADVLIVARDA----DALAQARDElaeefpEREVHGLAADVSDDEDRRAILDWVED 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  79 KYGGVDVLVNNAA--IAFKVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPSG--RVVNIASIAG 142
Cdd:PRK09242   85 HWDGLHILVNNAGgnIRKAAIDYTE--DEWRGIFETNLFSAFELSRYAHPLLKQHAssAIVNIGSVSG 150
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-235 2.33e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 87.69  E-value: 2.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08213   13 KTALVTGGSRGLGLQIAEALGEAGA-RVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAfkvadttpFGNQAEE------------TLRTNFFATRDICRELLpIIKPSGRVVNIASIAGsmalrqcsqs 152
Cdd:PRK08213   92 ILVNNAGAT--------WGAPAEDhpveawdkvmnlNVRGLFLLSQAVAKRSM-IPRGYGRIINVASVAG---------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 153 LKekfrsediteEELVELMENFvedakkgvhtqkgwpnwAYGVSKIGVIVLSRiqakELSHKRGQSKILLNSCCPGWVKT 232
Cdd:PRK08213  153 LG----------GNPPEVMDTI-----------------AYNTSKGAVINFTR----ALAAEWGPHGIRVNAIAPGFFPT 201


                  ...
gi 1993940993 233 DMA 235
Cdd:PRK08213  202 KMT 204
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 5-147 4.68e-20

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: 86.73  E-value: 4.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCrQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGG-V 83
Cdd:cd05329     7 KTALVTGGTKGIGYAIVEELA-GLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGGkL 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  84 DVLVNNAA--IAFKVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPSGR--VVNIASIAGSMALR 147
Cdd:cd05329    86 NILVNNAGtnIRKEAKDYTE--EDYSLIMSTNFEAAYHLSRLAHPLLKASGNgnIVFISSVAGVIAVP 151
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 5-234 1.25e-19

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 85.51  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05366     3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSFD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIafkvADTTPFGNQAEETLRT----NFFATRDICRELLPIIKP---SGRVVNIASIAGsmalrqcsqslkekf 157
Cdd:cd05366    83 VMVNNAGI----APITPLLTITEEDLKKvyavNVFGVLFGIQAAARQFKKlghGGKIINASSIAG--------------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993 158 rsediteeelvelmenfvedakkgvhtQKGWPNW-AYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDM 234
Cdd:cd05366   144 ---------------------------VQGFPNLgAYSASKFAVRGLTQTAAQELAPK----GITVNAYAPGIVKTEM 190
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-245 1.44e-19

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 85.22  E-value: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEgrgmAAVQTLQNEGLDphFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06463    8 KVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAE----NEAKELREKGVF--TIKCDVGNRDQVKKSKEVVEKEFGRVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFkvadTTPFGNQAEE----TLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGsmalrqcsqslkekfr 158
Cdd:PRK06463   82 VLVNNAGIMY----LMPFEEFDEEkynkMIKINLNGAIYTTYEFLPLLKLSknGAIVNIASNAG---------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmenfVEDAKKGVHTqkgwpnwaYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAgpH 238
Cdd:PRK06463  142 ----------------IGTAAEGTTF--------YAITKAGIIILTRRLAFEL----GKYGIRVNAVAPGWVETDMT--L 191


                  ....*..
gi 1993940993 239 ATKTPDE 245
Cdd:PRK06463  192 SGKSQEE 198
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 5-146 1.49e-19

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: 85.33  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEG-LDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd05332     4 KVVIITGASSGIGEELAYHLARLGA-RLVLSARREERLEEVKSECLELGaPSPHVVPLDMSDLEDAEQVVEEALKLFGGL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  84 DVLVNNAAIAFKvadtTPFGNQAEETLR----TNFFATRDICRELLP--IIKPSGRVVNIASIAGSMAL 146
Cdd:cd05332    83 DILINNAGISMR----SLFHDTSIDVDRkimeVNYFGPVALTKAALPhlIERSQGSIVVVSSIAGKIGV 147
PRK06124 PRK06124
SDR family oxidoreductase;
5-254 1.51e-19

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 85.15  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06124   12 QVALVTGSARGLGFEIARALAGAGA-HVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFK--VADTTPfgNQAEETLRTNFFATRDICRELLPIIKP--SGRVVNIASIAGSMAlrqcsqslkekfRSE 160
Cdd:PRK06124   91 ILVNNVGARDRrpLAELDD--AAIRALLETDLVAPILLSRLAAQRMKRqgYGRIIAITSIAGQVA------------RAG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 161 DIteeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTD----MA- 235
Cdd:PRK06124  157 DA-----------------------------VYPAAKQGLTGLMRALAAEF----GPHGITSNAIAPGYFATEtnaaMAa 203

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1993940993 236 ----GPHATK--------TPDEGAITPVYLA 254
Cdd:PRK06124  204 dpavGPWLAQrtplgrwgRPEEIAGAAVFLA 234
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 9-140 5.13e-19

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 83.67  E-value: 5.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   9 VTGANKGIGLAIVRALcrQFAG-HVYLTARDEGRGMAAVQtlQNEGLdpHFHQLDITDLSSIRRIRDFMRDKYGGVDVLV 87
Cdd:COG3967    10 ITGGTSGIGLALAKRL--HARGnTVIITGRREEKLEEAAA--ANPGL--HTIVLDVADPASIAALAEQVTAEFPDLNVLI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993  88 NNAAI--AFKVADTTPFGNQAEETLRTNFFATRDICRELLPIIK--PSGRVVNIASI 140
Cdd:COG3967    84 NNAGImrAEDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKaqPEAAIVNVSSG 140
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
4-236 6.33e-19

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 83.28  E-value: 6.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQfAGHVYLTarDEGRGMAAVQTLQNEGLDP---HFHQLDITDLSSIRRIRDFMRDKY 80
Cdd:PRK12824    2 KKIALVTGAKRGIGSAIARELLND-GYRVIAT--YFSGNDCAKDWFEEYGFTEdqvRLKELDVTDTEECAEALAEIEEEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  81 GGVDVLVNNAAI----AFKvaDTTPfgNQAEETLRTNFFATRDICRELLPII--KPSGRVVNIASIAGsmalrqcsqslk 154
Cdd:PRK12824   79 GPVDILVNNAGItrdsVFK--RMSH--QEWNDVINTNLNSVFNVTQPLFAAMceQGYGRIINISSVNG------------ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 155 ekfrsediteeelvelmenfvedaKKGvhtQKGWPNwaYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDM 234
Cdd:PRK12824  143 ------------------------LKG---QFGQTN--YSAAKAGMIGFTKALASEG----ARYGITVNCIAPGYIATPM 189


                  ..
gi 1993940993 235 AG 236
Cdd:PRK12824  190 VE 191
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 4-141 7.55e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 83.52  E-value: 7.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK06198    6 GKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRL 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993  84 DVLVNNAAIAFK--VADTTP--FGNQAEETLRTNFF----ATRDICRELLPiikpsGRVVNIASIA 141
Cdd:PRK06198   86 DALVNAAGLTDRgtILDTSPelFDRHFAVNVRAPFFlmqeAIKLMRRRKAE-----GTIVNIGSMS 146
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-235 8.25e-19

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 82.81  E-value: 8.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07666    8 KNALITGAGRGIGRAVAIALAKE-GVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGSID 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIA-F-KVADTTPfgNQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASIAGsmalrqcsqslkekfrse 160
Cdd:PRK07666   87 ILINNAGISkFgKFLELDP--AEWEKIIQVNLMGVYYATRAVLPsmIERQSGDIINISSTAG------------------ 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993 161 diteeelvelmenfvedakkgvhtQKGWPNW-AYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDMA 235
Cdd:PRK07666  147 ------------------------QKGAAVTsAYSASKFGVLGLTESLMQEVR----KHNIRVTALTPSTVATDMA 194
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-145 5.03e-18

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 81.16  E-value: 5.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQ-FAghVYLTA-RDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK12745    2 RPVALVTGGRRGIGLGIARALAAAgFD--LAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993  82 GVDVLVNNAAIAFKVA----DTTP--FGNQAEETLRTNFFATRDICRELL----PIIKPSGRVVNIASIAGSMA 145
Cdd:PRK12745   80 RIDCLVNNAGVGVKVRgdllDLTPesFDRVLAINLRGPFFLTQAVAKRMLaqpePEELPHRSIVFVSSVNAIMV 153
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 5-172 5.55e-18

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: 80.24  E-value: 5.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGhVYLTARDEGRGMAAVQTLQnegldPHFHQL--DITDLSSIRRIRDFMRDKYGG 82
Cdd:cd08929     1 KAALVTGASRGIGEATARLLHAEGYR-VGICARDEARLAAAAAQEL-----EGVLGLagDVRDEADVRRAVDAMEEAFGG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIAF--KVADTTPfgnqaEE---TLRTNFFATRDICRELLPIIKPSGR--VVNIASIAGSMALRQCSQSLKE 155
Cdd:cd08929    75 LDALVNNAGVGVmkPVEELTP-----EEwrlVLDTNLTGAFYCIHKAAPALLRRGGgtIVNVGSLAGKNAFKGGAAYNAS 149

                         170
                  ....*....|....*..
gi 1993940993 156 KFRSEDITEEELVELME 172
Cdd:cd08929   150 KFGLLGLSEAAMLDLRE 166
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 5-144 5.93e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 81.61  E-value: 5.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQ--TLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:PRK06197   17 RVAVVTGANTGLGYETAAALAAKGA-HVVLAVRNLDKGKAAAAriTAATPGADVTLQELDLTSLASVRAAADALRAAYPR 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993  83 VDVLVNNAAIAFKVADTTPFGnqAEETLRTN----FFATRDICRELLPIikPSGRVVNIASIAGSM 144
Cdd:PRK06197   96 IDLLINNAGVMYTPKQTTADG--FELQFGTNhlghFALTGLLLDRLLPV--PGSRVVTVSSGGHRI 157
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 1-142 7.36e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 80.72  E-value: 7.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   1 MSCPKVAMVTGANKGIGLAIVRALCRqfAGH-VYLTARDEGR--GMAAVQTLqnegldphfhQLDITDLSSIRRIRDFMR 77
Cdd:PRK06179    1 MSNSKVALVTGASSGIGRATAEKLAR--AGYrVFGTSRNPARaaPIPGVELL----------ELDVTDDASVQAAVDEVI 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  78 DKYGGVDVLVNNAAIAF--KVADTTPFgnQAEETLRTNFFATRDICRELLPIIKP--SGRVVNIASIAG 142
Cdd:PRK06179   69 ARAGRIDVLVNNAGVGLagAAEESSIA--QAQALFDTNVFGILRMTRAVLPHMRAqgSGRIINISSVLG 135
PRK07454 PRK07454
SDR family oxidoreductase;
4-268 7.77e-18

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 80.39  E-value: 7.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRqfAG-HVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIR-RIRDFMrDKYG 81
Cdd:PRK07454    6 MPRALITGASSGIGKATALAFAK--AGwDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIApGIAELL-EQFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIAFKVA-DTTPFGnQAEETLRTNFFATRDICRELLPII--KPSGRVVNIASIAGSMAlrqcsqslkekfr 158
Cdd:PRK07454   83 CPDVLINNAGMAYTGPlLEMPLS-DWQWVIQLNLTSVFQCCSAVLPGMraRGGGLIINVSSIAARNA------------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmenfvedakkgvhtqkgWPNW-AYGVSKIGVIVLSRIQAKElshKRGQSkILLNSCCPGWVKT----- 232
Cdd:PRK07454  149 -----------------------------FPQWgAYCVSKAALAAFTKCLAEE---ERSHG-IRVCTITLGAVNTplwdt 195

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1993940993 233 DMAGPH----ATKTPDEGAITPVYLALLseediePHGQFV 268
Cdd:PRK07454  196 ETVQADfdrsAMLSPEQVAQTILHLAQL------PPSAVI 229
PRK06181 PRK06181
SDR family oxidoreductase;
5-142 1.06e-17

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 80.41  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAG---HVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK06181    2 KVVIITGASEGIG----RALAVRLARagaQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993  82 GVDVLVNNAAI----AF-KVADTTPFgnqaEETLRTNFFATRDICRELLPIIKPS-GRVVNIASIAG 142
Cdd:PRK06181   78 GIDILVNNAGItmwsRFdELTDLSVF----ERVMRVNYLGAVYCTHAALPHLKASrGQIVVVSSLAG 140
PRK06949 PRK06949
SDR family oxidoreductase;
5-238 1.48e-17

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 79.81  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGhVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06949   10 KVALVTGASSGLGARFAQVLAQAGAK-VVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGTID 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAF--KVADTTP--FGNQAEETLRTNFFATRDICRELL------PIIKPSGRVVNIASIAGsmaLRqcsqslk 154
Cdd:PRK06949   89 ILVNNSGVSTtqKLVDVTPadFDFVFDTNTRGAFFVAQEVAKRMIarakgaGNTKPGGRIINIASVAG---LR------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 155 ekfrsediteeelvelmenfvedakkgVHTQKGwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDM 234
Cdd:PRK06949  159 ---------------------------VLPQIG----LYCMSKAAVVHMTRAMALEW----GRHGINVNAICPGYIDTEI 203


                  ....
gi 1993940993 235 AGPH 238
Cdd:PRK06949  204 NHHH 207
PRK07201 PRK07201
SDR family oxidoreductase;
5-141 2.07e-17

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 81.92  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07201  372 KVVLITGASSGIGRATAIKVAEA-GATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVD 450

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  85 VLVNNA--AIAFKVADTTPFGNQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASIA 141
Cdd:PRK07201  451 YLVNNAgrSIRRSVENSTDRFHDYERTMAVNYFGAVRLILGLLPhmRERRFGHVVNVSSIG 511
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 6-237 2.70e-17

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


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 79.04  E-value: 2.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   6 VAMVTGANKGIGLAIVRALCRqfAGHVYLTA--RDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd05337     3 VAIVTGASRGIGRAIATELAA--RGFDIAINdlPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAFKVA----DTTP--FGNQAEETLRTNFFATRDICRELL----PIIKPSGRVVNIASIAGSMALrqcsqsl 153
Cdd:cd05337    81 DCLVNNAGIAVRPRgdllDLTEdsFDRLIAINLRGPFFLTQAVARRMVeqpdRFDGPHRSIIFVTSINAYLVS------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 154 kekfrsediteeelvelmenfvedakkgvhtqkgwPNWA-YGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKT 232
Cdd:cd05337   154 -----------------------------------PNRGeYCISKAGLSMATRLLAYRL----ADEGIAVHEIRPGLIHT 194


                  ....*
gi 1993940993 233 DMAGP 237
Cdd:cd05337   195 DMTAP 199
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 5-146 4.48e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 78.83  E-value: 4.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGrgmAAVQTLQNEGLDpHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07825    6 KVVAITGGARGIGLATARALAALGA-RVAIGDLDEA---LAKETAAELGLV-VGGPLDVTDPASFAAFLDAVEADLGPID 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993  85 VLVNNAAiafkVADTTPFGNQAEETLRTNFfatrDI--------CRELLPIIKPSGR--VVNIASIAGSMAL 146
Cdd:PRK07825   81 VLVNNAG----VMPVGPFLDEPDAVTRRIL----DVnvygvilgSKLAAPRMVPRGRghVVNVASLAGKIPV 144
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 5-145 5.06e-17

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: 78.09  E-value: 5.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRgmaaVQTLQNEgLDPHFH------QLDITDLSSIRRIRDFMRD 78
Cdd:cd05346     1 KTVLITGASSGIGEATARRFAKA-GAKLILTGRRAER----LQELADE-LGAKFPvkvlplQLDVSDRESIEAALENLPE 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993940993  79 KYGGVDVLVNNAAIAfkvADTTPFGNQAEE----TLRTNFFATRDICRELLPII--KPSGRVVNIASIAGSMA 145
Cdd:cd05346    75 EFRDIDILVNNAGLA---LGLDPAQEADLEdwetMIDTNVKGLLNVTRLILPIMiaRNQGHIINLGSIAGRYP 144
PRK08219 PRK08219
SDR family oxidoreductase;
5-142 8.05e-17

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 77.28  E-value: 8.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFagHVYLTARDEGRGMAAVQTLQNEgldpHFHQLDITDLSSIRRirdfMRDKYGGVD 84
Cdd:PRK08219    4 PTALITGASRGIGAAIARELAPTH--TLLLGGRPAERLDELAAELPGA----TPFPVDLTDPEAIAA----AVEQLGRLD 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  85 VLVNNAAIAF--KVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPS-GRVVNIASIAG 142
Cdd:PRK08219   74 VLVHNAGVADlgPVAESTV--DEWRATLEVNVVAPAELTRLLLPALRAAhGHVVFINSGAG 132
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 5-234 1.15e-16

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: 77.15  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMAAVQTLQNEGLDPhfhQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd08944     4 KVAIVTGAGAGIGAACAARLARE-GARVVVADIDGGAAQAVVAQIAGGALAL---RVDVTDEQQVAALFERAVEEFGGLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAF---KVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGsmalrqcsqslkekfrs 159
Cdd:cd08944    80 LLVNNAGAMHltpAIIDTDL--AVWDQTMAINLRGTFLCCRHAAPRMIARggGSIVNLSSIAG----------------- 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993 160 editeeelvelmenfvedakkgvhtQKGWPNW-AYGVSKIGVIVLSRIQAKELSHkrgqSKILLNSCCPGWVKTDM 234
Cdd:cd08944   141 -------------------------QSGDPGYgAYGASKAAIRNLTRTLAAELRH----AGIRCNALAPGLIDTPL 187
PRK09072 PRK09072
SDR family oxidoreductase;
10-153 1.50e-16

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 77.29  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  10 TGANKGIGLAIVRALCRQFAgHVYLTARDEGRgmaaVQTLQNEGLDPHFHQL---DITDLSSIRRIRDFMRdKYGGVDVL 86
Cdd:PRK09072   11 TGASGGIGQALAEALAAAGA-RLLLVGRNAEK----LEALAARLPYPGRHRWvvaDLTSEAGREAVLARAR-EMGGINVL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  87 VNNAAiafkvadTTPFG-------NQAEETLRTNFFATRDICRELLPIIK--PSGRVVNIASIAGSM------------- 144
Cdd:PRK09072   85 INNAG-------VNHFAlledqdpEAIERLLALNLTAPMQLTRALLPLLRaqPSAMVVNVGSTFGSIgypgyasycaskf 157


                  ....*....
gi 1993940993 145 ALRQCSQSL 153
Cdd:PRK09072  158 ALRGFSEAL 166
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
5-139 1.74e-16

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 79.12  E-value: 1.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGlDPHFHQLDITDLSSIRR-IRDFMRDkYGGV 83
Cdd:PRK08324  423 KVALVTGAAGGIGKATAKRLAAEGA-CVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAAVQAaFEEAALA-FGGV 499

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993940993  84 DVLVNNAAIAFkvadTTPFGNQAEETLRT----NFFATRDICRELLPIIKPS---GRVVNIAS 139
Cdd:PRK08324  500 DIVVSNAGIAI----SGPIEETSDEDWRRsfdvNATGHFLVAREAVRIMKAQglgGSIVFIAS 558
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
5-249 2.11e-16

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 76.76  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAavQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08226    7 KTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLA--DELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRID 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAiafkVADTTPFGNQAEET----LRTNFFATRDICRELLP--IIKPSGRVVNIASIAGSMalrqcsqslkekfr 158
Cdd:PRK08226   85 ILVNNAG----VCRLGSFLDMSDEDrdfhIDINIKGVWNVTKAVLPemIARKDGRIVMMSSVTGDM-------------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmenfVEDAKKGvhtqkgwpnwAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDMAGPH 238
Cdd:PRK08226  147 ----------------VADPGET----------AYALTKAAIVGLTKSLAVEYA----QSGIRVNAICPGYVRTPMAESI 196

                         250
                  ....*....|....
gi 1993940993 239 ATKT-PD--EGAIT 249
Cdd:PRK08226  197 ARQSnPEdpESVLT 210
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 5-147 3.01e-16

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: 76.04  E-value: 3.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGhVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd08934     4 KVALVTGASSGIGEATARALAAEGAA-VAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  85 VLVNNAAI----AFKVADTTPFgnqaEETLRTNFFATRDICRELLPIIKP--SGRVVNIASIAGSMALR 147
Cdd:cd08934    83 ILVNNAGImllgPVEDADTTDW----TRMIDTNLLGLMYTTHAALPHHLLrnKGTIVNISSVAGRVAVR 147
PRK07063 PRK07063
SDR family oxidoreductase;
5-259 3.31e-16

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 76.24  E-value: 3.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGhVYLTARDEGRGMAAVQTLQNE--GLDPHFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:PRK07063    8 KVALVTGAAQGIGAAIARAFAREGAA-VALADLDAALAERAAAAIARDvaGARVLAVPADVTDAASVAAAVAAAEEAFGP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAI-AFKVADTTPfgnqaEETLRTNFFATRD----ICRELLP--IIKPSGRVVNIASiagsmalrqcsqslke 155
Cdd:PRK07063   87 LDVLVNNAGInVFADPLAMT-----DEDWRRCFAVDLDgawnGCRAVLPgmVERGRGSIVNIAS---------------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 156 kfrsediteeelvelmenfvedakkgVHTQKGWPN-WAYGVSKIGVIVLSRIQAKELShKRGqskILLNSCCPGWVKTDM 234
Cdd:PRK07063  146 --------------------------THAFKIIPGcFPYPVAKHGLLGLTRALGIEYA-ARN---VRVNAIAPGYIETQL 195

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1993940993 235 A--------GPHATK-------------TPDEGAITPVYLAllSEE 259
Cdd:PRK07063  196 TedwwnaqpDPAAARaetlalqpmkrigRPEEVAMTAVFLA--SDE 239
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 5-145 4.63e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 75.57  E-value: 4.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALcRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07523   11 RRALVTGSSQGIGYALAEGL-AQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPID 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  85 VLVNNAAIAFKvadtTP---FGNQA-EETLRTN----FFATRDICRELlpIIKPSGRVVNIASIAGSMA 145
Cdd:PRK07523   90 ILVNNAGMQFR----TPledFPADAfERLLRTNissvFYVGQAVARHM--IARGAGKIINIASVQSALA 152
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-244 5.19e-16

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: 75.50  E-value: 5.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHV--YLTARDEGRgmAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:cd05358     4 KVALVTGASSGIGKAIAIRLATAGANVVvnYRSKEDAAE--EVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAI--AFKVADTTPfgNQAEETLRTN----FFATRDICRELLPiIKPSGRVVNIASiagsmalrqcsqslkek 156
Cdd:cd05358    82 LDILVNNAGLqgDASSHEMTL--EDWNKVIDVNltgqFLCAREAIKRFRK-SKIKGKIINMSS----------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 157 frsediteeelvelmenfvedakkgVHTQKGWP-NWAYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDMA 235
Cdd:cd05358   142 -------------------------VHEKIPWPgHVNYAASKGGVKMMTKTLAQEYAPK----GIRVNAIAPGAINTPIN 192


                  ....*....
gi 1993940993 236 GPhATKTPD 244
Cdd:cd05358   193 AE-AWDDPE 200
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 5-229 6.78e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 75.43  E-value: 6.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALcRQFAGHVYLTARDEGRGMAAVQTLqneGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08265    7 KVAIVTGGATLIGAAVARAL-VAAGARVAIVDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVARFGRVD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIafkvadttpFGNQAEETLRTNFFATRDI-----------CRELLPiiKPSGRVVNIASIAGSMAlrqcsqsl 153
Cdd:PRK08265   83 ILVNLACT---------YLDDGLASSRADWLAALDVnlvsaamlaqaAHPHLA--RGGGAIVNFTSISAKFA-------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993 154 kekfrsediteeelvelmenfvedakkgvhtQKGwpNWAYGVSKIGVIVLSRIQAKELSHKRgqskILLNSCCPGW 229
Cdd:PRK08265  144 -------------------------------QTG--RWLYPASKAAIRQLTRSMAMDLAPDG----IRVNSVSPGW 182
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 5-233 1.39e-15

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: 74.37  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLD---PHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:cd05364     4 KVAIITGSSSGIGAGTAILFARLGA-RLALTGRDAERLEETRQSCLQAGVSekkILLVVADLTEEEGQDRIISTTLAKFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIAFKVADTTPFGNQAEETLRTNFFATRDICRELLP-IIKPSGRVVNIASIAGSmalRQCSQSLkekfrse 160
Cdd:cd05364    83 RLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPhLIKTKGEIVNVSSVAGG---RSFPGVL------- 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993940993 161 diteeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTD 233
Cdd:cd05364   153 -------------------------------YYCISKAALDQFTRCTALEL----APKGVRVNSVSPGVIVTG 190
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 5-142 1.75e-15

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: 73.83  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDP----HFHQLDITDLSSIRRIRDFMRDKY 80
Cdd:cd08939     2 KHVLITGGSSGIGKALAKELVKEGA-NVIIVARSESKLEEAVEEIEAEANASgqkvSYISADLSDYEEVEQAFAQAVEKG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993  81 GGVDVLVNNA--AIAFKVADTTPfgNQAEETLRTNFFATRDICRELLPIIK--PSGRVVNIASIAG 142
Cdd:cd08939    81 GPPDLVVNCAgiSIPGLFEDLTA--EEFERGMDVNYFGSLNVAHAVLPLMKeqRPGHIVFVSSQAA 144
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 6-150 1.83e-15

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 73.86  E-value: 1.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   6 VAMVTGANKGIGLAIVRALCRQFAGH-VYLTARDEgrgmAAVQTLQNE---GLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSPSvVVLLARSE----EPLQELKEElrpGLRVTTVKADLSDAAGVEQLLEAIRKLDG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993  82 GVDVLVNNAAIAF---KVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPSG---RVVNIASIAGSMALRQCS 150
Cdd:cd05367    77 ERDLLINNAGSLGpvsKIEFIDL--DELQKYFDLNLTSPVCLTSTLLRAFKKRGlkkTVVNVSSGAAVNPFKGWG 149
PRK06138 PRK06138
SDR family oxidoreductase;
5-254 2.18e-15

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 73.65  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDeGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06138    6 RVAIVTGAGSGIGRATAKLFAREGA-RVVVADRD-AEAAERVAAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWGRLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNA--AIAFKVADTTPfgNQAEETLRTNFFATRDICRELLPIIKP--SGRVVNIASIAGSMALRQcsqslkekfrse 160
Cdd:PRK06138   84 VLVNNAgfGCGGTVVTTDE--ADWDAVMRVNVGGVFLWAKYAIPIMQRqgGGSIVNTASQLALAGGRG------------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 161 diteeelvelmenfvedakkgvhtqkgwpNWAYGVSKIGVIVLSRIQAKELSHKRgqskILLNSCCPGWVKTDM------ 234
Cdd:PRK06138  150 -----------------------------RAAYVASKGAIASLTRAMALDHATDG----IRVNAVAPGTIDTPYfrrifa 196

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1993940993 235 --AGPHATK-------------TPDEGAITPVYLA 254
Cdd:PRK06138  197 rhADPEALRealrarhpmnrfgTAEEVAQAALFLA 231
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 5-148 2.33e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 73.54  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDphfHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06841   16 KVAVVTGGASGIGHAIAELFAAKGA-RVALLDRSEDVAEVAAQLLGGNAKG---LVCDVSDSQSVEAAVAAVISAFGRID 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  85 VLVNNAAIAFkVADTTPFGNQA-EETLRTN----FFATRDICRELLPiiKPSGRVVNIASIAGSMALRQ 148
Cdd:PRK06841   92 ILVNSAGVAL-LAPAEDVSEEDwDKTIDINlkgsFLMAQAVGRHMIA--AGGGKIVNLASQAGVVALER 157
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 5-232 2.78e-15

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: 73.38  E-value: 2.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIvralCRQFAGH---VYLTARDEGRGmaaVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:cd09761     2 KVAIVTGGGHGIGKQI----CLDFLEAgdkVVFADIDEERG---ADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIAFKVADTTPFGNQAEETLRTNFFATRDICRELLP-IIKPSGRVVNIASiagsmalrqcsqslKEKFRSE 160
Cdd:cd09761    75 RIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDeLIKNKGRIINIAS--------------TRAFQSE 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993 161 DITEeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELShkrgqSKILLNSCCPGWVKT 232
Cdd:cd09761   141 PDSE---------------------------AYAASKGGLVALTHALAMSLG-----PDIRVNCISPGWINT 180
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 5-264 3.44e-15

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: 73.65  E-value: 3.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMAAVQTLQNEGLDPHF--HQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:cd09807     2 KTVIITGANTGIGKETARELARR-GARVIMACRDMAKCEEAAAEIRRDTLNHEVivRHLDLASLKSIRAFAAEFLAEEDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIA----FKVAD--TTPFG-NQAEETLRTNFFAtrdicrELLPIIKPSgRVVNIASIAgsmalrqcsqslke 155
Cdd:cd09807    81 LDVLINNAGVMrcpySKTEDgfEMQFGvNHLGHFLLTNLLL------DLLKKSAPS-RIVNVSSLA-------------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 156 kFRSEDITEEELvelmeNFVEDAKKGVhtqkgwpnwAYGVSKIGVIVLSRiqakELSHKRGQSKILLNSCCPGWVKTDM- 234
Cdd:cd09807   140 -HKAGKINFDDL-----NSEKSYNTGF---------AYCQSKLANVLFTR----ELARRLQGTGVTVNALHPGVVRTELg 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1993940993 235 --AGPHAT--------------KTPDEGAITPVYLALlsEEDIEPH 264
Cdd:cd09807   201 rhTGIHHLflstllnplfwpfvKTPREGAQTSIYLAL--AEELEGV 244
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 6-254 3.67e-15

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: 73.05  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   6 VAMVTGANKGIGlaivRALCRQFAGH---VYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:cd05339     1 IVLITGGGSGIG----RLLALEFAKRgakVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIA--FKVADTTPFgnQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASIAGSMALrqcsqslkekfr 158
Cdd:cd05339    77 VTILINNAGVVsgKKLLELPDE--EIEKTFEVNTLAHFWTTKAFLPdmLERNHGHIVTIASVAGLISP------------ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmeNFVEDakkgvhtqkgwpnwaYGVSKIGVIVLSRIQAKELshKRGQSKILLNSC-CPGWVKTDM-AG 236
Cdd:cd05339   143 --------------AGLAD---------------YCASKAAAVGFHESLRLEL--KAYGKPGIKTTLvCPYFINTGMfQG 191

                         250
                  ....*....|....*...
gi 1993940993 237 PHATKTPDEGAITPVYLA 254
Cdd:cd05339   192 VKTPRPLLAPILEPEYVA 209
PRK06182 PRK06182
short chain dehydrogenase; Validated
 4-145 3.79e-15

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 73.46  E-value: 3.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQfaGH-VYLTARDEGRgmaaVQTLQNEGLDPHfhQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:PRK06182    3 KKVALVTGASSGIGKATARRLAAQ--GYtVYGAARRVDK----MEDLASLGVHPL--SLDVTDEASIKAAVDTIIAEEGR 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993  83 VDVLVNNAAiafkvadttpFG----------NQAEETLRTNFFATRDICRELLPII--KPSGRVVNIASIAGSMA 145
Cdd:PRK06182   75 IDVLVNNAG----------YGsygaiedvpiDEARRQFEVNLFGAARLTQLVLPHMraQRSGRIINISSMGGKIY 139
PRK05693 PRK05693
SDR family oxidoreductase;
5-144 3.83e-15

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 73.29  E-value: 3.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQF--AGH-VYLTARDEgrgmAAVQTLQNEGLDPHfhQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK05693    2 PVVLITGCSSGIG----RALADAFkaAGYeVWATARKA----EDVEALAAAGFTAV--QLDVNDGAALARLAEELEAEHG 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  82 GVDVLVNNAAiafkVADTTPFGNQAEETLR----TNFFATRDICRELLPIIKPS-GRVVNIASIAGSM 144
Cdd:PRK05693   72 GLDVLINNAG----YGAMGPLLDGGVEAMRrqfeTNVFAVVGVTRALFPLLRRSrGLVVNIGSVSGVL 135
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 5-162 4.01e-15

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: 72.81  E-value: 4.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMA------------AVQTLQNEGLDPHFHQLDITDLSSIRRI 72
Cdd:cd05338     4 KVAFVTGASRGIGRAIALRLAKAGA-TVVVAAKTASEGDNgsakslpgtieeTAEEIEAAGGQALPIVVDVRDEDQVRAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  73 RDFMRDKYGGVDVLVNNAAIAF--KVADTTP--FGNQAEETLRTNFFATRDICRELLPiiKPSGRVVNIAS--------- 139
Cdd:cd05338    83 VEATVDQFGRLDILVNNAGAIWlsLVEDTPAkrFDLMQRVNLRGTYLLSQAALPHMVK--AGQGHILNISPplslrparg 160

                         170       180
                  ....*....|....*....|....*..
gi 1993940993 140 ----IAGSMALRQCSQSLKEKFRSEDI 162
Cdd:cd05338   161 dvayAAGKAGMSRLTLGLAAELRRHGI 187
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 5-242 4.20e-15

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: 72.75  E-value: 4.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRR-IRDFMRDkYGGV 83
Cdd:cd05352     9 KVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKtFKQIQKD-FGKI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAF-KVADTTPFgNQAEETLRTNFFATRDICRELLPIIKPSGR--VVNIASIAGSMALRQCSQSlkekfrse 160
Cdd:cd05352    88 DILIANAGITVhKPALDYTY-EQWNKVIDVNLNGVFNCAQAAAKIFKKQGKgsLIITASMSGTIVNRPQPQA-------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 161 diteeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDMAGPHAT 240
Cdd:cd05352   159 -------------------------------AYNASKAAVIHLAKSLAVEWAKY----FIRVNSISPGYIDTDLTDFVDK 203


                  ..
gi 1993940993 241 KT 242
Cdd:cd05352   204 EL 205
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 5-230 7.89e-15

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 72.30  E-value: 7.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFA---GHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK07890    6 KVVVVSGVGPGLG----RTLAVRAAragADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNaaiAFKVADTTPFGNQAEETLR----TNFFATRDICRELLPIIKPS-GRVVNIasiaGSMALRqcsqslkek 156
Cdd:PRK07890   82 RVDALVNN---AFRVPSMKPLADADFAHWRavieLNVLGTLRLTQAFTPALAESgGSIVMI----NSMVLR--------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993 157 frsediteeelvelmenfvedakkgvHTQKGWPnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWV 230
Cdd:PRK07890  146 --------------------------HSQPKYG--AYKMAKGALLAASQSLATEL----GPQGIRVNSVAPGYI 187
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 5-171 8.56e-15

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: 71.57  E-value: 8.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALcRQFAGHVYLTARDEgrgmAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05370     6 NTVLITGGTSGIGLALARKF-LEAGNTVIITGRRE----ERLAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIA--FKVADTTPFGNQAEETLRTNFFATRDICRELLPIIK--PSGRVVNIASI-------------AGSMALR 147
Cdd:cd05370    81 ILINNAGIQrpIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKkqPEATIVNVSSGlafvpmaanpvycATKAALH 160

                         170       180
                  ....*....|....*....|....
gi 1993940993 148 QCSQSLKEKFRSEDIteeELVELM 171
Cdd:cd05370   161 SYTLALRHQLKDTGV---EVVEIV 181
PRK07074 PRK07074
SDR family oxidoreductase;
5-244 8.95e-15

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 72.11  E-value: 8.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAG---HVYLTARDEGRGMAAVQTLQNEGLDPhfHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK07074    3 RTALVTGAAGGIG----QALARRFLAagdRVLALDIDAAALAAFADALGDARFVP--VACDLTDAASLAAALANAAAERG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNA--AIAFKVADTTPFGNQAEETLrtNFFATRDICRELL-PIIKPS-GRVVNIASIAGSMALrqcsqslkekf 157
Cdd:PRK07074   77 PVDVLVANAgaARAASLHDTTPASWRADNAL--NLEAAYLCVEAVLeGMLKRSrGAVVNIGSVNGMAAL----------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 158 rsediteeelvelmenfvedakkgvhtqkGWPnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGP 237
Cdd:PRK07074  144 -----------------------------GHP--AYSAAKAGLIHYTKLLAVEY----GRFGIRANAVAPGTVKTQAWEA 188


                  ....*..
gi 1993940993 238 HATKTPD 244
Cdd:PRK07074  189 RVAANPQ 195
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 5-250 1.03e-14

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


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 71.72  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGldpHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAGERA---IAIQADVRDRDQVQAMIEEAKNHFGPVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAF-------KVADTTP---FGNQAEETLRtnffATRDICRELLPIIKP--SGRVVNIASiagsmalrqcsqs 152
Cdd:cd05349    78 TIVNNALIDFpfdpdqrKTFDTIDwedYQQQLEGAVK----GALNLLQAVLPDFKErgSGRVINIGT------------- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 153 lkekfrsediteeelvELMENFVEdakkgvhtqkgwPNWAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVK- 231
Cdd:cd05349   141 ----------------NLFQNPVV------------PYHDYTTAKAALLGFTRNMAKEL----GPYGITVNMVSGGLLKv 188

                         250       260
                  ....*....|....*....|....
gi 1993940993 232 TDmagpHATKTPDE-----GAITP 250
Cdd:cd05349   189 TD----ASAATPKEvfdaiAQTTP 208
PRK06484 PRK06484
short chain dehydrogenase; Validated
 4-232 1.41e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 73.34  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRalcrQFAGHVYLTARDEGRGMAAVQTLQNEGlDPHFH-QLDITDLSSIRRIRDFMRDKYGG 82
Cdd:PRK06484  269 PRVVAITGGARGIGRAVAD----RFAAAGDRLLIIDRDAEGAKKLAEALG-DEHLSvQADITDEAAVESAFAQIQARWGR 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIAFKVAdttPFGNQAEETLRT----NFFATRDICRELLPIIKPSGRVVNIASIAGSMALRqcsqslkekfr 158
Cdd:PRK06484  344 LDVLVNNAGIAEVFK---PSLEQSAEDFTRvydvNLSGAFACARAAARLMSQGGVIVNLGSIASLLALP----------- 409

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993 159 sediteeelvelmenfvedakkgvhtqkgwPNWAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKT 232
Cdd:PRK06484  410 ------------------------------PRNAYCASKAAVTMLSRSLACEW----APAGIRVNTVAPGYIET 449
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-142 2.34e-14

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 72.56  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAV-QTLQNEGLdphfhQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK08261  211 KVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAGEALAAVaNRVGGTAL-----ALDITAPDAPARIAEHLAERHGGL 285

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993  84 DVLVNNAAIafkVADTTpFGNQAEET----LRTNFFATRDICRELLP--IIKPSGRVVNIASIAG 142
Cdd:PRK08261  286 DIVVHNAGI---TRDKT-LANMDEARwdsvLAVNLLAPLRITEALLAagALGDGGRIVGVSSISG 346
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-237 2.94e-14

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 70.53  E-value: 2.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFA---GHVYLTARDEGRgmaavQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK06935   16 KVAIVTGGNTGLGQGYAVALAKAGAdiiITTHGTNWDETR-----RLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIAFKvadtTPFGNQAEE--------TLRTNFFATRDICRELLPiiKPSGRVVNIASiagsmalrqcsqsl 153
Cdd:PRK06935   91 KIDILVNNAGTIRR----APLLEYKDEdwnavmdiNLNSVYHLSQAVAKVMAK--QGSGKIINIAS-------------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 154 kekfrsediteeelvelMENFvedakkgvhtQKGWPNWAYGVSKIGVIVLSRIQAKELSHKRGQskilLNSCCPGWVKTD 233
Cdd:PRK06935  151 -----------------MLSF----------QGGKFVPAYTASKHGVAGLTKAFANELAAYNIQ----VNAIAPGYIKTA 199


                  ....
gi 1993940993 234 MAGP 237
Cdd:PRK06935  200 NTAP 203
PRK07774 PRK07774
SDR family oxidoreductase;
5-245 2.94e-14

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 70.54  E-value: 2.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQtLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07774    7 KVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQ-IVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGID 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAI----AFKVADTTPFGNQaEETLRTNFFATRDICRELLPII--KPSGRVVNIASIAGSMAlrqcsqslkekfr 158
Cdd:PRK07774   86 YLVNNAAIyggmKLDLLITVPWDYY-KKFMSVNLDGALVCTRAVYKHMakRGGGAIVNQSSTAAWLY------------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmENFvedakkgvhtqkgwpnwaYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAgph 238
Cdd:PRK07774  152 -------------SNF------------------YGLAKVGLNGLTQQLAREL----GGMNIRVNAIAPGPIDTEAT--- 193


                  ....*..
gi 1993940993 239 ATKTPDE 245
Cdd:PRK07774  194 RTVTPKE 200
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 9-234 3.88e-14

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: 70.22  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   9 VTGANKGIGLAIVRALcrQFAGHVYLtardegrgmaavqtlqneGLD--PHFHQLDITDLSSIRR-IRDFMRDKYGGVDV 85
Cdd:cd05328     4 ITGAASGIGAATAELL--EDAGHTVI------------------GIDlrEADVIADLSTPEGRAAaIADVLARCSGVLDG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  86 LVNNAAiafkVADTTPFGNqaeeTLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGsMALRQcsqslkekfrsediT 163
Cdd:cd05328    64 LVNCAG----VGGTTVAGL----VLKVNYFGLRALMEALLPRLRKGhgPAAVVVSSIAG-AGWAQ--------------D 120

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993 164 EEELVELMENFVEDAKKGVHTQKGWP-NWAYGVSKIGVIVLSRIQAKELSHKRGqskILLNSCCPGWVKTDM 234
Cdd:cd05328   121 KLELAKALAAGTEARAVALAEHAGQPgYLAYAGSKEALTVWTRRRAATWLYGAG---VRVNTVAPGPVETPI 189
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 5-261 3.90e-14

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: 70.23  E-value: 3.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMAAVQTLQNEGLDPHF-HQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd05343     7 RVALVTGASVGIGAAVARALVQH-GMKVVGCARRVDKIEALAAECQSAGYPTLFpYQCDLSNEEQILSMFSAIRTQHQGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAFK--VADTTPFGNQaeETLRTNFFATRDICRELLPIIK----PSGRVVNIASIAGSMALRQCSQSLkekf 157
Cdd:cd05343    86 DVCINNAGLARPepLLSGKTEGWK--EMFDVNVLALSICTREAYQSMKernvDDGHIININSMSGHRVPPVSVFHF---- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 158 rsediteeelvelmenfvedakkgvhtqkgwpnwaYGVSKIGVIVLSRIQAKELSHKrgQSKILLNSCCPGWVKTDMAGP 237
Cdd:cd05343   160 -----------------------------------YAATKHAVTALTEGLRQELREA--KTHIRATSISPGLVETEFAFK 202

                         250       260
                  ....*....|....*....|....
gi 1993940993 238 HATKTPDEGAITPVYLALLSEEDI 261
Cdd:cd05343   203 LHDNDPEKAAATYESIPCLKPEDV 226
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 5-232 4.09e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 70.14  E-value: 4.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLqnEGLdphFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06057    8 RVAVITGGGSGIGLATARRLAAEGA-TVVVGDIDPEAGKAAADEV--GGL---FVPTDVTDEDAVNALFDTAAETYGSVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIafkvadTTPFGNQAEET--------LRTNFFATRDICRELLPIIKPSGR--VVNIASIAGSM--ALRQCSqs 152
Cdd:PRK06057   82 IAFNNAGI------SPPEDDSILNTgldawqrvQDVNLTSVYLCCKAALPHMVRQGKgsIINTASFVAVMgsATSQIS-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 153 lkekfrsediteeelvelmenfvedakkgvhtqkgwpnwaYGVSKIGVIVLSRiqakELSHKRGQSKILLNSCCPGWVKT 232
Cdd:PRK06057  154 ----------------------------------------YTASKGGVLAMSR----ELGVQFARQGIRVNALCPGPVNT 189
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 5-140 4.53e-14

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: 70.40  E-value: 4.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFA--GHVYLTARDEGrgmaAVQTLQ---NEGLD----PHfhqlDITDLSSIRRIRDF 75
Cdd:cd05355    27 KKALITGGDSGIGRAVAIAFAREGAdvAINYLPEEEDD----AEETKKlieEEGRKclliPG----DLGDESFCRDLVKE 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  76 MRDKYGGVDVLVNNAA---IAFKVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPSGRVVNIASI 140
Cdd:cd05355    99 VVKEFGKLDILVNNAAyqhPQESIEDITT--EQLEKTFRTNIFSMFYLTKAALPHLKKGSSIINTTSV 164
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 5-234 4.62e-14

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 70.03  E-value: 4.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHV--YLTARDEGRGMaaVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:PRK12935    7 KVAIVTGGAKGIGKAITVALAQEGAKVVinYNSSKEAAENL--VNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAI----AFKVADTTPFgnqaEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGSMAlrqcsqslkek 156
Cdd:PRK12935   85 VDILVNNAGItrdrTFKKLNREDW----ERVIDVNLSSVFNTTSAVLPYITEAeeGRIISISSIIGQAG----------- 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993 157 frsediteeelvelmenfvedakkgvhtqkGWPNWAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDM 234
Cdd:PRK12935  150 ------------------------------GFGQTNYSAAKAGMLGFTKSLALELA----KTNVTVNAICPGFIDTEM 193
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-164 4.93e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 70.33  E-value: 4.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   1 MSCPKVAMVTGANKGIGLAIVRALCRqfAGH-VYLTARDEgrgmAAVQTLQNEGLDP-HFHQLDITDLSSIRRIRDFMRD 78
Cdd:PRK06180    1 MSSMKTWLITGVSSGFGRALAQAALA--AGHrVVGTVRSE----AARADFEALHPDRaLARLLDVTDFDAIDAVVADAEA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  79 KYGGVDVLVNNAAIA-FKVADTTPfgnqaEETLR----TNFFATRDICRELLPIIKP--SGRVVNIASIAGSMALRQCSQ 151
Cdd:PRK06180   75 TFGPIDVLVNNAGYGhEGAIEESP-----LAEMRrqfeVNVFGAVAMTKAVLPGMRArrRGHIVNITSMGGLITMPGIGY 149

                         170
                  ....*....|...
gi 1993940993 152 SLKEKFRSEDITE 164
Cdd:PRK06180  150 YCGSKFALEGISE 162
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 5-231 5.43e-14

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


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 69.67  E-value: 5.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALcRQFAGHVYLTARDEGRGMAAVQTLQNE-GLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd08930     3 KIILITGAAGLIGKAFCKAL-LSAGARLILADINAPALEQLKEELTNLyKNRVIALELDITSKESIKELIESYLEKFGRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAFKVaDTTPFGNQAEETLRTN--------FFATRDICRELLPiiKPSGRVVNIASIAGSMAlrqcsqslkE 155
Cdd:cd08930    82 DILINNAYPSPKV-WGSRFEEFPYEQWNEVlnvnlggaFLCSQAFIKLFKK--QGKGSIINIASIYGVIA---------P 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993 156 KFRSEDITEeelvelMENFVEdakkgvhtqkgwpnwaYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVK 231
Cdd:cd08930   150 DFRIYENTQ------MYSPVE----------------YSVIKAGIIHLTKYLAKYYADT----GIRVNAISPGGIL 199
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 7-251 5.65e-14

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: 69.69  E-value: 5.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALCRQfAGHV---YLTARDEGRGMAAvqTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAER-GADVvinYRKSKDAAAEVAA--EIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAI-AFK-VADTTPfgNQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGSMAlrqcsqslkekfrs 159
Cdd:cd05359    78 DVLVSNAAAgAFRpLSELTP--AHWDAKMNTNLKALVHCAQQAAKLMRERggGRIVAISSLGSIRA-------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 160 editeeelvelmenfvedakkgvhtqkgWPNW-AYGVSKIGVIVLSRIQAKELShKRGqskILLNSCCPGWVKTDMAG-- 236
Cdd:cd05359   142 ----------------------------LPNYlAVGTAKAALEALVRYLAVELG-PRG---IRVNAVSPGVIDTDALAhf 189

                         250
                  ....*....|....*.
gi 1993940993 237 PHATKTPDE-GAITPV 251
Cdd:cd05359   190 PNREDLLEAaAANTPA 205
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 7-240 5.73e-14

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: 69.67  E-value: 5.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGlaivRALCRQFAG---HVYLTARDEGRgmaaVQTLQNE--GLDPHF--HQLDITDLSSIRRIRDFMRDK 79
Cdd:cd05350     1 VLITGASSGIG----RALAREFAKagyNVALAARRTDR----LDELKAEllNPNPSVevEILDVTDEERNQLVIAELEAE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  80 YGGVDVLVNNAAIAFkvadTTPFGN-QAE---ETLRTNFFATRDICRELLPII--KPSGRVVNIASIAGsmalrqcsqsl 153
Cdd:cd05350    73 LGGLDLVIINAGVGK----GTSLGDlSFKafrETIDTNLLGAAAILEAALPQFraKGRGHLVLISSVAA----------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 154 kekFRsediteeelvelmenfvedakkgvhtqkGWPNW-AYGVSKIGVIVLsriqAKELSHKRGQSKILLNSCCPGWVKT 232
Cdd:cd05350   138 ---LR----------------------------GLPGAaAYSASKAALSSL----AESLRYDVKKRGIRVTVINPGFIDT 182


                  ....*...
gi 1993940993 233 DMAGPHAT 240
Cdd:cd05350   183 PLTANMFT 190
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 5-146 7.60e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 69.55  E-value: 7.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALcRQFAGHVYLTARDegrgmaavqtlQNEGLDP--HFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:PRK06523   10 KRALVTGGTKGIGAATVARL-LEAGARVVTTARS-----------RPDDLPEgvEFVAADLTTAEGCAAVARAVLERLGG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993940993  83 VDVLVNNAAiafkvADTTPFGNQA-------EETLRTNFFATRDICRELLP--IIKPSGRVVNIASIAGSMAL 146
Cdd:PRK06523   78 VDILVHVLG-----GSSAPAGGFAaltdeewQDELNLNLLAAVRLDRALLPgmIARGSGVIIHVTSIQRRLPL 145
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 5-146 1.07e-13

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: 69.03  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCR--QFAGHVYLTARD--------EGRGMAAVQTLQnegldphFHQLDITDLSSIRRIRD 74
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLASdpSKRFKVYATMRDlkkkgrlwEAAGALAGGTLE-------TLQLDVCDSKSVAAAVE 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  75 FMRDKYggVDVLVNNAAIAFkvadTTPFGNQAEETLR----TNFFATRDICRELLPIIKP--SGRVVNIASIAGSMAL 146
Cdd:cd09806    74 RVTERH--VDVLVCNAGVGL----LGPLEALSEDAMAsvfdVNVFGTVRMLQAFLPDMKRrgSGRILVTSSVGGLQGL 145
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 5-142 1.08e-13

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: 69.85  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd09810     2 GTVVITGASSGLGLAAAKALARRGEWHVVMACRDFLKAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRPLD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993940993  85 VLVNNAAIAFKVADTTPFGNQA-EETLRTN----FFATRDICRELLPIIKPSGRVVNIASIAG 142
Cdd:cd09810    82 ALVCNAAVYLPTAKEPRFTADGfELTVGVNhlghFLLTNLLLEDLQRSENASPRIVIVGSITH 144
PRK05866 PRK05866
SDR family oxidoreductase;
5-146 1.08e-13

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 69.39  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK05866   41 KRILLTGASSGIGEAAAEQFARRGA-TVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVD 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  85 VLVNNAA--IAFKVADTTPFGNQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIAS---IAGSMAL 146
Cdd:PRK05866  120 ILINNAGrsIRRPLAESLDRWHDVERTMVLNYYAPLRLIRGLAPgmLERGDGHIINVATwgvLSEASPL 188
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 6-142 1.34e-13

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: 68.56  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   6 VAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDV 85
Cdd:cd05360     2 VVVITGASSGIGRATALAFAERGA-KVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  86 LVNNAAIAF--KVADTTPfgNQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAG 142
Cdd:cd05360    81 WVNNAGVAVfgRFEDVTP--EEFRRVFDVNYLGHVYGTLAALPHLRRRggGALINVGSLLG 139
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 5-275 1.37e-13

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 68.78  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHqLDITDLSSIRRIRDFM---RDKYG 81
Cdd:cd09808     2 RSFLITGANSGIGKAAALAIAKR-GGTVHMVCRNQTRAEEARKEIETESGNQNIF-LHIVDMSDPKQVWEFVeefKEEGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIAFKVADTTPFGnqAEETLRTNFFATRDICRELLPIIK--PSGRVVNIASiaGSMalrqcsqsLKEKFRS 159
Cdd:cd09808    80 KLHVLINNAGCMVNKRELTEDG--LEKNFATNTLGTYILTTHLIPVLEkeEDPRVITVSS--GGM--------LVQKLNT 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 160 EDITEEelvelmenfvEDAKKGvhtqkgwpNWAYGVSKIGVIVLSRIQAKelshkrGQSKILLNSCCPGWVKT-----DM 234
Cdd:cd09808   148 NNLQSE----------RTAFDG--------TMVYAQNKRQQVIMTEQWAK------KHPEIHFSVMHPGWADTpavrnSM 203

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1993940993 235 AGPHAT-----KTPDEGAITPVYLALLSEEDIEPHGQFVCEKKTQS 275
Cdd:cd09808   204 PDFHARfkdrlRSEEQGADTVVWLALSSAAAKAPSGRFYQDRKPVS 249
PRK08628 PRK08628
SDR family oxidoreductase;
5-139 1.81e-13

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 68.45  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLtARDEgRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08628    8 KVVIVTGGASGIGAAISLRLAEEGAIPVIF-GRSA-PDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRID 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  85 VLVNNAAIAFKVA-DTtpfGNQA-EETLRTNFFATRDICRELLPIIKPS-GRVVNIAS 139
Cdd:PRK08628   86 GLVNNAGVNDGVGlEA---GREAfVASLERNLIHYYVMAHYCLPHLKASrGAIVNISS 140
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 5-141 2.00e-13

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: 68.32  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCrQFAGHVYLTARDEgrgmaAVQTLQNEGLDP----HFHQLDITDLSSIRRIRDFMRDKY 80
Cdd:cd08937     5 KVVVVTGAAQGIGRGVAERLA-GEGARVLLVDRSE-----LVHEVLAEILAAgdaaHVHTADLETYAGAQGVVRAAVERF 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993  81 GGVDVLVNNA--AIAFKVADTTPfGNQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASIA 141
Cdd:cd08937    79 GRVDVLINNVggTIWAKPYEHYE-EEQIEAEIRRSLFPTLWCCRAVLPhmLERQQGVIVNVSSIA 142
PRK06172 PRK06172
SDR family oxidoreductase;
5-247 2.09e-13

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 68.24  E-value: 2.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06172    8 KVALVTGGAAGIGRATALAFAREGA-KVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIafkVADTTPFGNQAEEtlrtNFFATRDI-------C-RELLPII--KPSGRVVNIASIAGSMALRQCSqslk 154
Cdd:PRK06172   87 YAFNNAGI---EIEQGRLAEGSEA----EFDAIMGVnvkgvwlCmKYQIPLMlaQGGGAIVNTASVAGLGAAPKMS---- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 155 ekfrsediteeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDM 234
Cdd:PRK06172  156 -------------------------------------IYAASKHAVIGLTKSAAIEYAKK----GIRVNAVCPAVIDTDM 194

                         250
                  ....*....|...
gi 1993940993 235 AGPHATKTPDEGA 247
Cdd:PRK06172  195 FRRAYEADPRKAE 207
PRK06128 PRK06128
SDR family oxidoreductase;
7-140 2.53e-13

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 68.73  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALCRQFAGHV--YLtARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06128   58 ALITGADSGIGRATAIAFAREGADIAlnYL-PEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGLD 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  85 VLVNNAA--IAFK-VADTTPfgNQAEETLRTNFFATRDICRELLPIIKPSGRVVNIASI 140
Cdd:PRK06128  137 ILVNIAGkqTAVKdIADITT--EQFDATFKTNVYAMFWLCKAAIPHLPPGASIINTGSI 193
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 5-235 2.79e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 67.82  E-value: 2.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLtardeGRGMAAVQTLQNE-GLDPhfHQLDITDLSSIRRIrdfmRDKYGGV 83
Cdd:PRK07060   10 KSVLVTGASSGIGRACAVALAQRGARVVAA-----ARNAAALDRLAGEtGCEP--LRLDVGDDAAIRAA----LAAAGAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAF--KVADTTpfGNQAEETLRTNFFATRDICRELLPIIKPSGR---VVNIASIAGSMALRQCSqslkekfr 158
Cdd:PRK07060   79 DGLVNCAGIASleSALDMT--AEGFDRVMAVNARGAALVARHVARAMIAAGRggsIVNVSSQAALVGLPDHL-------- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993 159 sediteeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMA 235
Cdd:PRK07060  149 ---------------------------------AYCASKAALDAITRVLCVEL----GPHGIRVNSVNPTVTLTPMA 188
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-234 3.05e-13

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 67.82  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06077    7 KVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVAD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFkvadTTPFGNQ----AEETLRTNFFATRDICRELLPIIKPSGRVVNIASIAgsmalrqcsqslkekfrse 160
Cdd:PRK06077   87 ILVNNAGLGL----FSPFLNVddklIDKHISTDFKSVIYCSQELAKEMREGGAIVNIASVA------------------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993 161 diteeelvelmenfvedakkGVHTQKGWPnwAYGVSKIGVIVLSRIQAKELShkrgqSKILLNSCCPGWVKTDM 234
Cdd:PRK06077  144 --------------------GIRPAYGLS--IYGAMKAAVINLTKYLALELA-----PKIRVNAIAPGFVKTKL 190
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 5-254 3.34e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 67.51  E-value: 3.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLdpHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK12828    8 KVVAITGGFGGLGRATAAWLAARGA-RVALIGRGAAPLSQTLPGVPADAL--RIGGIDLVDPQAARRAVDEVNRQFGRLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAiAF---KVADTTPfgNQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASIAGSMAlrqcsqslkekfrs 159
Cdd:PRK12828   85 ALVNIAG-AFvwgTIADGDA--DTWDRMYGVNVKTTLNASKAALPalTASGGGRIVNIGAGAALKA-------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 160 editeeelvelmenfvedakkgvhtqkGWPNWAYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDMAGPHA 239
Cdd:PRK12828  148 ---------------------------GPGMGAYAAAKAGVARLTEALAAELLDR----GITVNAVLPSIIDTPPNRADM 196

                         250       260
                  ....*....|....*....|..
gi 1993940993 240 TK-------TPDEGAITPVYLA 254
Cdd:PRK12828  197 PDadfsrwvTPEQIAAVIAFLL 218
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 5-254 3.58e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 67.44  E-value: 3.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQ-FAGHVYLTARDEGRGMAA--VQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK12827    7 RRVLITGGSGGLGRAIAVRLAADgADVIVLDIHPMRGRAEADavAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEFG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIafkvADTTPF----GNQAEETLRTNFFATRDICRELL-PIIKP--SGRVVNIASIAGSMALRqcsqslk 154
Cdd:PRK12827   87 RLDILVNNAGI----ATDAAFaelsIEEWDDVIDVNLDGFFNVTQAALpPMIRArrGGRIVNIASVAGVRGNR------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 155 ekfrsediteeelvelmenfvedakKGVhtqkgwpnwAYGVSKIGVIVLSRIQAKELSHKRgqskILLNSCCPGWVKTDM 234
Cdd:PRK12827  156 -------------------------GQV---------NYAASKAGLIGLTKTLANELAPRG----ITVNAVAPGAINTPM 197

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1993940993 235 A-----GPHATKT--------PDEGAITPVYLA 254
Cdd:PRK12827  198 AdnaapTEHLLNPvpvqrlgePDEVAALVAFLV 230
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 5-266 3.86e-13

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: 67.22  E-value: 3.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGhVYLTARDEGRGMAAVQTLQNEG-LDPHFHQLDITDLSS--IRRIRDFMRDKYG 81
Cdd:cd05340     5 RIILVTGASDGIGREAALTYARYGAT-VILLGRNEEKLRQVADHINEEGgRQPQWFILDLLTCTSenCQQLAQRIAVNYP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIafkVADTTPFGNQAEETLRT----NFFATRDICRELLPIIKpsgrvvniASIAGSMALRQCSqslkekf 157
Cdd:cd05340    84 RLDGVLHNAGL---LGDVCPLSEQNPQVWQDv*qvNVNATFMLTQALLPLLL--------KSDAGSLVFTSSS------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 158 rsediteeelvelmenfvedakkgvHTQKGWPNW-AYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDM-- 234
Cdd:cd05340   146 -------------------------VGRQGRANWgAYAVSKFATEGL*QVLADEYQ----QRNLRVNCINPGGTRTAMra 196

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1993940993 235 -----AGPHATKTPDEgaITPVYLALLSEEDIEPHGQ 266
Cdd:cd05340   197 safptEDPQKLKTPAD--IMPLYLWLMGDDSRRKTGM 231
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
5-142 5.41e-13

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 66.97  E-value: 5.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLqneGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07067    7 KVALLTGAASGIGEAVAERYLAEGA-RVVIADIKPARARLAALEI---GPAAIAVSLDVTRQDSIDRIVAAAVERFGGID 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993  85 VLVNNAAIaFKVAdttPFGNQAEET--------LRTNFFATRDICRELLPIIKpSGRVVNIASIAG 142
Cdd:PRK07067   83 ILFNNAAL-FDMA---PILDISRDSydrlfavnVKGLFFLMQAVARHMVEQGR-GGKIINMASQAG 143
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 4-142 5.96e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 67.64  E-value: 5.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK07109    8 RQVVVITGASAGVGRATARAFARRGA-KVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGPI 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993  84 DVLVNNAAIA-F-KVADTTPfgnqaEETLR---TNFFATRDICRELLPIIKPSGR--VVNIASIAG 142
Cdd:PRK07109   87 DTWVNNAMVTvFgPFEDVTP-----EEFRRvteVTYLGVVHGTLAALRHMRPRDRgaIIQVGSALA 147
PRK07856 PRK07856
SDR family oxidoreductase;
5-143 9.14e-13

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 66.50  E-value: 9.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMaavqtlqnEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07856    7 RVVLVTGGTRGIGAGIARAFLAAGA-TVVVCGRRAPETV--------DGRPAEFHAADVRDPDQVAALVDAIVERHGRLD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993  85 VLVNNA-----AIAfkvADTTPfgNQAEETLRTNFFATRDICRELLPIIKPS---GRVVNIASIAGS 143
Cdd:PRK07856   78 VLVNNAggspyALA---AEASP--RFHEKIVELNLLAPLLVAQAANAVMQQQpggGSIVNIGSVSGR 139
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 5-268 9.56e-13

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 66.46  E-value: 9.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGhVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK13394    8 KTAVVTGAASGIGKEIALELARAGAA-VAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFkvadTTPFGNQAEET--------LRTNFFATRDICRELLPiIKPSGRVVNIASiagsmalrqcsqslkek 156
Cdd:PRK13394   87 ILVSNAGIQI----VNPIENYSFADwkkmqaihVDGAFLTTKAALKHMYK-DDRGGVVIYMGS----------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 157 frsediteeelvelmenfvedakkgVHTQKGWP-NWAYGVSKIGVIVLSRIQAKELSHKRGQSkillNSCCPGWVKTDMA 235
Cdd:PRK13394  145 -------------------------VHSHEASPlKSAYVTAKHGLLGLARVLAKEGAKHNVRS----HVVCPGFVRTPLV 195

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1993940993 236 GPHATKTPDEGAItpvylallSEEDI--------EPHGQFV 268
Cdd:PRK13394  196 DKQIPEQAKELGI--------SEEEVvkkvmlgkTVDGVFT 228
PRK07035 PRK07035
SDR family oxidoreductase;
5-254 1.38e-12

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 65.81  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07035    9 KIALVTGASRGIGEAIAKLLAQQGA-HVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRLD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAiafkvadTTP-FGNQA-------EETLRTN----FFatrdICRELLPIIKPSGR--VVNIASIAGsmalrqcs 150
Cdd:PRK07035   88 ILVNNAA-------ANPyFGHILdtdlgafQKTVDVNirgyFF----MSVEAGKLMKEQGGgsIVNVASVNG-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 151 qslkekfrsediteeelvelmenFVEDAKKGVhtqkgwpnwaYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWV 230
Cdd:PRK07035  149 -----------------------VSPGDFQGI----------YSITKAAVISMTKAFAKEC----APFGIRVNALLPGLT 191

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1993940993 231 KTDMAGP---------HATKT--------PDEGAITPVYLA 254
Cdd:PRK07035  192 DTKFASAlfkndailkQALAHiplrrhaePSEMAGAVLYLA 232
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 5-148 1.39e-12

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: 66.02  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGL-DPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd08933    10 KVVIVTGGSRGIGRGIVRAFVENGA-KVVFCARGEAAGQALESELNRAGPgSCKFVPCDVTKEEDIKTLISVTVERFGRI 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  84 DVLVNNAaiAFKVADTTPFGNQAEE---TLRTNFFATRDICRELLPIIKPS-GRVVNIASIAGSMALRQ 148
Cdd:cd08933    89 DCLVNNA--GWHPPHQTTDETSAQEfrdLLNLNLISYFLASKYALPHLRKSqGNIINLSSLVGSIGQKQ 155
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 5-227 1.53e-12

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: 65.88  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAvqtlQNEGLDPHFH--QLDITDLSSIRRIRDFMRDKYGG 82
Cdd:cd08943     2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVA----EAAQGGPRALgvQCDVTSEAQVQSAFEQAVLEFGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIAFkvadTTPFGNQAEETLRT----NFFATRDICRELLPIIKPS---GRVVNIASiagsmalrqcsqslke 155
Cdd:cd08943    78 LDIVVSNAGIAT----SSPIAETSLEDWNRsmdiNLTGHFLVSREAFRIMKSQgigGNIVFNAS---------------- 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993 156 kfrsediteeelvelmenfvedaKKGVHTQKGwpNWAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCP 227
Cdd:cd08943   138 -----------------------KNAVAPGPN--AAAYSAAKAAEAHLARCLALEG----GEDGIRVNTVNP 180
PRK12743 PRK12743
SDR family oxidoreductase;
4-236 2.00e-12

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 65.44  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQfaGH-VYLT-ARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK12743    2 AQVAIVTASDSGIGKACALLLAQQ--GFdIGITwHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIAFKvadtTPFGNQAEETLRTNFFATRD---IC-----RELLPIIKPsGRVVNIASIAGSMALrqcsqsl 153
Cdd:PRK12743   80 RIDVLVNNAGAMTK----APFLDMDFDEWRKIFTVDVDgafLCsqiaaRHMVKQGQG-GRIINITSVHEHTPL------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 154 kekfrsediteeelvelmenfVEDAkkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTD 233
Cdd:PRK12743  148 ---------------------PGAS-------------AYTAAKHALGGLTKAMALEL----VEHGILVNAVAPGAIATP 189


                  ...
gi 1993940993 234 MAG 236
Cdd:PRK12743  190 MNG 192
PRK05855 PRK05855
SDR family oxidoreductase;
5-147 2.28e-12

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 66.54  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK05855  316 KLVVVTGAGSGIGRETALAFAREGA-EVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPD 394

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993  85 VLVNNAAI--AFKVADTTPfgNQAEETLRTNF---------FATRDICRELlpiikpSGRVVNIASIAGSMALR 147
Cdd:PRK05855  395 IVVNNAGIgmAGGFLDTSA--EDWDRVLDVNLwgvihgcrlFGRQMVERGT------GGHIVNVASAAAYAPSR 460
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-145 3.15e-12

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 64.60  E-value: 3.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYltardegrgmaAVQTLQNEGLDPHFH--QLDIT-DLSSIrrirdfmRDKYG 81
Cdd:PRK06550    6 KTVLITGAASGIGLAQARAFLAQGA-QVY-----------GVDKQDKPDLSGNFHflQLDLSdDLEPL-------FDWVP 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  82 GVDVLVNNAAI--AFK-VADTTPfgNQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASIAGSMA 145
Cdd:PRK06550   67 SVDILCNTAGIldDYKpLLDTSL--EEWQHIFDTNLTSTFLLTRAYLPqmLERKSGIIINMCSIASFVA 133
PRK06114 PRK06114
SDR family oxidoreductase;
5-234 3.29e-12

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 64.80  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06114    9 QVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAELGALT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFKVADTTPFGNQAEETLRTNFFATRDICRELLPIIKPSGR--VVNIASIAGSMALRQCSQSlkekfrsedi 162
Cdd:PRK06114   89 LAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGgsIVNIASMSGIIVNRGLLQA---------- 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993 163 teeelvelmenfvedakkgvHtqkgwpnwaYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDM 234
Cdd:PRK06114  159 --------------------H---------YNASKAGVIHLSKSLAMEWVGR----GIRVNSISPGYTATPM 197
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 5-143 3.53e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 64.68  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNE-GLDPHFHQLDITDLSSIRRIRDFmrdkYGGV 83
Cdd:PRK06125    8 KRVLITGASKGIGAAAAEAFAAEGC-HLHLVARDADALEALAADLRAAhGVDVAVHALDLSSPEAREQLAAE----AGDI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNA-AIafkvadttPFGNQA---EETLRTNF----FATRDICRELLPIIKP--SGRVVNIASIAGS 143
Cdd:PRK06125   83 DILVNNAgAI--------PGGGLDdvdDAAWRAGWelkvFGYIDLTRLAYPRMKArgSGVIVNVIGAAGE 144
PRK06196 PRK06196
oxidoreductase; Provisional
 5-254 3.63e-12

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 65.47  E-value: 3.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRqfAG-HVYLTARDEGRGMAAVQTLQNEGLDPhfhqLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK06196   27 KTAIVTGGYSGLGLETTRALAQ--AGaHVIVPARRPDVAREALAGIDGVEVVM----LDLADLESVRAFAERFLDSGRRI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAfkVADTTPFGNQAEETLRTNFFATRDICRELLPIIKPSG--RVVNIASIAGSMAlrqcsqslkeKFRSED 161
Cdd:PRK06196  101 DILINNAGVM--ACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAgaRVVALSSAGHRRS----------PIRWDD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 162 iteeelvelmenfvedakkgVHTQKGWPNW-AYGVSK-------IGVIVLSR---IQAKEL----------SHKRGQSKI 220
Cdd:PRK06196  169 --------------------PHFTRGYDKWlAYGQSKtanalfaVHLDKLGKdqgVRAFSVhpggiltplqRHLPREEQV 228

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1993940993 221 LLnsccpGWVktDMAGPHAT---KTPDEGAITPVYLA 254
Cdd:PRK06196  229 AL-----GWV--DEHGNPIDpgfKTPAQGAATQVWAA 258
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 5-248 4.88e-12

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: 64.40  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEglDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05326     5 KVAIITGGASGIGEATARLFAKHGA-RVVIADIDDDAGQAVAAELGDP--DISFVHCDVTVEADVRAAVDTAVARFGRLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNA----AIAFKVADTTpfGNQAEETLRTN----FFATRDICRELLPiiKPSGRVVNIASIAGSMAlrqcsqslkek 156
Cdd:cd05326    82 IMFNNAgvlgAPCYSILETS--LEEFERVLDVNvygaFLGTKHAARVMIP--AKKGSIVSVASVAGVVG----------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 157 frsediteeelvelmenfvedakkgvhtqkGWPNWAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAG 236
Cdd:cd05326   147 ------------------------------GLGPHAYTASKHAVLGLTRSAATEL----GEHGIRVNCVSPYGVATPLLT 192

                         250
                  ....*....|..
gi 1993940993 237 PHAtkTPDEGAI 248
Cdd:cd05326   193 AGF--GVEDEAI 202
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 5-141 5.88e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 64.61  E-value: 5.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEglDPHFHQL-DITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK05872   10 KVVVVTGAARGIGAELARRLHARGA-KLALVDLEEAELAALAAELGGD--DRVLTVVaDVTDLAAMQAAAEEAVERFGGI 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993940993  84 DVLVNNAAIA----FKVADTTPFgnqaEETLRTNFFATRDICRELLP-IIKPSGRVVNIASIA 141
Cdd:PRK05872   87 DVVVANAGIAsggsVAQVDPDAF----RRVIDVNLLGVFHTVRATLPaLIERRGYVLQVSSLA 145
PRK05993 PRK05993
SDR family oxidoreductase;
1-147 7.62e-12

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 63.89  E-value: 7.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   1 MSCPKVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEgrgmAAVQTLQNEGLDPHfhQLDITDLSSIRRIRDFMRDKY 80
Cdd:PRK05993    1 MDMKRSILITGCSSGIGAYCARALQSD-GWRVFATCRKE----EDVAALEAEGLEAF--QLDYAEPESIAALVAQVLELS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  81 GG-VDVLVNNAAIAfkvadttpfgnQA-------EETLR----TNFFATRDICRELLPIIKP--SGRVVNIASIAGSMAL 146
Cdd:PRK05993   74 GGrLDALFNNGAYG-----------QPgavedlpTEALRaqfeANFFGWHDLTRRVIPVMRKqgQGRIVQCSSILGLVPM 142


                  .
gi 1993940993 147 R 147
Cdd:PRK05993  143 K 143
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 3-234 9.17e-12

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: 63.26  E-value: 9.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   3 CPKVAMVTGANKGIGLAIVRALCRQFAGHVYLTardegRGMAAVQTLQNEglDPHFH--QLDITDLSSIRrirdFMRDKY 80
Cdd:cd05351     6 AGKRALVTGAGKGIGRATVKALAKAGARVVAVS-----RTQADLDSLVRE--CPGIEpvCVDLSDWDATE----EALGSV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  81 GGVDVLVNNAAIAFkvadTTPFGNQAEET--------LRTNFFATRDICRELLPIIKPsGRVVNIASIAGSMALRQcsqs 152
Cdd:cd05351    75 GPVDLLVNNAAVAI----LQPFLEVTKEAfdrsfdvnVRAVIHVSQIVARGMIARGVP-GSIVNVSSQASQRALTN---- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 153 lkekfrsediteeelvelmenfvedakkgvHTqkgwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKT 232
Cdd:cd05351   146 ------------------------------HT-------VYCSTKAALDMLTKVMALEL----GPHKIRVNSVNPTVVMT 184


                  ..
gi 1993940993 233 DM 234
Cdd:cd05351   185 DM 186
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 5-232 1.11e-11

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: 63.33  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd08936    11 KVALVTASTDGIGLAIARRLAQDGA-HVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGVD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAI---AFKVADTTpfgnqaEE----TLRTNFFATRDICRELLPII--KPSGRVVNIASIAGSMALrqcsqslke 155
Cdd:cd08936    90 ILVSNAAVnpfFGNILDST------EEvwdkILDVNVKATALMTKAVVPEMekRGGGSVVIVSSVAAFHPF--------- 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993 156 kfrsediteeelvelmenfvedakkgvhtqkgwPNWA-YGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKT 232
Cdd:cd08936   155 ---------------------------------PGLGpYNVSKTALLGLTKNLAPELA----PRNIRVNCLAPGLIKT 195
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-150 1.34e-11

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 62.93  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALcrqfaghvyltaRDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06398    7 KVAIVTGGSQGIGKAVVNRL------------KEEGSNVINFDIKEPSYNDVDYFKVDVSNKEQVIKGIDYVISKYGRID 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  85 VLVNNAAI-AFKVADTTPFGnQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGSMALRQCS 150
Cdd:PRK06398   75 ILVNNAGIeSYGAIHAVEED-EWDRIINVNVNGIFLMSKYTIPYMLKQdkGVIINIASVQSFAVTRNAA 142
PRK07062 PRK07062
SDR family oxidoreductase;
5-140 1.69e-11

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 62.75  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEglDPHFHQL----DITDLSSIRRIRDFMRDKY 80
Cdd:PRK07062    9 RVAVVTGGSSGIGLATVELLLEAGA-SVAICGRDEERLASAEARLREK--FPGARLLaarcDVLDEADVAAFAAAVEARF 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993  81 GGVDVLVNNAAIAFKV--ADTTpfgNQA-EETLRTNFFATRDICRELLPIIKPS--GRVVNIASI 140
Cdd:PRK07062   86 GGVDMLVNNAGQGRVStfADTT---DDAwRDELELKYFSVINPTRAFLPLLRASaaASIVCVNSL 147
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 5-228 3.61e-11

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 61.73  E-value: 3.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGlDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd08942     7 KIVLVTGGSRGIGRMIAQGFLEAGA-RVIISARKAEACADAAEELSAYG-ECIAIPADLSSEEGIEALVARVAERSDRLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFKVA-DTTP---FGNQAEETLRTNFFATrdicRELLPIIKPSG------RVVNIASIAGSMalrqcsqslk 154
Cdd:cd08942    85 VLVNNAGATWGAPlEAFPesgWDKVMDINVKSVFFLT----QALLPLLRAAAtaenpaRVINIGSIAGIV---------- 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993 155 ekfrsediteeelVELMENFvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELSHKRgqskILLNSCCPG 228
Cdd:cd08942   151 -------------VSGLENY-----------------SYGASKAAVHQLTRKLAKELAGEH----ITVNAIAPG 190
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 5-143 5.28e-11

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: 61.25  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGldpHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05345     6 KVAIVTGAGSGFGEGIARRFAQEGA-RVVIADINADGAERVAADIGEAA---IAIQADVTKRADVEAMVEAALSKFGRLD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993  85 VLVNNAAIAFKVADTTPFG-NQAEETLRTNFFATRDICRELLPIIKPSGRVV--NIASIAGS 143
Cdd:cd05345    82 ILVNNAGITHRNKPMLEVDeEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGViiNIASTAGL 143
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 6-233 7.58e-11

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: 60.66  E-value: 7.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   6 VAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGrGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDV 85
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEG-AEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  86 LVNNAAIAFKVADTTP-FGNQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGSMalrqcsqslkekfRSEDI 162
Cdd:cd05365    80 LVNNAGGGGPKPFDMPmTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAggGAILNISSMSSEN-------------KNVRI 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993 163 TeeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRiqakELSHKRGQSKILLNSCCPGWVKTD 233
Cdd:cd05365   147 A----------------------------AYGSSKAAVNHMTR----NLAFDLGPKGIRVNAVAPGAVKTD 185
PRK07831 PRK07831
SDR family oxidoreductase;
5-150 8.40e-11

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 60.82  E-value: 8.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGA-NKGIGLAIVRAlCRQFAGHVYLTARDEGRGMAAVQTLQNE-GLDPHFHQL-DITDLSSIRRIRDFMRDKYG 81
Cdd:PRK07831   18 KVVLVTAAaGTGIGSATARR-ALEEGARVVISDIHERRLGETADELAAElGLGRVEAVVcDVTSEAQVDALIDAAVERLG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIA--FKVADTTPfgnqaEE-------TLRTNFFATRDICRELLPiIKPSGRVVNIASI------------ 140
Cdd:PRK07831   97 RLDVLVNNAGLGgqTPVVDMTD-----DEwsrvldvTLTGTFRATRAALRYMRA-RGHGGVIVNNASVlgwraqhgqahy 170

                         170
                  ....*....|....
gi 1993940993 141 ----AGSMALRQCS 150
Cdd:PRK07831  171 aaakAGVMALTRCS 184
PRK07806 PRK07806
SDR family oxidoreductase;
5-139 1.58e-10

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 59.73  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARD-EGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK07806    7 KTALVTGSSRGIGADTAKILAGAGA-HVVVNYRQkAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993  84 DVLVNNAAIAFKVadttpfGNQAEETLRTNFFATRDICRELLPIIKPSGRVVNIAS 139
Cdd:PRK07806   86 DALVLNASGGMES------GMDEDYAMRLNRDAQRNLARAALPLMPAGSRVVFVTS 135
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 5-145 1.85e-10

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 59.90  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfagHVYLTARDegrgmaaVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08220    9 KTVWVTGAAQGIGYAVALAFVEA---GAKVIGFD-------QAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLD 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  85 VLVNNAAIaFKVADTTPFGNQA-EETLRTNFFATRDICRELLPIIKP--SGRVVNIASIAG-----SMA 145
Cdd:PRK08220   79 VLVNAAGI-LRMGATDSLSDEDwQQTFAVNAGGAFNLFRAVMPQFRRqrSGAIVTVGSNAAhvpriGMA 146
PRK07024 PRK07024
SDR family oxidoreductase;
4-142 1.89e-10

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 59.56  E-value: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVaMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGlDPHFHQLDITDLSSIRRI-RDFMrDKYGG 82
Cdd:PRK07024    3 LKV-FITGASSGIGQALAREYARQGA-TLGLVARRTDALQAFAARLPKAA-RVSVYAADVRDADALAAAaADFI-AAHGL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIAFKV-----ADTTPFgnqaEETLRTNFFATrdiCRELLPIIKP-----SGRVVNIASIAG 142
Cdd:PRK07024   79 PDVVIANAGISVGTlteerEDLAVF----REVMDTNYFGM---VATFQPFIAPmraarRGTLVGIASVAG 141
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 5-142 1.95e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 60.05  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFA--GHVYLTA-RDEGRGMAAVQTlqnEGLDPHFHQLDITDlssirriRDFMRD--- 78
Cdd:PRK06701   47 KVALITGGDSGIGRAVAVLFAKEGAdiAIVYLDEhEDANETKQRVEK---EGVKCLLIPGDVSD-------EAFCKDave 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  79 ----KYGGVDVLVNNAAI---AFKVADTTpfGNQAEETLRTNFFATRDICRELLPIIKPSGRVVNIASIAG 142
Cdd:PRK06701  117 etvrELGRLDILVNNAAFqypQQSLEDIT--AEQLDKTFKTNIYSYFHMTKAALPHLKQGSAIINTGSITG 185
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
5-234 1.98e-10

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 59.74  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQ-FAghVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK08643    3 KVALVTGAGQGIGFAIAKRLVEDgFK--VAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIafkvADTTPFGNQAEETLRTNFfatrdicrellpiikpsgrVVNIASIAGSMalrqcsQSLKEKFRSED-- 161
Cdd:PRK08643   81 NVVVNNAGV----APTTPIETITEEQFDKVY-------------------NINVGGVIWGI------QAAQEAFKKLGhg 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993 162 --ITeeelvelmeNFVEDAKkgvhtQKGWPNWA-YGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDM 234
Cdd:PRK08643  132 gkII---------NATSQAG-----VVGNPELAvYSSTKFAVRGLTQTAARDLASE----GITVNAYAPGIVKTPM 189
PRK08589 PRK08589
SDR family oxidoreductase;
5-145 2.04e-10

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 59.79  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAghvYLTARDEGRGMA-AVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK08589    7 KVAVITGASTGIGQASAIALAQEGA---YVLAVDIAEAVSeTVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  84 DVLVNNAAI---AFKVAD--TTPFGNQAEETLRTNFFATrdicRELLPI-IKPSGRVVNIASIAGSMA 145
Cdd:PRK08589   84 DVLFNNAGVdnaAGRIHEypVDVFDKIMAVDMRGTFLMT----KMLLPLmMEQGGSIINTSSFSGQAA 147
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 9-112 2.20e-10

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: 60.46  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   9 VTGANKGIGLAIVRALCRQFAGHVYLTAR-----DEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd08953   210 VTGGAGGIGRALARALARRYGARLVLLGRsplppEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYGAI 289

                          90       100
                  ....*....|....*....|....*....
gi 1993940993  84 DVLVNNAAIafkVADTTPFGNQAEETLRT 112
Cdd:cd08953   290 DGVIHAAGV---LRDALLAQKTAEDFEAV 315
PLN02253 PLN02253
xanthoxin dehydrogenase
 5-238 2.31e-10

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 59.84  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHqLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PLN02253   19 KVALVTGGATGIGESIVRLFHKHGA-KVCIVDLQDDLGQNVCDSLGGEPNVCFFH-CDVTVEDDVSRAVDFTVDKFGTLD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIA------FKVADTTPFGNQAEETLRTNFFATRDICRELLPIIKpsGRVVNIASIAGSMalrqcsqslkekfr 158
Cdd:PLN02253   97 IMVNNAGLTgppcpdIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKK--GSIVSLCSVASAI-------------- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmenfvedAKKGVHtqkgwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGPH 238
Cdd:PLN02253  161 -------------------GGLGPH--------AYTGSKHAVLGLTRSVAAEL----GKHGIRVNCVSPYAVPTALALAH 209
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-139 2.58e-10

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 59.33  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHV--YLTARDegrgmAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG- 81
Cdd:PRK08642    6 QTVLVTGGSRGLGAAIARAFAREGARVVvnYHQSED-----AAEALADELGDRAIALQADVTDREQVQAMFATATEHFGk 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIAFKV-ADTTP---------FGNQAEETLRtnffATRDICRELLP--IIKPSGRVVNIAS 139
Cdd:PRK08642   81 PITTVVNNALADFSFdGDARKkadditwedFQQQLEGSVK----GALNTIQAALPgmREQGFGRIINIGT 146
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 5-142 2.77e-10

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 59.53  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08277   11 KVAVITGGGGVLGGAMAKELARAGA-KVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGPCD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNA------AIAFKVADTTPFGNQA---------EETLRTNFFATrdicreLLP--------IIKPSGRVVNIASIA 141
Cdd:PRK08277   90 ILINGAggnhpkATTDNEFHELIEPTKTffdldeegfEFVFDLNLLGT------LLPtqvfakdmVGRKGGNIINISSMN 163


                  .
gi 1993940993 142 G 142
Cdd:PRK08277  164 A 164
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 5-146 3.05e-10

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: 59.39  E-value: 3.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd08935     6 KVAVITGGTGVLGGAMARALAQAGA-KVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGTVD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFKVADTTPFGNQAEETlrTNFFATRDICRE----------LLP--------IIKPSGRVVNIASIAGSMAL 146
Cdd:cd08935    85 ILINGAGGNHPDATTDPEHYEPETE--QNFFDLDEEGWEfvfdlnlngsFLPsqvfgkdmLEQKGGSIINISSMNAFSPL 162
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 5-140 3.24e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 59.31  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDE--GRGMAAvqtLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:PRK07097   11 KIALITGASYGIGFAIAKAYAKAGATIVFNDINQElvDKGLAA---YRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIAFKVADTTPFGNQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASI 140
Cdd:PRK07097   88 IDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPsmIKKGHGKIINICSM 147
PRK07069 PRK07069
short chain dehydrogenase; Validated
 7-142 5.79e-10

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 58.18  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHF---HQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK07069    2 AFITGAAGGLGRAIARRMAEQGA-KVFLTDINDAAGLDAFAAEINAAHGEGVafaAVQDVTDEAQWQALLAQAADAMGGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993  84 DVLVNNAAIAfkvADTTPFGNQAEETLRTNFFATRDI---CRELLPIIKPS--GRVVNIASIAG 142
Cdd:PRK07069   81 SVLVNNAGVG---SFGAIEQIELDEWRRVMAINVESIflgCKHALPYLRASqpASIVNISSVAA 141
PRK08177 PRK08177
SDR family oxidoreductase;
4-239 6.15e-10

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 57.73  E-value: 6.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGR--GMAAVQTLQNEgldphfhQLDITDLSSIRRIRDFMRDKYg 81
Cdd:PRK08177    1 KRTALIIGASRGLGLGLVDRLLERGW-QVTATVRGPQQdtALQALPGVHIE-------KLDMNDPASLDQLLQRLQGQR- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 gVDVLVNNAAIAfKVADTTPFGNQAEETLR---TNFFATRDICRELLPIIKP-SGRVVNIASIAGSMALrqcsqslkekf 157
Cdd:PRK08177   72 -FDLLFVNAGIS-GPAHQSAADATAAEIGQlflTNAIAPIRLARRLLGQVRPgQGVLAFMSSQLGSVEL----------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 158 rsEDITEEELvelmenfvedakkgvhtqkgwpnwaYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGP 237
Cdd:PRK08177  139 --PDGGEMPL-------------------------YKASKAALNSMTRSFVAEL----GEPTLTVLSMHPGWVKTDMGGD 187


                  ..
gi 1993940993 238 HA 239
Cdd:PRK08177  188 NA 189
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 5-141 8.80e-10

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 57.65  E-value: 8.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEgrgmaAVQTLQNEGLDPHFHQLDIT-DL---SSIRRIRDFMRDKY 80
Cdd:PRK12823    9 KVVVVTGAAQGIGRGVALRAAAE-GARVVLVDRSE-----LVHEVAAELRAAGGEALALTaDLetyAGAQAAMAAAVEAF 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  81 GGVDVLVNN--AAIAFKvadttPFG----NQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASIA 141
Cdd:PRK12823   83 GRIDVLINNvgGTIWAK-----PFEeyeeEQIEAEIRRSLFPTLWCCRAVLPhmLAQGGGAIVNVSSIA 146
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 5-178 9.39e-10

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: 57.46  E-value: 9.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAGH---VYLTARDEgRGMAAVQtLQNEGLDPHFHQLDITDLSSIRR-IRDFMRDKY 80
Cdd:cd08931     1 KAIFITGAASGIG----RETALLFARNgwfVGLYDIDE-DGLAALA-AELGAENVVAGALDVTDRAAWAAaLADFAAATG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  81 GGVDVLVNNAAIA-FKVADTTPFGnQAEETLRTNFFATRDICRELLPIIK--PSGRVVNIASIAG-------------SM 144
Cdd:cd08931    75 GRLDALFNNAGVGrGGPFEDVPLA-AHDRMVDINVKGVLNGAYAALPYLKatPGARVINTASSSAiygqpdlavysatKF 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1993940993 145 ALRQCSQSLKEKFRSEDIteeELVELMENFVEDA 178
Cdd:cd08931   154 AVRGLTEALDVEWARHGI---RVADVWPWFVDTP 184
PRK08267 PRK08267
SDR family oxidoreductase;
8-142 1.00e-09

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 57.64  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   8 MVTGANKGIGLAIVRAlcrqFAGH---VYLTARDEGrGMAAVQTLQNEGlDPHFHQLDITDLSSI-RRIRDFMRDKYGGV 83
Cdd:PRK08267    5 FITGAASGIGRATALL----FAAEgwrVGAYDINEA-GLAALAAELGAG-NAWTGALDVTDRAAWdAALADFAAATGGRL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993  84 DVLVNNAAIAFkvadTTPFGNQAEE----TLRTNFFATRDICRELLPIIK--PSGRVVNIASIAG 142
Cdd:PRK08267   79 DVLFNNAGILR----GGPFEDIPLEahdrVIDINVKGVLNGAHAALPYLKatPGARVINTSSASA 139
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 5-254 1.12e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 57.63  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAGH---VYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK07478    7 KVAIITGASSGIG----RAAAKLFAREgakVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  82 GVDVLVNNAAIAFKVADTTPFGNQA-EETLRTN----FFATRdicRELLPIIKPSGrvvniasiaGSMAlrqcsqslkek 156
Cdd:PRK07478   83 GLDIAFNNAGTLGEMGPVAEMSLEGwRETLATNltsaFLGAK---HQIPAMLARGG---------GSLI----------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 157 FRSediteeelvelmeNFVEdakkgvHTqKGWP-NWAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDM- 234
Cdd:PRK07478  140 FTS-------------TFVG------HT-AGFPgMAAYAASKAGLIGLTQVLAAEY----GAQGIRVNALLPGGTDTPMg 195

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1993940993 235 -------------AGPHATK---TPDEGAITPVYLA 254
Cdd:PRK07478  196 ramgdtpealafvAGLHALKrmaQPEEIAQAALFLA 231
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 5-145 1.41e-09

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 57.36  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRqfAG-HVYLTARDEGRgMAAVQTLQNEGLDPHfhQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK08263    4 KVWFITGASRGFGRAWTEAALE--RGdRVVATARDTAT-LADLAEKYGDRLLPL--ALDVTDRAAVFAAVETAVEHFGRL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  84 DVLVNNAAIAFkvadttpFG-------NQAEETLRTNFFATRDICRELLPIIKP--SGRVVNIASIAGSMA 145
Cdd:PRK08263   79 DIVVNNAGYGL-------FGmieevteSEARAQIDTNFFGALWVTQAVLPYLREqrSGHIIQISSIGGISA 142
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 6-143 1.55e-09

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 57.07  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   6 VAMVTGANKGIGLAIVRALCRQfaGH-VYLTARDEGRgmaaVQTLQNE-GLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK10538    2 IVLVTGATAGFGECITRRFIQQ--GHkVIATGRRQER----LQELKDElGDNLYIAQLDVRNRAAIEEMLASLPAEWRNI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993940993  84 DVLVNNAAIAFKVADTTPFGNQAEETL-RTNFFATRDICRELLP--IIKPSGRVVNIASIAGS 143
Cdd:PRK10538   76 DVLVNNAGLALGLEPAHKASVEDWETMiDTNNKGLVYMTRAVLPgmVERNHGHIINIGSTAGS 138
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 5-235 1.57e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 57.34  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANkGIGLAIVRalcRQFAG-HVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDkYGGV 83
Cdd:PRK06940    3 EVVVVIGAG-GIGQAIAR---RVGAGkKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQT-LGPV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIafkvadtTPFGNQAEETLRTNFFATRDICRELLPIIKPSGRVVNIASIAGSMaLRQCSQSLKEKFRSedIT 163
Cdd:PRK06940   78 TGLVHTAGV-------SPSQASPEAILKVDLYGTALVLEEFGKVIAPGGAGVVIASQSGHR-LPALTAEQERALAT--TP 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993 164 EEELVELMENFVEDAKKGVHtqkgwpnwAYGVSKIGVIVlsRIQAKelSHKRGQSKILLNSCCPGWVKTDMA 235
Cdd:PRK06940  148 TEELLSLPFLQPDAIEDSLH--------AYQIAKRANAL--RVMAE--AVKWGERGARINSISPGIISTPLA 207
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 5-146 1.64e-09

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: 57.29  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRAL----CRQFAGhvYLTarDEGRGMAAVQTLQNEGLdpHFHQLDITDLSSIRRIRDFMRDKY 80
Cdd:cd09805     1 KAVLITGCDSGFGNLLAKKLdslgFTVLAG--CLT--KNGPGAKELRRVCSDRL--RTLQLDVTKPEQIKRAAQWVKEHV 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  81 GGVDV--LVNNAAIA--FKVADTTPFGNqAEETLRTNFFATRDICRELLPIIKPS-GRVVNIASIAGSMAL 146
Cdd:cd09805    75 GEKGLwgLVNNAGILgfGGDEELLPMDD-YRKCMEVNLFGTVEVTKAFLPLLRRAkGRVVNVSSMGGRVPF 144
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 6-162 1.71e-09

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 56.62  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   6 VAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMA-AVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAE-GFSVALAARREAKLEAlLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAA--IAFKVADTTP--FGNQAEETLRTNFFATRDICRELLPiiKPSGRVV------------NIASIAGS-MALR 147
Cdd:cd05373    80 VLVYNAGanVWFPILETTPrvFEKVWEMAAFGGFLAAREAAKRMLA--RGRGTIIftgataslrgraGFAAFAGAkFALR 157

                         170
                  ....*....|....*
gi 1993940993 148 QCSQSLKEKFRSEDI 162
Cdd:cd05373   158 ALAQSMARELGPKGI 172
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
58-236 1.96e-09

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 56.55  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  58 FHQLDITDLSSIRRIrdfMRDKYGGVDVLVNNAAiafkVADTTPfgnqAEETLRTNFFATRDICRELLPIIKPSGRVVNI 137
Cdd:PRK12428   27 FIQADLGDPASIDAA---VAALPGRIDALFNIAG----VPGTAP----VELVARVNFLGLRHLTEALLPRMAPGGAIVNV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 138 ASIAGsMALRQCSQSLKEKFRSEDItEEELVELMENFVEDAKkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELSHKRGq 217
Cdd:PRK12428   96 ASLAG-AEWPQRLELHKALAATASF-DEGAAWLAAHPVALAT------------GYQLSKEALILWTMRQAQPWFGARG- 160

                         170
                  ....*....|....*....
gi 1993940993 218 skILLNSCCPGWVKTDMAG 236
Cdd:PRK12428  161 --IRVNCVAPGPVFTPILG 177
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 5-146 2.35e-09

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: 56.69  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRqfAGH-VYLTARDEGRGMAAV-QTLQNEGLDPHFHQLDITDLSSIRRIRD-FMRDKYG 81
Cdd:cd09763     4 KIALVTGASRGIGRGIALQLGE--AGAtVYITGRTILPQLPGTaEEIEARGGKCIPVRCDHSDDDEVEALFErVAREQQG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993  82 GVDVLVNNAAIAFK---VADTTPFGNQAEET--------LRTNFFATRDICRELLPIIKpsGRVVNIASIAGSMAL 146
Cdd:cd09763    82 RLDILVNNAYAAVQlilVGVAKPFWEEPPTIwddinnvgLRAHYACSVYAAPLMVKAGK--GLIVIISSTGGLEYL 155
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 5-142 2.39e-09

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: 56.53  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGrgMAAVQTLQNEGLdphFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:cd05371     3 LVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSP--GETVAKLGDNCR---FVPVDVTSEKDVKAALALAKAKFGRLD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993  85 VLVNNAAIAFKVADTTPFGNQA------EETLRTNFFATRDICRELLPII--------KPSGRVVNIASIAG 142
Cdd:cd05371    78 IVVNCAGIAVAAKTYNKKGQQPhslelfQRVINVNLIGTFNVIRLAAGAMgknepdqgGERGVIINTASVAA 149
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 5-258 2.52e-09

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 56.84  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDP--HFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:cd09809     2 KVIIITGANSGIGFETARSFALHGA-HVILACRNMSRASAAVSRILEEWHKArvEAMTLDLASLRSVQRFAEAFKAKNSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIAFKVADTTPFGnqAEETLRTNFFATRDICRELLPIIKPSG--RVVNIASiagsmalrqcsqslkEKFRSE 160
Cdd:cd09809    81 LHVLVCNAAVFALPWTLTEDG--LETTFQVNHLGHFYLVQLLEDVLRRSApaRVIVVSS---------------ESHRFT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 161 DItEEELVELMENFVEDAKKgvhtqKGWPNWAYGVSKIGVIVLSriqaKELSHKRGQSKILLNSCCPG-----------W 229
Cdd:cd09809   144 DL-PDSCGNLDFSLLSPPKK-----KYWSMLAYNRAKLCNILFS----NELHRRLSPRGITSNSLHPGnmmyssihrnwW 213

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1993940993 230 VKT---DMAGPHaTKTPDEGAITPVYLALLSE 258
Cdd:cd09809   214 VYTllfTLARPF-TKSMQQGAATTVYCATAPE 244
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 5-142 3.08e-09

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 56.09  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQtlqnegLDPHFH--QLDITDLSSIRRIRDFMRDKYGG 82
Cdd:cd05363     4 KTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAE------IGPAACaiSLDVTDQASIDRCVAALVDRWGS 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  83 VDVLVNNAAiAFkvaDTTPFGNQAEET--------LRTNFFATRDICRELLPIIKpSGRVVNIASIAG 142
Cdd:cd05363    78 IDILVNNAA-LF---DLAPIVDITRESydrlfainVSGTLFMMQAVARAMIAQGR-GGKIINMASQAG 140
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 5-139 3.35e-09

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: 56.06  E-value: 3.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGL-DPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd05369     4 KVAFITGGGTGIGKAIAKAFAELGA-SVAIAGRKPEVLEAAAEEISSATGgRAHPIQCDVRDPEAVEAAVDETLKEFGKI 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  84 DVLVNNAAIAFkVADTTPFGNQAEET-LRTN----FFATRDICRELLPiIKPSGRVVNIAS 139
Cdd:cd05369    83 DILINNAAGNF-LAPAESLSPNGFKTvIDIDlngtFNTTKAVGKRLIE-AKHGGSILNISA 141
PRK09186 PRK09186
flagellin modification protein A; Provisional
 5-231 6.02e-09

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 55.38  E-value: 6.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMAAVQTLQNEGLDPH--FHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:PRK09186    5 KTILITGAGGLIGSALVKAILEA-GGIVIAADIDKEALNELLESLGKEFKSKKlsLVELDITDQESLEEFLSKSAEKYGK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAaiafkvadtTPFGNQ--------AEETLRTN--------FFATRDICRELLpiIKPSGRVVNIASIAGSMAl 146
Cdd:PRK09186   84 IDGAVNCA---------YPRNKDygkkffdvSLDDFNENlslhlgssFLFSQQFAKYFK--KQGGGNLVNISSIYGVVA- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 147 rqcsqslkEKFRSEDITEeelvelMENFVEdakkgvhtqkgwpnwaYGVSKIGVIVLSRIQAKELSHKRgqskILLNSCC 226
Cdd:PRK09186  152 --------PKFEIYEGTS------MTSPVE----------------YAAIKAGIIHLTKYLAKYFKDSN----IRVNCVS 197


                  ....*
gi 1993940993 227 PGWVK 231
Cdd:PRK09186  198 PGGIL 202
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 5-162 6.54e-09

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: 54.92  E-value: 6.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMAAVQTLQNE-GLDPHFHQLDITDLSSI-RRIRDFMRDKygG 82
Cdd:cd05356     2 TWAVVTGATDGIGKAYAEELAKR-GFNVILISRTQEKLDAVAKEIEEKyGVETKTIAADFSAGDDIyERIEKELEGL--D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 VDVLVNNAAIAFKVADT---TPfGNQAEETLRTNFFATRDICRELLPII--KPSGRVVNIASIAGSM------------- 144
Cdd:cd05356    79 IGILVNNVGISHSIPEYfleTP-EDELQDIINVNVMATLKMTRLILPGMvkRKKGAIVNISSFAGLIptpllatysaska 157

                         170
                  ....*....|....*...
gi 1993940993 145 ALRQCSQSLKEKFRSEDI 162
Cdd:cd05356   158 FLDFFSRALYEEYKSQGI 175
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 5-244 7.16e-09

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: 55.17  E-value: 7.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEgrgmaAVQTLQNEGLDPHfHQLDITDLSSIRR-IRDFMRdkyggV 83
Cdd:cd05368     3 KVALITAAAQGIGRAIALAFAREGANVIATDINEE-----KLKELERGPGITT-RVLDVTDKEQVAAlAKEEGR-----I 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIafkvadtTPFGN-------QAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASIAGSMalrqcsqslk 154
Cdd:cd05368    72 DVLFNCAGF-------VHHGSildceddDWDFAMNLNVRSMYLMIKAVLPkmLARKDGSIINMSSVASSI---------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 155 ekfrsediteeelvelmenfvedakkgvhtqKGWPN-WAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTD 233
Cdd:cd05368   135 -------------------------------KGVPNrFVYSTTKAAVIGLTKSVAADFA----QQGIRCNAICPGTVDTP 179

                         250
                  ....*....|.
gi 1993940993 234 MAGPHATKTPD 244
Cdd:cd05368   180 SLEERIQAQPD 190
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 5-143 7.28e-09

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 55.02  E-value: 7.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYltardegrgMAAVQtlQNEGLDPHFH--QLDITDLSSIRRIRDFMRDKYGG 82
Cdd:PRK06171   10 KIIIVTGGSSGIGLAIVKELLANGA-NVV---------NADIH--GGDGQHENYQfvPTDVSSAEEVNHTVAEIIEKFGR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993  83 VDVLVNNAAIAFKVADTTPFGNQAEETLRTN-------------FFATRDICRELlpIIKPSGRVVNIASIAGS 143
Cdd:PRK06171   78 IDGLVNNAGINIPRLLVDEKDPAGKYELNEAafdkmfninqkgvFLMSQAVARQM--VKQHDGVIVNMSSEAGL 149
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-141 8.04e-09

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 55.37  E-value: 8.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   9 VTGANKGIGLAIVRALCRQfaGH-VYLTARDEgRGMAAVQTLQNEgldpHFHQLDITDLSSIRRIrdfMRdkygGVDVLV 87
Cdd:COG0451     4 VTGGAGFIGSHLARRLLAR--GHeVVGLDRSP-PGAANLAALPGV----EFVRGDLRDPEALAAA---LA----GVDAVV 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993  88 NNAAIAfkvadtTPFGNQAEETLRTNFFATRDI---CREllpiiKPSGRVVNIASIA 141
Cdd:COG0451    70 HLAAPA------GVGEEDPDETLEVNVEGTLNLleaARA-----AGVKRFVYASSSS 115
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 5-266 8.15e-09

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 54.88  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAGH----------------VYLTARDEGRGMAAVQTLQNEGLDPHFHQlditDLSs 68
Cdd:PRK08945   13 RIILVTGAGDGIG----REAALTYARHgatvillgrteekleaVYDEIEAAGGPQPAIIPLDLLTATPQNYQ----QLA- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  69 irrirDFMRDKYGGVDVLVNNAAIafkVADTTPFGNQAEET----LRTNFFATRDICRELLPIIK--PSGRVVNIASIAG 142
Cdd:PRK08945   84 -----DTIEEQFGRLDGVLHNAGL---LGELGPMEQQDPEVwqdvMQVNVNATFMLTQALLPLLLksPAASLVFTSSSVG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 143 smalrqcsqslkekfrsediteeelvelmenfvedakkgvhtQKGWPNW-AYGVSKIGVIVLSRIQAKELSHkrgqSKIL 221
Cdd:PRK08945  156 ------------------------------------------RQGRANWgAYAVSKFATEGMMQVLADEYQG----TNLR 189

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1993940993 222 LNSCCPGWVKTDMAG-------PHATKTPDEgaITPVYLALLSEEDIEPHGQ 266
Cdd:PRK08945  190 VNCINPGGTRTAMRAsafpgedPQKLKTPED--IMPLYLYLMGDDSRRKNGQ 239
PRK07832 PRK07832
SDR family oxidoreductase;
5-146 1.29e-08

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 54.66  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQ-LDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK07832    1 KRCFVTGAASGIGRATALRLAAQGA-ELFLTDRDADGLAQTVADARALGGTVPEHRaLDISDYDAVAAFAADIHAAHGSM 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  84 DVLVNNAAIAF--KVADTTpfGNQAEETLRTNFFATRDICRELLPIIKPSGR---VVNIASIAGSMAL 146
Cdd:PRK07832   80 DVVMNIAGISAwgTVDRLT--HEQWRRMVDVNLMGPIHVIETFVPPMVAAGRgghLVNVSSAAGLVAL 145
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
5-91 1.50e-08

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 53.95  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08063    5 KVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLD 84


                  ....*..
gi 1993940993  85 VLVNNAA 91
Cdd:PRK08063   85 VFVNNAA 91
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 9-112 2.13e-08

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: 52.87  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993    9 VTGANKGIGLAIVRALCRQFAGHVYLTAR---DEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDV 85
Cdd:smart00822   5 ITGGLGGLGRALARWLAERGARRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTG 84

                           90       100
                   ....*....|....*....|....*..
gi 1993940993   86 LVNNAAiafkVADTTPFGNQAEETLRT 112
Cdd:smart00822  85 VIHAAG----VLDDGVLASLTPERFAA 107
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 9-254 2.16e-08

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 53.65  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   9 VTGANKGIGLAIVRALCRQfaGH-VYLTARDEGRGMAAVQTLqnegldPHFHQLDITDLSSIRRIRDFMRD--KYGGVDV 85
Cdd:cd08951    12 ITGSSDGLGLAAARTLLHQ--GHeVVLHARSQKRAADAKAAC------PGAAGVLIGDLSSLAETRKLADQvnAIGRFDA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  86 LVNNAAIAF----KVADTtpfgnQAEETLRTNFFATrdicRELLPIIKPSGRVVNIASiagSMAlRQCSQSLkekfrsED 161
Cdd:cd08951    84 VIHNAGILSgpnrKTPDT-----GIPAMVAVNVLAP----YVLTALIRRPKRLIYLSS---GMH-RGGNASL------DD 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 162 IteeelvelmenfveDAKKgvhtqKGWPNW-AYGVSKIGVIVLSRIQAkelshkRGQSKILLNSCCPGWVKTDMAGPHAT 240
Cdd:cd08951   145 I--------------DWFN-----RGENDSpAYSDSKLHVLTLAAAVA------RRWKDVSSNAVHPGWVPTKMGGAGAP 199

                         250
                  ....*....|....
gi 1993940993 241 KTPDEGAITPVYLA 254
Cdd:cd08951   200 DDLEQGHLTQVWLA 213
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 5-234 2.32e-08

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: 53.68  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQ-NEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:cd05330     4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiAPDAEVLLIKADVSDEAQVEAYVDATVEQFGRI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAFKVADTTPFG-NQAEETLRTNFFATRDICRELLPIIKP--SGRVVNIASIAGSmalrqcsqslkekfrse 160
Cdd:cd05330    84 DGFFNNAGIEGKQNLTEDFGaDEFDKVVSINLRGVFYGLEKVLKVMREqgSGMIVNTASVGGI----------------- 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993 161 diteeelvelmenfvedakKGVHTQKGwpnwaYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDM 234
Cdd:cd05330   147 -------------------RGVGNQSG-----YAAAKHGVVGLTRNSAVEY----GQYGIRINAIAPGAILTPM 192
PRK05854 PRK05854
SDR family oxidoreductase;
5-141 2.56e-08

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 53.92  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRqfAG-HVYLTARDEGRGMAAVQTLQNEGLDPH--FHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK05854   15 KRAVVTGASDGLGLGLARRLAA--AGaEVILPVRNRAKGEAAVAAIRTAVPDAKlsLRALDLSSLASVAALGEQLRAEGR 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993  82 GVDVLVNNAAIafkvadTTPFGNQA-----EETLRTNFFATRDICRELLPIIKPSG-RVVNIASIA 141
Cdd:PRK05854   93 PIHLLINNAGV------MTPPERQTtadgfELQFGTNHLGHFALTAHLLPLLRAGRaRVTSQSSIA 152
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 5-237 3.58e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 53.22  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCrQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08085   10 KNILITGSAQGIGFLLATGLA-EYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPID 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFKVADTTPFGNQAEETLRTN----FFATRDICRELlpIIKPSGRVVNIasiaGSMalrqcsQSlkeKFRSE 160
Cdd:PRK08085   89 VLINNAGIQRRHPFTEFPEQEWNDVIAVNqtavFLVSQAVARYM--VKRQAGKIINI----CSM------QS---ELGRD 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993 161 DITeeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDMAGP 237
Cdd:PRK08085  154 TIT----------------------------PYAASKGAVKMLTRGMCVELA----RHNIQVNGIAPGYFKTEMTKA 198
PRK12746 PRK12746
SDR family oxidoreductase;
5-234 4.13e-08

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 52.73  E-value: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAGHVYLTARDEGRGMAA----VQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKY 80
Cdd:PRK12746    7 KVALVTGASRGIG----RAIAMRLANDGALVAIHYGRNKQAadetIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  81 ------GGVDVLVNNAAIAFKVADTTPFGNQAEETLRTNFFATRDICRELLPIIKPSGRVVNIASiagsmalrqcsqslk 154
Cdd:PRK12746   83 qirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEGRVINISS--------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 155 ekfrsediteeelVELMENFVEDAkkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDM 234
Cdd:PRK12746  148 -------------AEVRLGFTGSI-------------AYGLSKGALNTMTLPLAKHL----GERGITVNTIMPGYTKTDI 197
PRK06953 PRK06953
SDR family oxidoreductase;
5-245 6.11e-08

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 52.00  E-value: 6.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfaGH-VYLTARDEGrGMAAVQTlqnegLDPHFHQLDITDLSSIRRirdfMRDKYGG- 82
Cdd:PRK06953    2 KTVLIVGASRGIGREFVRQYRAD--GWrVIATARDAA-ALAALQA-----LGAEALALDVADPASVAG----LAWKLDGe 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  83 -VDVLVNNAAIAFKVADTTPFGNQAE--ETLRTNFFATRDICRELLPIIKPSGRVvnIASIAGSMALrqcsqslkekfrs 159
Cdd:PRK06953   70 aLDAAVYVAGVYGPRTEGVEPITREDfdAVMHTNVLGPMQLLPILLPLVEAAGGV--LAVLSSRMGS------------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 160 editeeeLVELMENFvedakkgvhtqkgwpNWAYGVSKIG---VIVLSRIQAkelshkRGQSKILLNsccPGWVKTDMAG 236
Cdd:PRK06953  135 -------IGDATGTT---------------GWLYRASKAAlndALRAASLQA------RHATCIALH---PGWVRTDMGG 183


                  ....*....
gi 1993940993 237 PHATKTPDE 245
Cdd:PRK06953  184 AQAALDPAQ 192
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 8-254 6.94e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 52.50  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   8 MVTGANKGIGLAIVRALCrQFAGHVYLTARDEGRGMAAVQTLqnEGLDP----HFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK05875   11 LVTGGGSGIGKGVAAGLV-AAGAAVMIVGRNPDKLAAAAEEI--EALKGagavRYEPADVTDEDQVARAVDAATAWHGRL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAFKVADTTPFGNQA-EETLRTNFFAT----RDICRELlpIIKPSGRVVNIASIAGSMALRqcsqslkekfr 158
Cdd:PRK05875   88 HGVVHCAGGSETIGPITQIDSDAwRRTVDLNVNGTmyvlKHAAREL--VRGGGGSFVGISSIAASNTHR----------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmenfvedakkgvhtqkgwpnW--AYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAG 236
Cdd:PRK05875  155 --------------------------------WfgAYGVTKSAVDHLMKLAADEL----GPSWVRVNSIRPGLIRTDLVA 198

                         250
                  ....*....|....*...
gi 1993940993 237 PhatkTPDEGAITPVYLA 254
Cdd:PRK05875  199 P----ITESPELSADYRA 212
PRK08278 PRK08278
SDR family oxidoreductase;
5-101 7.44e-08

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 52.21  E-value: 7.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFA----------------GHVYLTARD-EGRGMAAVQTlqnegldphfhQLDITDLS 67
Cdd:PRK08278    7 KTLFITGASRGIGLAIALRAARDGAniviaaktaephpklpGTIHTAAEEiEAAGGQALPL-----------VGDVRDED 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1993940993  68 SIRRIRDFMRDKYGGVDVLVNNA-AIAF-KVADTTP 101
Cdd:PRK08278   76 QVAAAVAKAVERFGGIDICVNNAsAINLtGTEDTPM 111
PRK07814 PRK07814
SDR family oxidoreductase;
5-147 7.74e-08

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 52.09  E-value: 7.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRqfAG-HVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK07814   11 QVAVVTGAGRGLGAAIALAFAE--AGaDVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRL 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1993940993  84 DVLVNNAAIAFKVA--DTTPfgNQAEETLRTNFFATRDICRELLPII---KPSGRVVNIASIAGSMALR 147
Cdd:PRK07814   89 DIVVNNVGGTMPNPllSTST--KDLADAFTFNVATAHALTVAAVPLMlehSGGGSVINISSTMGRLAGR 155
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 5-232 8.07e-08

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 52.04  E-value: 8.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08936    8 KVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFGTLD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFKVADTTPFGNQAEETLRTN----FFATRDICRELLPIIKPsGRVVNIASiagsmalrqcsqslkekfrse 160
Cdd:PRK08936   88 VMINNAGIENAVPSHEMSLEDWNKVINTNltgaFLGSREAIKYFVEHDIK-GNIINMSS--------------------- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993940993 161 diteeelvelmenfvedakkgVHTQKGWPNWA-YGVSKIGVIVLSRIQAKELSHKRgqskILLNSCCPGWVKT 232
Cdd:PRK08936  146 ---------------------VHEQIPWPLFVhYAASKGGVKLMTETLAMEYAPKG----IRVNNIGPGAINT 193
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 5-269 8.14e-08

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 52.16  E-value: 8.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGmAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06113   12 KCAIITGAGAGIGKEIAITFATAGASVVVSDINADAAN-HVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGKVD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAiafkVADTTPFGNQAEETLRT---NFFATRDICRELLPIIKPS--GRVVNIASIAGsmalrqcsqslkekfrs 159
Cdd:PRK06113   91 ILVNNAG----GGGPKPFDMPMADFRRAyelNVFSFFHLSQLVAPEMEKNggGVILTITSMAA----------------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 160 editeeelvelmENfvedakKGVHTQkgwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWVKTDMAGphA 239
Cdd:PRK06113  150 ------------EN------KNINMT------SYASSKAAASHLVRNMAFDL----GEKNIRVNGIAPGAILTDALK--S 199

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1993940993 240 TKTPD-EGAI---TPvyLALLSE-EDIEPHGQFVC 269
Cdd:PRK06113  200 VITPEiEQKMlqhTP--IRRLGQpQDIANAALFLC 232
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
5-142 1.50e-07

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 51.22  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLdpHFHQLDITDLSSIRR-IRDFMR----DK 79
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGT-HVISISRTENKELTKLAEQYNSNL--TFHSLDLQDVHELETnFNEILSsiqeDN 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  80 YGGVdVLVNNAAIafkVADTTPFGNQAEETLRT----NFFA----TRDICRELLPiIKPSGRVVNIASIAG 142
Cdd:PRK06924   79 VSSI-HLINNAGM---VAPIKPIEKAESEELITnvhlNLLApmilTSTFMKHTKD-WKVDKRVINISSGAA 144
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-233 1.67e-07

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 51.06  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLqneGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK12481    9 KVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQVEAL---GRKFHFITADLIQQKDIDSIVSQAVEVMGHID 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIaFKVADTTPFGNQAEETL-----RTNFFATRDICRELLPiIKPSGRVVNIASiagsmalrqcsqslkekfrs 159
Cdd:PRK12481   86 ILINNAGI-IRRQDLLEFGNKDWDDVininqKTVFFLSQAVAKQFVK-QGNGGKIINIAS-------------------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993 160 editeeelvelMENFvedakkgvhtQKGWPNWAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTD 233
Cdd:PRK12481  144 -----------MLSF----------QGGIRVPSYTASKSAVMGLTRALATELS----QYNINVNAIAPGYMATD 192
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 7-141 2.74e-07

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: 50.55  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALcRQFAGHVylTARDEgrgmaAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDVL 86
Cdd:cd05331     1 VIVTGAAQGIGRAVARHL-LQAGATV--IALDL-----PFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDAL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  87 VNNAAIaFKVADTTPFGNQA-EETLRTNFFATRDICRELLPIIKP--SGRVVNIASIA 141
Cdd:cd05331    73 VNCAGV-LRPGATDPLSTEDwEQTFAVNVTGVFNLLQAVAPHMKDrrTGAIVTVASNA 129
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 7-236 2.94e-07

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 50.30  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALCRQFAghvylTARDEGRGMAAVQTLQNE-GLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDV 85
Cdd:PRK12936    9 ALVTGASGGIGEEIARLLHAQGA-----IVGLHGTRVEKLEALAAElGERVKIFPANLSDRDEVKALGQKAEADLEGVDI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  86 LVNNAAIA----FKVADTTPFGNQAEETLRTNFFATRDICRELLPiiKPSGRVVNIASIAgsmalrqcsqslkekfrsed 161
Cdd:PRK12936   84 LVNNAGITkdglFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMR--RRYGRIINITSVV-------------------- 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993 162 iteeelvelmenfvedakkGVHTQKGWPNwaYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDMAG 236
Cdd:PRK12936  142 -------------------GVTGNPGQAN--YCASKAGMIGFSKSLAQEIATR----NVTVNCVAPGFIESAMTG 191
PLN00015 PLN00015
protochlorophyllide reductase
 9-142 3.20e-07

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 50.47  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   9 VTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLqneGLDPHFHQLDITDLSSIRRIRDFMRD--KYG-GVDV 85
Cdd:PLN00015    2 ITGASSGLGLATAKALAETGKWHVVMACRDFLKAERAAKSA---GMPKDSYTVMHLDLASLDSVRQFVDNfrRSGrPLDV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993  86 LVNNAAIAFKVADTTPFGNQA-EETLRTNFFATRDICRELLPIIK----PSGRVVNIASIAG 142
Cdd:PLN00015   79 LVCNAAVYLPTAKEPTFTADGfELSVGTNHLGHFLLSRLLLDDLKksdyPSKRLIIVGSITG 140
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-145 4.17e-07

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 50.07  E-value: 4.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANK--GIGLAIVRALCRQ----FAGHVYLTARDEGRGMAAVQT--LQNEGLDP----HFHQLDITDLSSIRR 71
Cdd:PRK12748    5 KKIALVTGASRlnGIGAAVCRRLAAKgidiFFTYWSPYDKTMPWGMHDKEPvlLKEEIESYgvrcEHMEIDLSQPYAPNR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  72 IRDFMRDKYGGVDVLVNNAAiafkVADTTPFGNQAEETL--------RTNFFATRDICRELLPiiKPSGRVVNIAS--IA 141
Cdd:PRK12748   85 VFYAVSERLGDPSILINNAA----YSTHTRLEELTAEQLdkhyavnvRATMLLSSAFAKQYDG--KAGGRIINLTSgqSL 158


                  ....
gi 1993940993 142 GSMA 145
Cdd:PRK12748  159 GPMP 162
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 5-260 4.22e-07

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 50.08  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPH--------FHQLDITDLSSIRRIRDFM 76
Cdd:cd08941     2 KVVLVTGANSGLGLAICERLLAEDDENPELTLILACRNLQRAEAACRALLASHpdarvvfdYVLVDLSNMVSVFAAAKEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  77 RDKYGGVDVLVNNAAI----------AFKVADTTP--------FGNQAE---------------ETLRTNFFATRDICRE 123
Cdd:cd08941    82 KKRYPRLDYLYLNAGImpnpgidwigAIKEVLTNPlfavtnptYKIQAEgllsqgdkatedglgEVFQTNVFGHYYLIRE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 124 LLPIIKPS---GRVVNIASIAGSmalrqcsqslKEKFRSEDIteeelvelmenfvedakKGVHTQKgwpnwAYGVSKIGV 200
Cdd:cd08941   162 LEPLLCRSdggSQIIWTSSLNAS----------PKYFSLEDI-----------------QHLKGPA-----PYSSSKYLV 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 201 IVLSriqakeLSHKRGQSKILLNS--CCPGWVKTDM-----------------------AGPHATKTPDEGAITPVYLAL 255
Cdd:cd08941   210 DLLS------LALNRKFNKLGVYSyvVHPGICTTNLtygilppftwtlalplfyllrrlGSPWHTISPYNGAEALVWLAL 283


                  ....*
gi 1993940993 256 LSEED 260
Cdd:cd08941   284 QKPES 288
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 5-145 4.40e-07

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: 49.89  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGA--NKGIGLAIVRALCRQFA--GHVYLTARDEGRgmaaVQTLQNE-GLDPHFHQLDITDLSSIRRIRDFMRDK 79
Cdd:cd05372     2 KRILITGIanDRSIAWGIAKALHEAGAelAFTYQPEALRKR----VEKLAERlGESALVLPCDVSNDEEIKELFAEVKKD 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1993940993  80 YGGVDVLVNnaAIAFkvADTTPFGNQAEETLRTNFFATRDI--------CRELLPIIKPSGRVVNIASIAGSMA 145
Cdd:cd05372    78 WGKLDGLVH--SIAF--APKVQLKGPFLDTSRKGFLKALDIsayslvslAKAALPIMNPGGSIVTLSYLGSERV 147
PRK08017 PRK08017
SDR family oxidoreductase;
5-142 5.03e-07

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 49.70  E-value: 5.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfaGHVYLTARDEGRGMAAVQTLQNEGLDphfhqLDITDLSSIRR-IRDFMRDKYGGV 83
Cdd:PRK08017    3 KSVLITGCSSGIGLEAALELKRR--GYRVLAACRKPDDVARMNSLGFTGIL-----LDLDDPESVERaADEVIALTDNRL 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  84 DVLVNNAAIAFKVADTTPFGNQAEETLRTNFFATRDICRELLPIIKPSG--RVVNIASIAG 142
Cdd:PRK08017   76 YGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGegRIVMTSSVMG 136
PRK06482 PRK06482
SDR family oxidoreductase;
4-145 5.39e-07

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 49.73  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIV-RALCRqfaGH-VYLTARDEGrgmaAVQTLQNE-GLDPHFHQLDITDLSSIRRIRDFMRDKY 80
Cdd:PRK06482    2 SKTWFITGASSGFGRGMTeRLLAR---GDrVAATVRRPD----ALDDLKARyGDRLWVLQLDVTDSAAVRAVVDRAFAAL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993  81 GGVDVLVNNAAI-----AFKVADTtpfgnQAEETLRTNFFATRDICRELLPIIKPS--GRVVNIASIAGSMA 145
Cdd:PRK06482   75 GRIDVVVSNAGYglfgaAEELSDA-----QIRRQIDTNLIGSIQVIRAALPHLRRQggGRIVQVSSEGGQIA 141
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 5-139 5.73e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 49.29  E-value: 5.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTL-QNEGLDPHFhQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK07677    2 KVVIITGGSSGMGKAMAKRFAEEGA-NVVITGRTKEKLEEAKLEIeQFPGQVLTV-QMDVRNPEDVQKMVEQIDEKFGRI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  84 DVLVNNAAIAFKVA--DTTPFGNQA--EETLRTNFFATRDICRELLPiIKPSGRVVNIAS 139
Cdd:PRK07677   80 DALINNAAGNFICPaeDLSVNGWNSviDIVLNGTFYCSQAVGKYWIE-KGIKGNIINMVA 138
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-92 6.03e-07

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 49.57  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08217    6 KVIVITGGAQGLGRAMAEYLAQKGA-KLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLN 84


                  ....*...
gi 1993940993  85 VLVNNAAI 92
Cdd:PRK08217   85 GLINNAGI 92
PRK06194 PRK06194
hypothetical protein; Provisional
 5-90 7.37e-07

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 49.24  E-value: 7.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAG---HVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK06194    7 KVAVITGAASGFG----LAFARIGAAlgmKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFG 82


                  ....*....
gi 1993940993  82 GVDVLVNNA 90
Cdd:PRK06194   83 AVHLLFNNA 91
PRK07985 PRK07985
SDR family oxidoreductase;
7-269 8.82e-07

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 49.22  E-value: 8.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALCRQFAGHV--YLTARDEGRGMAAvQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07985   52 ALVTGGDSGIGRAAAIAYAREGADVAisYLPVEEEDAQDVK-KIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALGGLD 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLvnnAAIAFK------VADTTpfGNQAEETLRTNFFATRDICRELLPIIKPSGRVVNIASIAGsmalRQCSQSLKEkfr 158
Cdd:PRK07985  131 IM---ALVAGKqvaipdIADLT--SEQFQKTFAINVFALFWLTQEAIPLLPKGASIITTSSIQA----YQPSPHLLD--- 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmenfvedakkgvhtqkgwpnwaYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPG--WVKTDMAG 236
Cdd:PRK07985  199 ----------------------------------YAATKAAILNYSRGLAKQVAEK----GIRVNIVAPGpiWTALQISG 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1993940993 237 PH--------ATKTPDEGA-----ITPVYLALLSEED----IEPHGqfVC 269
Cdd:PRK07985  241 GQtqdkipqfGQQTPMKRAgqpaeLAPVYVYLASQESsyvtAEVHG--VC 288
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
5-234 1.01e-06

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 48.86  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK12938    4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIAFKVADTTPFGNQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASIAGsmalrqcsqslkekfrsedi 162
Cdd:PRK12938   84 VLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDgmVERGWGRIINISSVNG-------------------- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993 163 teeelvelmenfvedaKKGvhtQKGWPNwaYGVSKIGVIVLSRIQAKELSHKrgqsKILLNSCCPGWVKTDM 234
Cdd:PRK12938  144 ----------------QKG---QFGQTN--YSTAKAGIHGFTMSLAQEVATK----GVTVNTVSPGYIGTDM 190
PRK09135 PRK09135
pteridine reductase; Provisional
 4-140 1.28e-06

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 48.39  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQFAgHVYLTARdegRGMAAVQTLQNE--GLDPH---FHQLDITDLSSIRRIRDFMRD 78
Cdd:PRK09135    6 AKVALITGGARRIGAAIARTLHAAGY-RVAIHYH---RSAAEADALAAElnALRPGsaaALQADLLDPDALPELVAACVA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  79 KYGGVDVLVNNAAIAFKvadtTPFGNQAEET--------LRTNFFATRDICRELLpiiKPSGRVVNIASI 140
Cdd:PRK09135   82 AFGRLDALVNNASSFYP----TPLGSITEAQwddlfasnLKAPFFLSQAAAPQLR---KQRGAIVNITDI 144
PRK09134 PRK09134
SDR family oxidoreductase;
1-137 1.78e-06

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 48.00  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   1 MSCPKVAMVTGANKGIGLAIVRALCRQ---FAGHvYLTARDEGRgmAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMR 77
Cdd:PRK09134    6 MAAPRAALVTGAARRIGRAIALDLAAHgfdVAVH-YNRSRDEAE--ALAAEIRALGRRAVALQADLADEAEVRALVARAS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993  78 DKYGGVDVLVNNAAIaFKVADTTPFGNQAEET-----LRTNFFATRDICRELLPiiKPSGRVVNI 137
Cdd:PRK09134   83 AALGPITLLVNNASL-FEYDSAASFTRASWDRhmatnLRAPFVLAQAFARALPA--DARGLVVNM 144
PRK06500 PRK06500
SDR family oxidoreductase;
5-254 1.92e-06

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 48.03  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLdphFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06500    7 KTALITGGTSGIGLETARQFLAEGA-RVAITGRDPASLEAARAELGESAL---VIRADAGDVAAQKALAQALAEAFGRLD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAiafkVADTTPFGNQAEE----TLRTN----FFatrdICRELLPII-KPSGRVVNiASIAGSMALRQCSqslke 155
Cdd:PRK06500   83 AVFINAG----VAKFAPLEDWDEAmfdrSFNTNvkgpYF----LIQALLPLLaNPASIVLN-GSINAHIGMPNSS----- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 156 kfrsediteeelvelmenfvedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELsHKRGqskILLNSCCPGWVKTDMA 235
Cdd:PRK06500  149 ------------------------------------VYAASKAALLSLAKTLSGEL-LPRG---IRVNAVSPGPVQTPLY 188

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1993940993 236 G----PHATK-----------------TPDEGAITPVYLA 254
Cdd:PRK06500  189 GklglPEATLdavaaqiqalvplgrfgTPEEIAKAVLYLA 228
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 5-92 3.01e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 47.36  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFA--------GHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFM 76
Cdd:PRK07791    7 RVVIVTGAGGGIGRAHALAFAAEGArvvvndigVGLDGSASGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLVDAA 86

                          90
                  ....*....|....*.
gi 1993940993  77 RDKYGGVDVLVNNAAI 92
Cdd:PRK07791   87 VETFGGLDVLVNNAGI 102
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 7-198 3.92e-06

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 46.91  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGlaivRALCRQFAGHVY-LTARDegRGMAAVQTLQNEGLdpHFHQLDITDLSSIRRirdFMRDKygGVDV 85
Cdd:pfam01370   1 ILVTGATGFIG----SHLVRRLLEKGYeVIGLD--RLTSASNTARLADL--RFVEGDLTDRDALEK---LLADV--RPDA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  86 LVNNAAIAFKVADttpfGNQAEETLRTNFFATRDICRELLpiIKPSGRVVNI--ASIAGSMAlrqcsqslkEKFRSEDIT 163
Cdd:pfam01370  68 VIHLAAVGGVGAS----IEDPEDFIEANVLGTLNLLEAAR--KAGVKRFLFAssSEVYGDGA---------EIPQEETTL 132

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1993940993 164 EEELVelmenfvedakkgvhtqkgwPNWAYGVSKI 198
Cdd:pfam01370 133 TGPLA--------------------PNSPYAAAKL 147
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 5-100 4.67e-06

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 47.60  E-value: 4.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMAAVQTLQNEGLDphfhqlDITDLSSI---------RRIRDF 75
Cdd:COG3347   426 RVALVTGGAGGIGRATAARLAAE-GAAVVVADLDGEAAEAAAAELGGGYGA------DAVDATDVdvtaeaavaAAFGFA 498

                          90       100
                  ....*....|....*....|....*
gi 1993940993  76 MRDkYGGVDVLVNNAAIAFKVADTT 100
Cdd:COG3347   499 GLD-IGGSDIGVANAGIASSSPEEE 522
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 5-137 6.57e-06

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 46.12  E-value: 6.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfaGH-VYLTARD-EGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAE--GYrVVVHYNRsEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993  83 VDVLVNNAAIAFkvaDTTPFGNQAEET-------LRTNFFATRDICRELLPIIKpsGRVVNI 137
Cdd:cd05357    79 CDVLVNNASAFY---PTPLGQGSEDAWaelfginLKAPYLLIQAFARRLAGSRN--GSIINI 135
PRK07577 PRK07577
SDR family oxidoreductase;
5-141 7.30e-06

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 45.87  E-value: 7.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDegrgmaavqtlQNEGLDPHFHQLDITDL----SSIRRIRDfmrdkY 80
Cdd:PRK07577    4 RTVLVTGATKGIGLALSLRLANL-GHQVIGIARS-----------AIDDFPGELFACDLADIeqtaATLAQINE-----I 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993  81 GGVDVLVNNAAIAFkvadTTPFGNQAEETLRT----NFFATRDICRELLPIIK--PSGRVVNIASIA 141
Cdd:PRK07577   67 HPVDAIVNNVGIAL----PQPLGKIDLAALQDvydlNVRAAVQVTQAFLEGMKlrEQGRIVNICSRA 129
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 7-141 8.11e-06

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


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 46.51  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALCRQfaGH-VYLTARDEGRGMAavqtLQNEGLdpHFHQLDITDLSSIRRIrdfMRdkygGVDV 85
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQ--GYrVRALVRSGSDAVL----LDGLPV--EVVEGDLTDAASLAAA---MK----GCDR 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  86 LVNNAAIafkvadTTPFGNQAEETLRTNFFATR---DICREllpiikpSG--RVVNIASIA 141
Cdd:cd05228    66 VFHLAAF------TSLWAKDRKELYRTNVEGTRnvlDAALE-------AGvrRVVHTSSIA 113
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-142 8.64e-06

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 46.31  E-value: 8.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHV---YLTARDEGRGMAAVQTLQNEGLdphFHQLDITDLSSIRRIRDfMRDKYG 81
Cdd:PRK07792   13 KVAVVTGAAAGLGRAEALGLARLGATVVvndVASALDASDVLDEIRAAGAKAV---AVAGDISQRATADELVA-TAVGLG 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993940993  82 GVDVLVNNAAIafkVADTTPFGNQAEE-------TLRTNFFATRDICRELLPIIKPS-----GRVVNIASIAG 142
Cdd:PRK07792   89 GLDIVVNNAGI---TRDRMLFNMSDEEwdaviavHLRGHFLLTRNAAAYWRAKAKAAggpvyGRIVNTSSEAG 158
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 5-91 1.08e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 45.72  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK07576   10 KNVVVVGGTSGINLGIAQAFARAGA-NVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPID 88


                  ....*..
gi 1993940993  85 VLVNNAA 91
Cdd:PRK07576   89 VLVSGAA 95
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 4-146 1.22e-05

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


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 45.39  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQF------------AGHVY-LTARDEgrgMAAVQTLQNEGLDPHFhqLDITDLSSIR 70
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGwrvvavdlcaddPAVGYpLATRAE---LDAVAAACPDQVLPVI--ADVRDPAALA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  71 RIRDFMRDKYGGVDVLVNNAAIafkVADTTPFGNQAEETLRT----NFFATRDICRELLPII----KP-SGRVVNIASIA 141
Cdd:TIGR04504  76 AAVALAVERWGRLDAAVAAAGV---IAGGRPLWETTDAELDLlldvNLRGVWNLARAAVPAMlarpDPrGGRFVAVASAA 152


                  ....*
gi 1993940993 142 GSMAL 146
Cdd:TIGR04504 153 ATRGL 157
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-112 1.69e-05

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: 44.48  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   9 VTGANKGIGLAIVRALCRQFAGHVYLTARD--EGRGMAA-VQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDV 85
Cdd:pfam08659   5 ITGGLGGLGRELARWLAERGARHLVLLSRSaaPRPDAQAlIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIRG 84

                          90       100
                  ....*....|....*....|....*..
gi 1993940993  86 LVNNAAiafkVADTTPFGNQAEETLRT 112
Cdd:pfam08659  85 VIHAAG----VLRDALLENMTDEDWRR 107
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 7-92 1.71e-05

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 45.33  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDVL 86
Cdd:PRK05876    9 AVITGGASGIGLATGTEFARRGA-RVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVV 87


                  ....*.
gi 1993940993  87 VNNAAI 92
Cdd:PRK05876   88 FSNAGI 93
PRK07102 PRK07102
SDR family oxidoreductase;
15-142 2.43e-05

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 44.53  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  15 GIGLAIVRALCRQFAG---HVYLTARDEGRGMAAVQTLQNEG-LDPHFHQLDITDLSsirRIRDFmrdkYGGVDVLVNNA 90
Cdd:PRK07102    8 GATSDIARACARRYAAagaRLYLAARDVERLERLADDLRARGaVAVSTHELDILDTA---SHAAF----LDSLPALPDIV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  91 AIAF------KVADTTPfgNQAEETLRTNFFATRDICRELLPIIKP--SGRVVNIASIAG 142
Cdd:PRK07102   81 LIAVgtlgdqAACEADP--ALALREFRTNFEGPIALLTLLANRFEArgSGTIVGISSVAG 138
PRK06947 PRK06947
SDR family oxidoreductase;
5-141 2.50e-05

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 44.41  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRaLCRQFAGHVYLT-ARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK06947    3 KVVLITGASRGIGRATAV-LAAARGWSVGINyARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993  84 DVLVNNAAIafkVADTTPFGNQAEETLR----TNFFATRDICRELLPIIKPS-----GRVVNIASIA 141
Cdd:PRK06947   82 DALVNNAGI---VAPSMPLADMDAARLRrmfdTNVLGAYLCAREAARRLSTDrggrgGAIVNVSSIA 145
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 9-169 2.73e-05

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


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 43.55  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   9 VTGANKGIGLAIVRALCRQfaGH-VYLTARDEgrgmaavQTLQNEGLDP-HFHQLDITDLSSIRRIRDfmrdkygGVDVL 86
Cdd:cd05226     3 ILGATGFIGRALARELLEQ--GHeVTLLVRNT-------KRLSKEDQEPvAVVEGDLRDLDSLSDAVQ-------GVDVV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  87 VNNAAiafkvadTTPFGNQAEETLRTNFFATRDICRE--LLPIIKPSGRVVNIASIAGSMALRQcSQSLKEKFRSEDITE 164
Cdd:cd05226    67 IHLAG-------APRDTRDFCEVDVEGTRNVLEAAKEagVKHFIFISSLGAYGDLHEETEPSPS-SPYLAVKAKTEAVLR 138


                  ....*
gi 1993940993 165 EELVE 169
Cdd:cd05226   139 EASLP 143
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 8-71 3.03e-05

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: 44.68  E-value: 3.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1993940993   8 MVTGANKGIGLAIVRALCRQFAGHVYLTAR--DEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRR 71
Cdd:cd05274   154 LITGGLGGLGLLVARWLAARGARHLVLLSRrgPAPRAAARAALLRAGGARVSVVRCDVTDPAALAA 219
PRK06123 PRK06123
SDR family oxidoreductase;
5-141 3.61e-05

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 44.00  E-value: 3.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVR-ALCRQFAGHV-YLTARDEGRgmAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGG 82
Cdd:PRK06123    3 KVMIITGASRGIGAATALlAAERGYAVCLnYLRNRDAAE--AVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993  83 VDVLVNNAAI---AFKVADTTpfGNQAEETLRTNFFATRDICRELLPIIKP-----SGRVVNIASIA 141
Cdd:PRK06123   81 LDALVNNAGIleaQMRLEQMD--AARLTRIFATNVVGSFLCAREAVKRMSTrhggrGGAIVNVSSMA 145
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 5-92 3.90e-05

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 44.18  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRgmaaVQTLQNE-GLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK06200    7 QVALITGGGSGIGRALVERFLAEGA-RVAVLERSAEK----LASLRQRfGDHVLVVEGDVTSYADNQRAVDQTVDAFGKL 81


                  ....*....
gi 1993940993  84 DVLVNNAAI 92
Cdd:PRK06200   82 DCFVGNAGI 90
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 5-234 4.14e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 43.91  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQ---FAGHvYLTARDEGRgmAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFM----- 76
Cdd:PRK12747    5 KVALVTGASRGIGRAIAKRLANDgalVAIH-YGNRKEEAE--ETVYEIQSNGGSAFSIGANLESLHGVEALYSSLdnelq 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  77 -RDKYGGVDVLVNNAAI---AFkVADTTP--FGNQAEETLRTNFFatrdICRELLPIIKPSGRVVNIASIAGSMALrqcs 150
Cdd:PRK12747   82 nRTGSTKFDILINNAGIgpgAF-IEETTEqfFDRMVSVNAKAPFF----IIQQALSRLRDNSRIINISSAATRISL---- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 151 qslkekfrsediteeelvelmENFVedakkgvhtqkgwpnwAYGVSKIGVIVLSRIQAKELshkrGQSKILLNSCCPGWV 230
Cdd:PRK12747  153 ---------------------PDFI----------------AYSMTKGAINTMTFTLAKQL----GARGITVNAILPGFI 191


                  ....
gi 1993940993 231 KTDM 234
Cdd:PRK12747  192 KTDM 195
PRK09730 PRK09730
SDR family oxidoreductase;
5-141 4.85e-05

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 43.69  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAGHVYLTARDEGRGMAAVQTLQNE----GLDPHFHQLDITDLSSIRRIRDFMRDKY 80
Cdd:PRK09730    2 AIALVTGGSRGIG----RATALLLAQEGYTVAVNYQQNLHAAQEVVNLitqaGGKAFVLQADISDENQVVAMFTAIDQHD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993  81 GGVDVLVNNAAIAFKVADTTPF-GNQAEETLRTNFFATRDICRELLPIIK-----PSGRVVNIASIA 141
Cdd:PRK09730   78 EPLAALVNNAGILFTQCTVENLtAERINRVLSTNVTGYFLCCREAVKRMAlkhggSGGAIVNVSSAA 144
PRK05867 PRK05867
SDR family oxidoreductase;
5-269 4.95e-05

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 43.87  E-value: 4.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCrQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK05867   10 KRALITGASTGIGKRVALAYV-EAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGID 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  85 VLVNNAAIafkVADTTPFGNQAEETLR------TNFFATRDICRELLPIIKPSGRVVNIASIAGSMAlrqcsqslkekfr 158
Cdd:PRK05867   89 IAVCNAGI---ITVTPMLDMPLEEFQRlqntnvTGVFLTAQAAAKAMVKQGQGGVIINTASMSGHII------------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993 159 sediteeelvelmenfvedakkGVHTQKGwpnwAYGVSKIGVIVLSRIQAKELShkrgQSKILLNSCCPGWVKTDMAGP- 237
Cdd:PRK05867  153 ----------------------NVPQQVS----HYCASKAAVIHLTKAMAVELA----PHKIRVNSVSPGYILTELVEPy 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1993940993 238 ---HA----------TKTPDEGAITPVYLA-----LLSEEDIEPHGQFVC 269
Cdd:PRK05867  203 teyQPlwepkiplgrLGRPEELAGLYLYLAseassYMTGSDIVIDGGYTC 252
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-139 5.05e-05

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 43.62  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGAN--KGIGLAIVRALCRQFAG--HVYLTARDEGR--GMAAVQT--LQNE----GLDPHFHQLDITDLSSIRRI 72
Cdd:PRK12859    7 KVAVVTGVSrlDGIGAAICKELAEAGADifFTYWTAYDKEMpwGVDQDEQiqLQEEllknGVKVSSMELDLTQNDAPKEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993940993  73 RDFMRDKYGGVDVLVNNAAiafkVADTTPFGNQAEETLRTNFF----ATRDICRELLPII--KPSGRVVNIAS 139
Cdd:PRK12859   87 LNKVTEQLGYPHILVNNAA----YSTNNDFSNLTAEELDKHYMvnvrATTLLSSQFARGFdkKSGGRIINMTS 155
PRK06139 PRK06139
SDR family oxidoreductase;
4-142 6.68e-05

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 43.56  E-value: 6.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQFAGHVyLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGV 83
Cdd:PRK06139    7 GAVVVITGASSGIGQATAEAFARRGARLV-LAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAASFGGRI 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1993940993  84 DVLVNNAAI-AFKVADTTPFgNQAEETLRTNFFATRDICRELLPIIKPSGR--VVNIASIAG 142
Cdd:PRK06139   86 DVWVNNVGVgAVGRFEETPI-EAHEQVIQTNLIGYMRDAHAALPIFKKQGHgiFINMISLGG 146
PRK05717 PRK05717
SDR family oxidoreductase;
5-93 1.11e-04

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 42.57  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQfAGHVYLTARDEGRGMAAVQTLqneGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK05717   11 RVALVTGAARGIGLGIAAWLIAE-GWQVVLADLDRERGSKVAKAL---GENAWFIAMDVADEAQVAAGVAEVLGQFGRLD 86


                  ....*....
gi 1993940993  85 VLVNNAAIA 93
Cdd:PRK05717   87 ALVCNAAIA 95
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 5-172 1.38e-04

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: 42.45  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAGHVYLTARDEGRGMAAVQTLQNE----GLDPHFHQLDITDLSSIRRIRDFMRDKY 80
Cdd:cd05322     3 QVAVVIGGGQTLG----EFLCHGLAEAGYDVAVADINSENAEKVADEInaeyGEKAYGFGADATNEQSVIALSKGVDEIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993  81 GGVDVLVNNAAIAfKVADTTPFGNQA-EETLRTN----FFATRDICRELlpiIKP--SGRVVNIASIAGSMALRQCSQSL 153
Cdd:cd05322    79 KRVDLLVYSAGIA-KSAKITDFELGDfDRSLQVNlvgyFLCAREFSKLM---IRDgiQGRIIQINSKSGKVGSKHNSGYS 154

                         170
                  ....*....|....*....
gi 1993940993 154 KEKFRSEDITEEELVELME 172
Cdd:cd05322   155 AAKFGGVGLTQSLALDLAE 173
PRK09291 PRK09291
SDR family oxidoreductase;
4-142 2.39e-04

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 41.52  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   4 PKVAMVTGANKGIGLAIVRALCRQfaGHvyltardegRGMAAVQT------LQNE----GLDPHFHQLDITDlsSIRRIR 73
Cdd:PRK09291    2 SKTILITGAGSGFGREVALRLARK--GH---------NVIAGVQIapqvtaLRAEaarrGLALRVEKLDLTD--AIDRAQ 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993940993  74 DFMRDkyggVDVLVNNAAI--AFKVADtTPFGNqAEETLRTNFFA----TRDICRELlpIIKPSGRVVNIASIAG 142
Cdd:PRK09291   69 AAEWD----VDVLLNNAGIgeAGAVVD-IPVEL-VRELFETNVFGplelTQGFVRKM--VARGKGKVVFTSSMAG 135
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 7-132 2.39e-04

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 41.03  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALcrQFAGHVYLTA-RDEGrgmaavqtlqnegldphFHQLDITDLSSIRRirdfMRDKYGGVDV 85
Cdd:cd11731     1 IIVIGATGTIGLAVAQLL--SAHGHEVITAgRSSG-----------------DYQVDITDEASIKA----LFEKVGHFDA 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1993940993  86 LVNNAAIAfkvadttPFGNQAEETLRTNFFATRD-------ICRELLPIIKPSG 132
Cdd:cd11731    58 IVSTAGDA-------EFAPLAELTDADFQRGLNSkllgqinLVRHGLPYLNDGG 104
PRK06720 PRK06720
hypothetical protein; Provisional
 5-92 3.56e-04

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 40.34  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAgHVYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK06720   17 KVAIVTGGGIGIGRNTALLLAKQGA-KVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVISITLNAFSRID 95


                  ....*...
gi 1993940993  85 VLVNNAAI 92
Cdd:PRK06720   96 MLFQNAGL 103
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 5-142 5.89e-04

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 40.40  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGlaivRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPHFH-----QLDITDLSSIRRIRDFMRDK 79
Cdd:PRK12384    3 QVAVVIGGGQTLG----AFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGmaygfGADATSEQSVLALSRGVDEI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  80 YGGVDVLVNNAAIAfKVADTTPFGNQA-EETLRTN----FFATRDICRELLPiIKPSGRVVNIASIAG 142
Cdd:PRK12384   79 FGRVDLLVYNAGIA-KAAFITDFQLGDfDRSLQVNlvgyFLCAREFSRLMIR-DGIQGRIIQINSKSG 144
PRK12744 PRK12744
SDR family oxidoreductase;
5-100 6.35e-04

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 40.49  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHV---YLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYG 81
Cdd:PRK12744    9 KVVLIAGGAKNLGGLIARDLAAQGAKAVaihYNSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAAFG 88

                          90       100
                  ....*....|....*....|.
gi 1993940993  82 GVDVLVNNAAIAFK--VADTT 100
Cdd:PRK12744   89 RPDIAINTVGKVLKkpIVEIS 109
PRK12742 PRK12742
SDR family oxidoreductase;
5-142 6.37e-04

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 40.13  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTArdeGRGMAAVQTLQNEGldphfHQLDITDLSSIRRIRDFMRDkYGGVD 84
Cdd:PRK12742    7 KKVLVLGGSRGIGAAIVRRFVTDGANVRFTYA---GSKDAAERLAQETG-----ATAVQTDSADRDAVIDVVRK-SGALD 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1993940993  85 VLVNNAAIAFKVADTTPFGNQAEETLRTNFFATRDICRELLPIIKPSGRVVNIASIAG 142
Cdd:PRK12742   78 ILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEGGRIIIIGSVNG 135
PRK07775 PRK07775
SDR family oxidoreductase;
7-148 1.11e-03

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 39.74  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   7 AMVTGANKGIGLAIVRALCRqfAGH-VYLTARDEGRGMAAVQTLQNEGLDPHFHQLDITDLSSIRRIRDFMRDKYGGVDV 85
Cdd:PRK07775   13 ALVAGASSGIGAATAIELAA--AGFpVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEV 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993940993  86 LVNNAA-IAF-KVADTTPfgNQAEETLRTNFFATRDICRELLP--IIKPSGRVVNIASiagSMALRQ 148
Cdd:PRK07775   91 LVSGAGdTYFgKLHEIST--EQFESQVQIHLVGANRLATAVLPgmIERRRGDLIFVGS---DVALRQ 152
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-140 2.93e-03

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 38.32  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDPhfhQLDITDLSSIRRIRDFMRDKYGGVD 84
Cdd:PRK08993   11 KVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPTETIEQVTALGRRFLSL---TADLRKIDGIPALLERAVAEFGHID 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993940993  85 VLVNNAAIaFKVADTTPFGNQAEE-----TLRTNFFATRDICRELLPIIKpSGRVVNIASI 140
Cdd:PRK08993   88 ILVNNAGL-IRREDAIEFSEKDWDdvmnlNIKSVFFMSQAAAKHFIAQGN-GGKIINIASM 146
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 5-92 9.82e-03

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


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 36.83  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993940993   5 KVAMVTGANKGIGLAIVRALCRQFAGHVYLTARDEGRGMAAVQTLQNEGLDP--HFHQLDITDLSSIRRIRDFmrdkyGG 82
Cdd:cd05237     3 KTILVTGGAGSIGSELVRQILKFGPKKLIVFDRDENKLHELVRELRSRFPHDklRFIIGDVRDKERLRRAFKE-----RG 77

                          90
                  ....*....|
gi 1993940993  83 VDVLVNNAAI 92
Cdd:cd05237    78 PDIVFHAAAL 87
 
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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