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Conserved domains on  [gi|1444067332|emb|SOZ27879|]
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2-hydroxycyclohexanecarboxyl-CoA dehydrogenase [Cupriavidus taiwanensis]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 21-253 1.52e-141

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member TIGR03206:

Pssm-ID: 473865  Cd Length: 250  Bit Score: 396.98  E-value: 1.52e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:TIGR03206  18 ATCRRFAEEGAKVAVFDLNREAAEKVAADIRAKGGNAQAFACDITDRDSVDTAVAAAEQALGPVDVLVNNAGWDKFGPFT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:TIGR03206  98 KTEPPLWERLIAINLTGALHMHHAVLPGMVERGAGRIVNIASDAARVGSSGEAVYAACKGGLVAFSKTMAREHARHGITV 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 181 NVVCPGPTETALFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:TIGR03206 178 NVVCPGPTDTALLDDICGGAENPEKLREAFTRAIPLGRLGQPDDLPGAILFFSSDDASFITGQVLSVSGGLTM 250
 
Name Accession Description Interval E-value
benzo_BadH TIGR03206
2-hydroxycyclohexanecarboxyl-CoA dehydrogenase; Members of this protein family are the enzyme ...
 21-253 1.52e-141

2-hydroxycyclohexanecarboxyl-CoA dehydrogenase; Members of this protein family are the enzyme 2-hydroxycyclohexanecarboxyl-CoA dehydrogenase. The enzymatic properties were confirmed experimentally in Rhodopseudomonas palustris; the enzyme is homotetrameric, and not sensitive to oxygen. This enzyme is part of proposed pathway for degradation of benzoyl-CoA to 3-hydroxypimeloyl-CoA that differs from the analogous in Thauera aromatica. It also may occur in degradation of the non-aromatic compound cyclohexane-1-carboxylate.


Pssm-ID: 132250  Cd Length: 250  Bit Score: 396.98  E-value: 1.52e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:TIGR03206  18 ATCRRFAEEGAKVAVFDLNREAAEKVAADIRAKGGNAQAFACDITDRDSVDTAVAAAEQALGPVDVLVNNAGWDKFGPFT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:TIGR03206  98 KTEPPLWERLIAINLTGALHMHHAVLPGMVERGAGRIVNIASDAARVGSSGEAVYAACKGGLVAFSKTMAREHARHGITV 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 181 NVVCPGPTETALFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:TIGR03206 178 NVVCPGPTDTALLDDICGGAENPEKLREAFTRAIPLGRLGQPDDLPGAILFFSSDDASFITGQVLSVSGGLTM 250
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 21-253 6.27e-87

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: 258.56  E-value: 6.27e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:COG1028    21 AIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:COG1028   101 ELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRV 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 181 NVVCPGPTETALFEdykqGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:COG1028   181 NAVAPGPIDTPMTR----ALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLTA 249
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 21-254 2.86e-75

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 228.92  E-value: 2.86e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAG-ERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:PRK05557   20 AIAERLAAQGANVVINYASSEAGaEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVDILVNNAGITRDNLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK05557  100 MRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGVIGFTKSLARELASRGIT 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 180 VNVVCPGPTETALFEDYkqgagnPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:PRK05557  180 VNAVAPGFIETDMTDAL------PEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHVNGGMVMG 248
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 21-252 5.66e-73

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: 222.81  E-value: 5.66e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW--DVFrp 98
Cdd:cd05333    15 AIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDILVNNAGItrDNL-- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:cd05333    93 LMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGI 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 179 TVNVVCPGPTETALFEDykqgagNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:cd05333   173 TVNAVAPGFIDTDMTDA------LPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGGMY 240
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 21-252 3.85e-65

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: 202.66  E-value: 3.85e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRAlsVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW--DVFRP 98
Cdd:pfam13561  11 AIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAV--LPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFapKLKGP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:pfam13561  89 FLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGI 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 179 TVNVVCPGPTETALFEdykqGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:pfam13561 167 RVNAISPGPIKTLAAS----GIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGYT 236
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 21-157 9.39e-09

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 53.64  E-value: 9.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   21 ATCLRFARAGAAVGVL----DLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVF 96
Cdd:smart00822  15 ALARWLAERGARRLVLlsrsGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVIHAAGVLDD 94

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332   97 RPFVKTEPAQWERLIAINLTGALHMHHAVLPgmvaRKAGRIVNIASDAARVGSSGEAVYAA 157
Cdd:smart00822  95 GVLASLTPERFAAVLAPKAAGAWNLHELTAD----LPLDFFVLFSSIAGVLGSPGQANYAA 151
 
Name Accession Description Interval E-value
benzo_BadH TIGR03206
2-hydroxycyclohexanecarboxyl-CoA dehydrogenase; Members of this protein family are the enzyme ...
 21-253 1.52e-141

2-hydroxycyclohexanecarboxyl-CoA dehydrogenase; Members of this protein family are the enzyme 2-hydroxycyclohexanecarboxyl-CoA dehydrogenase. The enzymatic properties were confirmed experimentally in Rhodopseudomonas palustris; the enzyme is homotetrameric, and not sensitive to oxygen. This enzyme is part of proposed pathway for degradation of benzoyl-CoA to 3-hydroxypimeloyl-CoA that differs from the analogous in Thauera aromatica. It also may occur in degradation of the non-aromatic compound cyclohexane-1-carboxylate.


Pssm-ID: 132250  Cd Length: 250  Bit Score: 396.98  E-value: 1.52e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:TIGR03206  18 ATCRRFAEEGAKVAVFDLNREAAEKVAADIRAKGGNAQAFACDITDRDSVDTAVAAAEQALGPVDVLVNNAGWDKFGPFT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:TIGR03206  98 KTEPPLWERLIAINLTGALHMHHAVLPGMVERGAGRIVNIASDAARVGSSGEAVYAACKGGLVAFSKTMAREHARHGITV 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 181 NVVCPGPTETALFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:TIGR03206 178 NVVCPGPTDTALLDDICGGAENPEKLREAFTRAIPLGRLGQPDDLPGAILFFSSDDASFITGQVLSVSGGLTM 250
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 21-253 6.27e-87

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: 258.56  E-value: 6.27e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:COG1028    21 AIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLDILVNNAGITPPGPLE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:COG1028   101 ELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRV 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 181 NVVCPGPTETALFEdykqGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:COG1028   181 NAVAPGPIDTPMTR----ALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLTA 249
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 21-254 2.86e-75

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 228.92  E-value: 2.86e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAG-ERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:PRK05557   20 AIAERLAAQGANVVINYASSEAGaEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVDILVNNAGITRDNLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK05557  100 MRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAASKAGVIGFTKSLARELASRGIT 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 180 VNVVCPGPTETALFEDYkqgagnPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:PRK05557  180 VNAVAPGFIETDMTDAL------PEDVKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHVNGGMVMG 248
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
21-253 9.00e-75

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 227.35  E-value: 9.00e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFR--P 98
Cdd:PRK05653   20 AIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALDILVNNAG--ITRdaL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK05653   98 LPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGI 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 179 TVNVVCPGPTETALFEdykqgaGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK05653  178 TVNAVAPGFIDTDMTE------GLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVNGGMYM 246
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 21-252 5.66e-73

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: 222.81  E-value: 5.66e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW--DVFrp 98
Cdd:cd05333    15 AIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDILVNNAGItrDNL-- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:cd05333    93 LMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGI 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 179 TVNVVCPGPTETALFEDykqgagNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:cd05333   173 TVNAVAPGFIDTDMTDA------LPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGGMY 240
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 21-253 3.47e-68

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 210.88  E-value: 3.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGV-LDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFR-- 97
Cdd:PRK12825   21 AIALRLARAGADVVVhYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRIDILVNNAG--IFEdk 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  98 PFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHD 177
Cdd:PRK12825   99 PLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGLVGLTKALARELAEYG 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444067332 178 ITVNVVCPGPTETALFEDykqgagNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK12825  179 ITVNMVAPGDIDTDMKEA------TIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQVIEVTGGVDV 248
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 21-247 5.98e-67

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: 207.14  E-value: 5.98e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAqIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd05233    13 AIARRLAREGAKVVLADRNEEALAELAA-IEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNNAGIARPGPLE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:cd05233    92 ELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRV 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 181 NVVCPGPTETALFEDYKqgagnPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSV 247
Cdd:cd05233   172 NAVAPGLVDTPMLAKLG-----PEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPV 233
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 21-252 3.85e-65

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: 202.66  E-value: 3.85e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRAlsVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW--DVFRP 98
Cdd:pfam13561  11 AIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAV--LPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFapKLKGP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:pfam13561  89 FLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGI 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 179 TVNVVCPGPTETALFEdykqGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:pfam13561 167 RVNAISPGPIKTLAAS----GIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGYT 236
FabG-like PRK07231
SDR family oxidoreductase;
21-252 3.47e-62

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 195.43  E-value: 3.47e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRdAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWD-VFRPF 99
Cdd:PRK07231   20 GIARRFAAEGARVVVTDRNEEAAERVAAEIL-AGGRAIAVAADVSDEADVEAAVAAALERFGSVDILVNNAGTThRNGPL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK07231   99 LDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIR 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 180 VNVVCPGPTETALFEDYkQGAGNPEKLvEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK07231  179 VNAVAPVVVETGLLEAF-MGEPTPENR-AKFLATIPLGRLGTPEDIANAALFLASDEASWITGVTLVVDGGRC 249
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
 24-253 6.16e-61

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 192.58  E-value: 6.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  24 LRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTE 103
Cdd:TIGR01963  19 RALAAAGANVVVNDFGEEGAEAAAKVAGDAGGSVIYLPADVTKEDEIADMIAAAAAEFGGLDILVNNAGIQHVAPIEEFP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVV 183
Cdd:TIGR01963  99 PEDWDRIIAVMLTSAFHTIRAALPHMKKQGWGRIINIASAHGLVASPFKSAYVAAKHGLIGLTKVLALEVAEHGITVNAI 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444067332 184 CPGPTETAL----FEDYKQGAGNPEKLV--EAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:TIGR01963 179 CPGYVRTPLvekqIADQAKTRGIPEEQVirEVMLKGQPTKRFVTVDEVAETALYLASDAAAQITGQAIVLDGGWTA 254
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 21-195 7.51e-61

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 190.13  E-value: 7.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:pfam00106  15 AIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILVNNAGITGLGPFS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:pfam00106  95 ELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRV 174

                         170
                  ....*....|....*
gi 1444067332 181 NVVCPGPTETALFED 195
Cdd:pfam00106 175 NAVAPGGVDTDMTKE 189
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-252 6.76e-60

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 189.67  E-value: 6.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGV-LDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTE 103
Cdd:PRK05565   24 LLAKEGAKVVIaYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKIDILVNNAGISNFGLVTDMT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVV 183
Cdd:PRK05565  104 DEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGAVNAFTKALAKELAPSGIRVNAV 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444067332 184 CPGPTETALFEDYKqgagNPEKlvEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK05565  184 APGAIDTEMWSSFS----EEDK--EGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQIITVDGGWT 246
PRK12826 PRK12826
SDR family oxidoreductase;
21-254 1.89e-58

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 185.89  E-value: 1.89e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK12826   21 AIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLDILVANAGIFPLTPFA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAAR-VGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK12826  101 EMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPrVGYPGLAHYAASKAGLVGFTRALALELAARNIT 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 180 VNVVCPGPTETalfedykQGAGN--PEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:PRK12826  181 VNSVHPGGVDT-------PMAGNlgDAQWAEAIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQTLPVDGGATLP 250
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 21-254 1.61e-56

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 180.94  E-value: 1.61e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK12939   22 AFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLDGLVNNAGITNSKSAT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK12939  102 ELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIGMTRSLARELGGRGITV 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 181 NVVCPGPTETALFEDYKQgagnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:PRK12939  182 NAIAPGLTATEATAYVPA-----DERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLLPVNGGFVMN 250
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
21-218 2.66e-56

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 180.45  E-value: 2.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:COG0300    20 ALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGPIDVLVNNAGVGGGGPFE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:COG0300   100 ELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAALEGFSESLRAELAPTGVRV 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1444067332 181 NVVCPGPTETALFEDYKQGAGN----PEKLVEAFTRSIPLGR 218
Cdd:COG0300   180 TAVCPGPVDTPFTARAGAPAGRpllsPEEVARAILRALERGR 221
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 21-231 7.20e-55

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: 176.53  E-value: 7.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIrdaGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:COG4221    20 ATARALAAAGARVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAGVALLGPLE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:COG4221    97 ELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRV 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 181 NVVCPGPTETALFEDykQGAGNPEKLVEAFTRSIPLgrigQPDDLPGAVLF 231
Cdd:COG4221   177 TVIEPGAVDTEFLDS--VFDGDAEAAAAVYEGLEPL----TPEDVAEAVLF 221
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 26-254 3.98e-54

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 175.07  E-value: 3.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPA 105
Cdd:PRK12429   24 LAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVDILVNNAGIQHVAPIEDFPTE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 106 QWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCP 185
Cdd:PRK12429  104 KWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICP 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 186 GPTETAL----FEDYKQGAGNPEKLV--EAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:PRK12429  184 GYVDTPLvrkqIPDLAKERGISEEEVleDVLLPLVPQKRFTTVEEIADYALFLASFAAKGVTGQAWVVDGGWTAQ 258
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
 21-253 7.91e-53

acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.


Pssm-ID: 273823 [Multi-domain]  Cd Length: 242  Bit Score: 171.46  E-value: 7.91e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSV-RCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:TIGR01829  15 AICQRLAKDGYRVAANCGPNEERAEAWLQEQGALGFDFRVvEGDVSSFESCKAAVAKVEAELGPVDVLVNNAGITRDATF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:TIGR01829  95 KKMTYEQWDAVIDTNLNSVFNVTQPVIDGMRERGWGRIINISSVNGQKGQFGQTNYSAAKAGMIGFTKALAQEGATKGVT 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 180 VNVVCPGPTETALFEdykqgaGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:TIGR01829 175 VNTISPGYIATDMVM------AMREDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYITGATLSINGGLYM 242
PRK07063 PRK07063
SDR family oxidoreductase;
1-253 1.22e-52

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 171.39  E-value: 1.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRD--AGGRALSVRCDITDRASVDAAVAAVE 78
Cdd:PRK07063    2 MNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARdvAGARVLAVPADVTDAASVAAAVAAAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  79 QELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAAC 158
Cdd:PRK07063   82 EAFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 159 KGGLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAA 238
Cdd:PRK07063  162 KHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPAAARAETLALQPMKRIGRPEEVAMTAVFLASDEAP 241

                         250
                  ....*....|....*
gi 1444067332 239 FITGQVLSVSGGLTM 253
Cdd:PRK07063  242 FINATCITIDGGRSV 256
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 21-252 3.44e-52

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: 169.76  E-value: 3.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGV-LDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:cd05362    18 AIAKRLARDGASVVVnYASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVDILVNNAGVMLKKPI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:cd05362    98 AETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAFTRVLAKELGGRGIT 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 180 VNVVCPGPTETALFEDykqgaGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:cd05362   176 VNAVAPGPVDTDMFYA-----GKTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQVIRANGGYV 243
PRK07774 PRK07774
SDR family oxidoreductase;
1-253 5.49e-52

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 169.54  E-value: 5.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK07774    1 MGRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNA---GWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSgeaVYAA 157
Cdd:PRK07774   81 FGGIDYLVNNAaiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYSN---FYGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 158 CKGGLVSFSKTIAREHARHDITVNVVCPGPTETAlfedyKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDA 237
Cdd:PRK07774  158 AKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTE-----ATRTVTPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEA 232

                         250
                  ....*....|....*.
gi 1444067332 238 AFITGQVLSVSGGLTM 253
Cdd:PRK07774  233 SWITGQIFNVDGGQII 248
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 21-253 1.64e-51

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: 168.33  E-value: 1.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVgVLDLN--PEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRP 98
Cdd:cd05358    18 AIAIRLATAGANV-VVNYRskEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFGTLDILVNNAGLQGDAS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGA-LHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHD 177
Cdd:cd05358    97 SHEMTLEDWNKVIDVNLTGQfLCAREAIKRFRKSKIKGKIINMSSVHEKIPWPGHVNYAASKGGVKMMTKTLAQEYAPKG 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444067332 178 ITVNVVCPGPTETALFEDYKqgaGNPEKLvEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:cd05358   177 IRVNAIAPGAINTPINAEAW---DDPEQR-ADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGTTLFVDGGMTL 248
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 21-252 5.99e-51

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: 166.68  E-value: 5.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd05344    16 AIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDILVNNAGGPPPGPFA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:cd05344    96 ELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTV 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 181 NVVCPGPTET----ALFEDYKQGAG-NPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:cd05344   176 NSVLPGYIDTervrRLLEARAEKEGiSVEEAEKEVASQIPLGRVGKPEELAALIAFLASEKASYITGQAILVDGGLT 252
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
56-254 6.60e-51

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 166.48  E-value: 6.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  56 RALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAG 135
Cdd:PRK12824   53 QVRLKELDVTDTEECAEALAEIEEEEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 136 RIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYkqgagnPEKLVEAFTRSIP 215
Cdd:PRK12824  133 RIINISSVNGLKGQFGQTNYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQM------GPEVLQSIVNQIP 206

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1444067332 216 LGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:PRK12824  207 MKRLGTPEEIAAAVAFLVSEAAGFITGETISINGGLYMH 245
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 27-252 1.49e-50

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: 165.61  E-value: 1.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  27 ARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQ 106
Cdd:cd05347    26 AEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDILVNNAGIIRRHPAEEFPEAE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 107 WERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPG 186
Cdd:cd05347   106 WRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVAGLTKALATEWARHGIQVNAIAPG 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 187 PTET----ALFEDykqgagnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:cd05347   186 YFATemteAVVAD--------PEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQIIFVDGGWL 247
PRK06138 PRK06138
SDR family oxidoreductase;
21-252 2.70e-50

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 165.32  E-value: 2.70e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRdAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK06138   20 ATAKLFAREGARVVVADRDAEAAERVAAAIA-AGGRAFARQGDVGSAEAVEALVDFVAARWGRLDVLVNNAGFGCGGTVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK06138   99 TTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIASLTRAMALDHATDGIRV 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444067332 181 NVVCPGPTETALFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK06138  179 NAVAPGTIDTPYFRRIFARHADPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFATGTTLVVDGGWL 250
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 4-250 7.93e-50

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: 163.71  E-value: 7.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIrdaGGRALSVRCDITDRASVDAAVAAVEQELGP 83
Cdd:cd05345     3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADI---GEAAIAIQADVTKRADVEAMVEAALSKFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  84 IDVLVNNAGWDVF-RPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGL 162
Cdd:cd05345    80 LDILVNNAGITHRnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 163 VSFSKTIAREHARHDITVNVVCPGPTETALFEDYkQGAGNPEKLvEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITG 242
Cdd:cd05345   160 VTATKAMAVELAPRNIRVNCLCPVAGETPLLSMF-MGEDTPENR-AKFRATIPLGRLSTPDDIANAALYLASDEASFITG 237


                  ....*...
gi 1444067332 243 QVLSVSGG 250
Cdd:cd05345   238 VALEVDGG 245
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 26-253 1.74e-48

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: 160.32  E-value: 1.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDL-NPEAGERVAAqirDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWD-VFRPFV--K 101
Cdd:cd05349    20 FAREGARVVVNYYrSTESAEAVAA---EAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIVNNALIDfPFDPDQrkT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 102 TEPAQWERL---IAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:cd05349    97 FDTIDWEDYqqqLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTTAKAALLGFTRNMAKELGPYGI 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 179 TVNVVCPG---PTETAlfedykqgAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:cd05349   177 TVNMVSGGllkVTDAS--------AATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVTGQNLVVDGGLVM 246
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 25-254 2.53e-48

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: 160.23  E-value: 2.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVLDLNPEAGERVAAQ-IRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTE 103
Cdd:cd05366    21 RLAADGFNIVLADLNLEEAAKSTIQeISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSFDVMVNNAGIAPITPLLTIT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMHHAVLPGMVARK-AGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNV 182
Cdd:cd05366   101 EEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSASKFAVRGLTQTAAQELAPKGITVNA 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 183 VCPGPTETALFEDY-----KQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:cd05366   181 YAPGIVKTEMWDYIdeevgEIAGKPEGEGFAEFSSSIPLGRLSEPEDVAGLVSFLASEDSDYITGQTILVDGGMVYR 257
PRK07074 PRK07074
SDR family oxidoreductase;
21-252 6.86e-48

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 159.16  E-value: 6.86e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAggRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK07074   17 ALARRFLAAGDRVLALDIDAAALAAFADALGDA--RFVPVACDLTDAASLAAALANAAAERGPVDVLVANAGAARAASLH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASdAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK07074   95 DTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGS-VNGMAALGHPAYSAAKAGLIHYTKLLAVEYGRFGIRA 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444067332 181 NVVCPGPTETALFEdyKQGAGNPEkLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK07074  174 NAVAPGTVKTQAWE--ARVAANPQ-VFEELKKWYPLQDFATPDDVANAVLFLASPAARAITGVCLPVDGGLT 242
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 26-251 8.19e-48

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 159.07  E-value: 8.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPA 105
Cdd:PRK07097   30 YAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDILVNNAGIIKRIPMLEMSAE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 106 QWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCP 185
Cdd:PRK07097  110 DFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAAKGGLKMLTKNIASEYGEANIQCNGIGP 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 186 GPTETA----LFEDYKQGAGNP-EKLVEAFTrsiPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:PRK07097  190 GYIATPqtapLRELQADGSRHPfDQFIIAKT---PAARWGDPEDLAGPAVFLASDASNFVNGHILYVDGGI 257
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-254 1.08e-47

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 158.65  E-value: 1.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAggrALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK07067    1 MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPA---AIAVSLDVTRQDSIDRIVAAAVER 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVAR-KAGRIVNIASDAARVGSSGEAVYAACK 159
Cdd:PRK07067   78 FGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQgRGGKIINMASQAGRRGEALVSHYCATK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 160 GGLVSFSKTIAREHARHDITVNVVCPGPTET-------ALFEDYK-QGAGNPEKLVEAftrSIPLGRIGQPDDLPGAVLF 231
Cdd:PRK07067  158 AAVISYTQSAALALIRHGINVNAIAPGVVDTpmwdqvdALFARYEnRPPGEKKRLVGE---AVPLGRMGVPDDLTGMALF 234

                         250       260
                  ....*....|....*....|...
gi 1444067332 232 FAGDDAAFITGQVLSVSGGLTMN 254
Cdd:PRK07067  235 LASADADYIVAQTYNVDGGNWMS 257
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 21-254 1.27e-47

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 158.12  E-value: 1.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEagervaaqiRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFR--P 98
Cdd:PRK08220   23 AVALAFVEAGAKVIGFDQAFL---------TQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLDVLVNAAG--ILRmgA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK08220   92 TDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSLAKCVGLELAPYGV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 179 TVNVVCPGPTETALF------EDYKQG--AGNPeklvEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK08220  172 RCNVVSPGSTDTDMQrtlwvdEDGEQQviAGFP----EQFKLGIPLGKIARPQEIANAVLFLASDLASHITLQDIVVDGG 247


                  ....
gi 1444067332 251 LTMN 254
Cdd:PRK08220  248 ATLG 251
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 21-251 5.76e-47

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 156.42  E-value: 5.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAG----ERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVF 96
Cdd:PRK12827   21 AIAVRLAADGADVIVLDIHPMRGraeaDAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEFGRLDILVNNAGIATD 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  97 RPFVKTEPAQWERLIAINLTGALHMHHAVLPGMV-ARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHAR 175
Cdd:PRK12827  101 AAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIrARRGGRIVNIASVAGVRGNRGQVNYAASKAGLIGLTKTLANELAP 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444067332 176 HDITVNVVCPGPTETAlfedykqGAGNPEkLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:PRK12827  181 RGITVNAVAPGAINTP-------MADNAA-PTEHLLNPVPVQRLGEPDEVAALVAFLVSDAASYVTGQVIPVDGGF 248
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 25-252 6.58e-47

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 156.36  E-value: 6.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVLDLNpEAGERVAAQIrdAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:PRK06841   34 LFAAKGARVALLDRS-EDVAEVAAQL--LGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILVNSAGVALLAPAEDVSE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVC 184
Cdd:PRK06841  111 EDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASKAGVVGMTKVLALEWGPYGITVNAIS 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 185 PGPTETALfedYKQGAGNPekLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK06841  191 PTVVLTEL---GKKAWAGE--KGERAKKLIPAGRFAYPEEIAAAALFLASDAAAMITGENLVIDGGYT 253
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-253 1.24e-46

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 156.21  E-value: 1.24e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK13394    2 MSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMV-ARKAGRIVNIASDAARVGSSGEAVYAACK 159
Cdd:PRK13394   82 FGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSVHSHEASPLKSAYVTAK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 160 GGLVSFSKTIAREHARHDITVNVVCPGPTETALFEdyKQ--------GAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLF 231
Cdd:PRK13394  162 HGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVD--KQipeqakelGISEEEVVKKVMLGKTVDGVFTTVEDVAQTVLF 239

                         250       260
                  ....*....|....*....|..
gi 1444067332 232 FAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK13394  240 LSSFPSAALTGQSFVVSHGWFM 261
PRK06172 PRK06172
SDR family oxidoreductase;
1-252 2.27e-46

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 155.29  E-value: 2.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK06172    2 SMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFR-PFVKTEPAQWERLIAINLTGA-LHMHHAvLPGMVARKAGRIVNIASDAARVGSSGEAVYAAC 158
Cdd:PRK06172   82 YGRLDYAFNNAGIEIEQgRLAEGSEAEFDAIMGVNVKGVwLCMKYQ-IPLMLAQGGGAIVNTASVAGLGAAPKMSIYAAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 159 KGGLVSFSKTIAREHARHDITVNVVCPGPTETALFEdyKQGAGNPEKLvEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAA 238
Cdd:PRK06172  161 KHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFR--RAYEADPRKA-EFAAAMHPVGRIGKVEEVASAVLYLCSDGAS 237

                         250
                  ....*....|....
gi 1444067332 239 FITGQVLSVSGGLT 252
Cdd:PRK06172  238 FTTGHALMVDGGAT 251
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 23-250 8.81e-46

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 153.57  E-value: 8.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  23 CLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWD-VFRPFVK 101
Cdd:PRK07890   22 AVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDALVNNAFRVpSMKPLAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 102 TEPAQWERLIAINLTGALHMHHAVLPGMvARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVN 181
Cdd:PRK07890  102 ADFAHWRAVIELNVLGTLRLTQAFTPAL-AESGGSIVMINSMVLRHSQPKYGAYKMAKGALLAASQSLATELGPQGIRVN 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 182 VVCPG----PTETALFEDYKQGAG-NPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK07890  181 SVAPGyiwgDPLKGYFRHQAGKYGvTVEQIYAETAANSDLKRLPTDDEVASAVLFLASDLARAITGQTLDVNCG 254
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
 24-254 1.66e-45

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 152.99  E-value: 1.66e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  24 LRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTE 103
Cdd:TIGR02415  18 ERLAKDGFAVAVADLNEETAKETAKEINQAGGKAVAYKLDVSDKDQVFSAIDQAAEKFGGFDVMVNNAGVAPITPILEIT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGalhmhhaVLPGM--VARK------AGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHAR 175
Cdd:TIGR02415  98 EEELKKVYNVNVKG-------VLFGIqaAARQfkkqghGGKIINAASIAGHEGNPILSAYSSTKFAVRGLTQTAAQELAP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 176 HDITVNVVCPGPTETALFE--DYK--QGAGNPE-KLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:TIGR02415 171 KGITVNAYCPGIVKTPMWEeiDEEtsEIAGKPIgEGFEEFSSEIALGRPSEPEDVAGLVSFLASEDSDYITGQSILVDGG 250


                  ....
gi 1444067332 251 LTMN 254
Cdd:TIGR02415 251 MVYN 254
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 21-253 1.89e-45

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: 152.62  E-value: 1.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRdaggralSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd05331    13 AVARHLLQAGATVIALDLPFVLLLEYGDPLR-------LTPLDVADAAAVREVCSRLLAEHGPIDALVNCAGVLRPGATD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:cd05331    86 PLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELAPYGVRC 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 181 NVVCPGPTETALFEDYKQGAGNPEKLV----EAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:cd05331   166 NVVSPGSTDTAMQRTLWHDEDGAAQVIagvpEQFRLGIPLGKIAQPADIANAVLFLASDQAGHITMHDLVVDGGATL 242
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 25-251 2.07e-45

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 152.90  E-value: 2.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVLDLNPEAGERVAAQIrdAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFRP---FVK 101
Cdd:PRK12829   30 AFAEAGARVHVCDVSEAALAATAARL--PGAKVTATVADVADPAQVERVFDTAVERFGGLDVLVNNAG--IAGPtggIDE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 102 TEPAQWERLIAINLTGALHMHHAVLPGMVARKAGR-IVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK12829  106 ITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGvIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRV 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444067332 181 NVVCPG----PTETALFEDYKQGAGNPEKLVEA-FTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:PRK12829  186 NAILPGivrgPRMRRVIEARAQQLGIGLDEMEQeYLEKISLGRMVEPEDIAATALFLASPAARYITGQAISVDGNV 261
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 21-252 2.31e-45

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: 152.12  E-value: 2.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDL-NPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:cd05359    13 AIALRLAERGADVVINYRkSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVLVSNAAAGAFRPL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:cd05359    93 SELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVRYLAVELGPRGIR 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 180 VNVVCPGPTETalfeDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:cd05359   173 VNAVSPGVIDT----DALAHFPNREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDGGLS 241
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 21-251 3.56e-45

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 151.82  E-value: 3.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAG-ERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:PRK12937   20 AIARRLAADGFAVAVNYAGSAAAaDELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRIDVLVNNAGVMPLGTI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK12937  100 ADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAASKAAVEGLVHVLANELRGRGIT 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444067332 180 VNVVCPGPTETALFEDykqgaGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:PRK12937  178 VNAVAPGPVATELFFN-----GKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQVLRVNGGF 244
PRK06124 PRK06124
SDR family oxidoreductase;
26-252 3.68e-45

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 152.17  E-value: 3.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPA 105
Cdd:PRK06124   31 LAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLDILVNNVGARDRRPLAELDDA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 106 QWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCP 185
Cdd:PRK06124  111 AIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAP 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 186 G--PTET--ALFEDykqgagnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK06124  191 GyfATETnaAMAAD--------PAVGPWLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGHVLAVDGGYS 253
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 26-252 5.15e-45

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: 151.83  E-value: 5.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDA--GGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTE 103
Cdd:cd08940    22 LAAAGANIVLNGFGDAAEIEAVRAGLAAkhGVKVLYHGADLSKPAAIEDMVAYAQRQFGGVDILVNNAGIQHVAPIEDFP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVV 183
Cdd:cd08940   102 TEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAI 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 184 CPGPTETALFE----DYKQGAGNPEK--LVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:cd08940   182 CPGWVLTPLVEkqisALAQKNGVPQEqaARELLLEKQPSKQFVTPEQLGDTAVFLASDAASQITGTAVSVDGGWT 256
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
21-254 4.70e-44

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 149.11  E-value: 4.70e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK08643   17 AIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNVVVNNAGVAPTTPIE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGalhmhhaVLPGM-VARKA-------GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIARE 172
Cdd:PRK08643   97 TITEEQFDKVYNINVGG-------VIWGIqAAQEAfkklghgGKIINATSQAGVVGNPELAVYSSTKFAVRGLTQTAARD 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 173 HARHDITVNVVCPGPTETALFED----YKQGAGNPEKL-VEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSV 247
Cdd:PRK08643  170 LASEGITVNAYAPGIVKTPMMFDiahqVGENAGKPDEWgMEQFAKDITLGRLSEPEDVANCVSFLAGPDSDYITGQTIIV 249


                  ....*..
gi 1444067332 248 SGGLTMN 254
Cdd:PRK08643  250 DGGMVFH 256
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 26-252 6.42e-44

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 148.94  E-value: 6.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPA 105
Cdd:PRK08213   32 LGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDILVNNAGATWGAPAEDHPVE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 106 QWERLIAINLTGALHMHHAVLP-GMVARKAGRIVNIASDAARVGSSGEAV----YAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK08213  112 AWDKVMNLNVRGLFLLSQAVAKrSMIPRGYGRIINVASVAGLGGNPPEVMdtiaYNTSKGAVINFTRALAAEWGPHGIRV 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 181 NVVCPG--PTetalfedyKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK08213  192 NAIAPGffPT--------KMTRGTLERLGEDLLAHTPLGRLGDDEDLKGAALLLASDASKHITGQILAVDGGVS 257
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 21-254 1.77e-43

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: 148.21  E-value: 1.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPE--AGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRP 98
Cdd:cd05355    41 AVAIAFAREGADVAINYLPEEedDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGKLDILVNNAAYQHPQE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKT-EPAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHD 177
Cdd:cd05355   121 SIEDiTTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGSPHLLDYAATKGAIVAFTRGLSLQLAEKG 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 178 ITVNVVCPGPTETALfedykQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:cd05355   199 IRVNAVAPGPIWTPL-----IPSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQDSSYVTGQVLHVNGGEIIN 270
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
26-253 5.81e-43

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 146.48  E-value: 5.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAgERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPA 105
Cdd:PRK08226   26 FARHGANLILLDISPEI-EKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDILVNNAGVCRLGSFLDMSDE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 106 QWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIAS-DAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVC 184
Cdd:PRK08226  105 DRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSvTGDMVADPGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAIC 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 185 PGPTETALFEDY--KQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK08226  185 PGYVRTPMAESIarQSNPEDPESVLTEMAKAIPLRRLADPLEVGELAAFLASDESSYLTGTQNVIDGGSTL 255
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 21-253 2.15e-42

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: 144.53  E-value: 2.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAgervaAQIRDAGGRALSVRCDITDRASVDAAVaaveQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd05368    17 AIALAFAREGANVIATDINEEK-----LKELERGPGITTRVLDVTDKEQVAALA----KEEGRIDVLFNCAGFVHHGSIL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARV-GSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:cd05368    88 DCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIkGVPNRFVYSTTKAAVIGLTKSVAADFAQQGIR 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 180 VNVVCPGPTETALFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:cd05368   168 CNAICPGTVDTPSLEERIQAQPDPEEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVIDGGWSL 241
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 24-253 2.31e-42

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: 144.98  E-value: 2.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  24 LRFARAGAAVGVLDLNpEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFR-PFVKT 102
Cdd:cd08937    22 ERLAGEGARVLLVDRS-ELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDVLINNVGGTIWAkPYEHY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 103 EPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSsgEAVYAACKGGLVSFSKTIAREHARHDITVNV 182
Cdd:cd08937   101 EEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGIY--RIPYSAAKGGVNALTASLAFEHARDGIRVNA 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 183 VCPGPTET-------ALFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:cd08937   179 VAPGGTEApprkiprNAAPMSEQEKVWYQRIVDQTLDSSLMGRYGTIDEQVRAILFLASDEASYITGTVLPVGGGDLG 256
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 4-254 4.13e-42

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: 144.30  E-value: 4.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIrdaGGRALSVRCDITDRASVDAAVAAVEQELGP 83
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEI---GPAACAISLDVTDQASIDRCVAALVDRWGS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  84 IDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVAR-KAGRIVNIASDAARVGSSGEAVYAACKGGL 162
Cdd:cd05363    78 IDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCATKAAV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 163 VSFSKTIAREHARHDITVNVVCPGPTET-------ALFEDYK-QGAGNPEKLVEAftrSIPLGRIGQPDDLPGAVLFFAG 234
Cdd:cd05363   158 ISLTQSAGLNLIRHGINVNAIAPGVVDGehwdgvdAKFARYEnRPRGEKKRLVGE---AVPFGRMGRAEDLTGMAIFLAS 234

                         250       260
                  ....*....|....*....|
gi 1444067332 235 DDAAFITGQVLSVSGGLTMN 254
Cdd:cd05363   235 TDADYIVAQTYNVDGGNWMS 254
PRK08589 PRK08589
SDR family oxidoreductase;
1-251 6.28e-42

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 144.15  E-value: 6.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAqIRDAGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK08589    1 MKRLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDK-IKSNGGKAKAYHVDISDEQQVKDFASEIKEQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFRPFVKTEPAQ-WERLIAINLTGALHMHHAVLPGMVaRKAGRIVNIASDAARVGSSGEAVYAACK 159
Cdd:PRK08589   80 FGRVDVLFNNAGVDNAAGRIHEYPVDvFDKIMAVDMRGTFLMTKMLLPLMM-EQGGSIINTSSFSGQAADLYRSGYNAAK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 160 GGLVSFSKTIAREHARHDITVNVVCPGPTETALFEDY----KQGAGnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGD 235
Cdd:PRK08589  159 GAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLtgtsEDEAG--KTFRENQKWMTPLGRLGKPEEVAKLVVFLASD 236

                         250
                  ....*....|....*.
gi 1444067332 236 DAAFITGQVLSVSGGL 251
Cdd:PRK08589  237 DSSFITGETIRIDGGV 252
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 23-253 7.29e-42

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 143.64  E-value: 7.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  23 CLRFARAGAAVGVLDLNPEAGERVAAQI--RDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK12384   19 CHGLAEEGYRVAVADINSEKAANVAQEInaEYGEGMAYGFGADATSEQSVLALSRGVDEIFGRVDLLVYNAGIAKAAFIT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARK-AGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK12384   99 DFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEYGIT 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 180 VNVVCPG-----PTETALFEDYKQGAGNPEKLVE-AFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK12384  179 VHSLMLGnllksPMFQSLLPQYAKKLGIKPDEVEqYYIDKVPLKRGCDYQDVLNMLLFYASPKASYCTGQSINVTGGQVM 258
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 1-253 5.93e-41

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 140.91  E-value: 5.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGV-LDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQ 79
Cdd:PRK12935    1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVInYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  80 ELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACK 159
Cdd:PRK12935   81 HFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 160 GGLVSFSKTIAREHARHDITVNVVCPGPTETALFedykqgAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAgDDAAF 239
Cdd:PRK12935  161 AGMLGFTKSLALELAKTNVTVNAICPGFIDTEMV------AEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLC-RDGAY 233

                         250
                  ....*....|....
gi 1444067332 240 ITGQVLSVSGGLTM 253
Cdd:PRK12935  234 ITGQQLNINGGLYM 247
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 4-250 7.99e-41

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: 140.70  E-value: 7.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIrdaGGRALSVRCDITDRASVDAAVAAVEQELGP 83
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQI---AGGALALRVDVTDEQQVAALFERAVEEFGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  84 IDVLVNNAG-WDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGL 162
Cdd:cd08944    78 LDLLVNNAGaMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 163 VSFSKTIAREHARHDITVNVVCPGPTETALFEDYKQG-AGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFIT 241
Cdd:cd08944   158 RNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGfEGALGPGGFHLLIHQLQGRLGRPEDVAAAVVFLLSDDASFIT 237


                  ....*....
gi 1444067332 242 GQVLSVSGG 250
Cdd:cd08944   238 GQVLCVDGG 246
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 1-252 1.05e-40

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 140.64  E-value: 1.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIrdaGGraLSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK06057    2 SQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEV---GG--LFVPTDVTDEDAVNALFDTAAET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGwdvFRP-----FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAV- 154
Cdd:PRK06057   77 YGSVDIAFNNAG---ISPpeddsILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQIs 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 155 YAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKqgAGNPEKLVEAFTRsIPLGRIGQPDDLPGAVLFFAG 234
Cdd:PRK06057  154 YTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELF--AKDPERAARRLVH-VPMGRFAEPEEIAAAVAFLAS 230

                         250
                  ....*....|....*...
gi 1444067332 235 DDAAFITGQVLSVSGGLT 252
Cdd:PRK06057  231 DDASFITASTFLVDGGIS 248
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 21-254 1.79e-40

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: 139.83  E-value: 1.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDaggRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd05341    20 AHARLLVAEGAKVVLSDILDEEGQAAAAELGD---AARFFHLDVTDEDGWTAVVDTAREAFGRLDVLVNNAGILTGGTVE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHD--I 178
Cdd:cd05341    97 TTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASKGAVRGLTKSAALECATQGygI 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 179 TVNVVCPGPTETALFEDY--KQGAGNPEKLVeaftrsiPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:cd05341   177 RVNSVHPGYIYTPMTDELliAQGEMGNYPNT-------PMGRAGEPDEIAYAVVYLASDESSFVTGSELVVDGGYTAG 247
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 26-250 5.74e-40

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: 138.47  E-value: 5.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF-VKTEP 104
Cdd:cd05365    19 LAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILVNNAGGGGPKPFdMPMTE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVC 184
Cdd:cd05365    99 EDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVA 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444067332 185 PGPTETalfeDYKQGAGNPEkLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:cd05365   179 PGAVKT----DALASVLTPE-IERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSGG 239
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 21-253 9.74e-40

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 137.78  E-value: 9.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFRP-- 98
Cdd:PRK08217   20 AMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLNGLINNAG--ILRDgl 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEP---------AQWERLIAINLTG--------ALHMhhavlpgMVARKAGRIVNIASdAARVGSSGEAVYAACKGG 161
Cdd:PRK08217   98 LVKAKDgkvtskmslEQFQSVIDVNLTGvflcgreaAAKM-------IESGSKGVIINISS-IARAGNMGQTNYSASKAG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 162 LVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKqgagnPEKLvEAFTRSIPLGRIGQPDDLPGAVLFFAGDDaaFIT 241
Cdd:PRK08217  170 VAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMK-----PEAL-ERLEKMIPVGRLGEPEEIAHTVRFIIEND--YVT 241

                         250
                  ....*....|..
gi 1444067332 242 GQVLSVSGGLTM 253
Cdd:PRK08217  242 GRVLEIDGGLRL 253
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 21-250 1.22e-39

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 137.77  E-value: 1.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGErVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAG---WdvFR 97
Cdd:PRK12823   23 GVALRAAAEGARVVLVDRSELVHE-VAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDVLINNVGgtiW--AK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  98 PFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARvgSSGEAVYAACKGGLVSFSKTIAREHARHD 177
Cdd:PRK12823  100 PFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIATR--GINRVPYSAAKGGVNALTASLAFEYAEHG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 178 ITVNVVCPGPTE---------TAlfEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVS 248
Cdd:PRK12823  178 IRVNAVAPGGTEapprrvprnAA--PQSEQEKAWYQQIVDQTLDSSLMKRYGTIDEQVAAILFLASDEASYITGTVLPVG 255


                  ..
gi 1444067332 249 GG 250
Cdd:PRK12823  256 GG 257
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 25-250 1.24e-39

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 137.61  E-value: 1.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVldlNPEAGERVAAQIRDAGGraLSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:PRK06463   26 AFLREGAKVAV---LYNSAENEAKELREKGV--FTIKCDVGNRDQVKKSKEVVEKEFGRVDVLVNNAGIMYLMPFEEFDE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAArVGSSGEAV--YAACKGGLVSFSKTIAREHARHDITVNV 182
Cdd:PRK06463  101 EKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAG-IGTAAEGTtfYAITKAGIIILTRRLAFELGKYGIRVNA 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 183 VCPGPTETalfeDYKQGAGNPE---KLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK06463  180 VAPGWVET----DMTLSGKSQEeaeKLRELFRNKTVLKTTGKPEDIANIVLFLASDDARYITGQVIVADGG 246
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 21-250 1.38e-39

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: 137.47  E-value: 1.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGG-RALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVF--- 96
Cdd:cd08930    17 AFCKALLSAGARLILADINAPALEQLKEELTNLYKnRVIALELDITSKESIKELIESYLEKFGRIDILINNAYPSPKvwg 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  97 RPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGE----------AVYAACKGGLVSFS 166
Cdd:cd08930    97 SRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIAPDFRiyentqmyspVEYSVIKAGIIHLT 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 167 KTIAREHARHDITVNVVCPGPTEtalfedykqgAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLS 246
Cdd:cd08930   177 KYLAKYYADTGIRVNAISPGGIL----------NNQPSEFLEKYTKKCPLKRMLNPEDLRGAIIFLLSDASSYVTGQNLV 246


                  ....
gi 1444067332 247 VSGG 250
Cdd:cd08930   247 IDGG 250
PRK06500 PRK06500
SDR family oxidoreductase;
1-250 3.05e-39

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 136.62  E-value: 3.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIrdaGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK06500    1 MSRLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAEL---GESALVIRADAGDVAAQKALAQALAEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPgMVARKAGRIVNiASDAARVGSSGEAVYAACKG 160
Cdd:PRK06500   78 FGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLP-LLANPASIVLN-GSINAHIGMPNSSVYAASKA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 161 GLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFI 240
Cdd:PRK06500  156 ALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATLDAVAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFI 235

                         250
                  ....*....|
gi 1444067332 241 TGQVLSVSGG 250
Cdd:PRK06500  236 VGSEIIVDGG 245
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 4-231 5.13e-39

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: 135.74  E-value: 5.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGP 83
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  84 IDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLV 163
Cdd:cd08934    81 LDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 164 SFSKTIAREHARHDITVNVVCPGPTETALfEDYKQGAGNPEKLVEAFTRSIPLgrigQPDDLPGAVLF 231
Cdd:cd08934   161 AFSEGLRQEVTERGVRVVVIEPGTVDTEL-RDHITHTITKEAYEERISTIRKL----QAEDIAAAVRY 223
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 30-253 1.15e-38

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 135.04  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  30 GAAVGVLDLNPEAGERVAAQIrdaGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQWER 109
Cdd:PRK12936   30 GAIVGLHGTRVEKLEALAAEL---GERVKIFPANLSDRDEVKALGQKAEADLEGVDILVNNAGITKDGLFVRMSDEDWDS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 110 LIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTE 189
Cdd:PRK12936  107 VLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIE 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 190 TALFEDYKqgagnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK12936  187 SAMTGKLN------DKQKEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTIHVNGGMAM 244
PRK06484 PRK06484
short chain dehydrogenase; Validated
 21-252 1.25e-38

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 140.75  E-value: 1.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIrdaGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAG-WDVF-RP 98
Cdd:PRK06484   20 AACQRFARAGDQVVVADRNVERARERADSL---GPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVNNAGvTDPTmTA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGR-IVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHD 177
Cdd:PRK06484   97 TLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKAAVISLTRSLACEWAAKG 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 178 ITVNVVCPGPTETALFEDYKQgAGNPEklVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK06484  177 IRVNAVLPGYVRTQMVAELER-AGKLD--PSAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGSTLVVDGGWT 248
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 21-250 1.30e-38

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: 135.02  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDA-GGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:cd05369    18 AIAKAFAELGASVAIAGRKPEVLEAAAEEISSAtGGRAHPIQCDVRDPEAVEAAVDETLKEFGKIDILINNAAGNFLAPA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKA-GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:cd05369    98 ESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGSPFQVHSAAAKAGVDALTRSLAVEWGPYGI 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 179 TVNVVCPGPTE-TALFEDYkqgaGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:cd05369   178 RVNAIAPGPIPtTEGMERL----APSGKSEKKMIERVPLGRLGTPEEIANLALFLLSDAASYINGTTLVVDGG 246
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 25-251 2.27e-38

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: 134.59  E-value: 2.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:cd08945    22 RLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDVLVNNAGRSGGGATAELAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLP--GMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNV 182
Cdd:cd08945   102 ELWLDVVETNLTGVFRVTKEVLKagGMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGITVNA 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 183 VCPGPTETALFEDYKQGAG-----NPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:cd08945   182 VCPGFVETPMAASVREHYAdiwevSTEEAFDRITARVPLGRYVTPEEVAGMVAYLIGDGAAAVTAQALNVCGGL 255
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 27-251 2.64e-38

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 134.11  E-value: 2.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  27 ARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQ 106
Cdd:PRK08085   30 AEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVLINNAGIQRRHPFTEFPEQE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 107 WERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPG 186
Cdd:PRK08085  110 WNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPG 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 187 PTET----ALFEDykqgagnpeklvEAFT----RSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:PRK08085  190 YFKTemtkALVED------------EAFTawlcKRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFVDGGM 250
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 26-250 1.09e-37

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 132.66  E-value: 1.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFvKTEPA 105
Cdd:PRK06113   31 FATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGKVDILVNNAGGGGPKPF-DMPMA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 106 QWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCP 185
Cdd:PRK06113  110 DFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAP 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 186 GPTETalfeDYKQGAGNPEkLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK06113  190 GAILT----DALKSVITPE-IEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGG 249
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-209 1.20e-37

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 132.12  E-value: 1.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK07666    2 AQSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKG 160
Cdd:PRK07666   82 LGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKF 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1444067332 161 GLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKQGAGNPEKLVEA 209
Cdd:PRK07666  162 GVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDGNPDKVMQP 210
PRK05650 PRK05650
SDR family oxidoreductase;
21-216 3.99e-37

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 131.70  E-value: 3.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK05650   15 AIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVNNAGVASGGFFE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK05650   95 ELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETLLVELADDEIGV 174

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1444067332 181 NVVCPGPTETALFEDYKQGAGNPEKLVEAFTRSIPL 216
Cdd:PRK05650  175 HVVCPSFFQTNLLDSFRGPNPAMKAQVGKLLEKSPI 210
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-254 4.51e-37

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 130.98  E-value: 4.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVgVLDLN--PEAGERVAAQIrdaGGRALSVRCDITDRASVDAAVAAVEQELG-PIDVLVNNAGWD-VFRPFVK 101
Cdd:PRK08642   25 FAREGARV-VVNYHqsEDAAEALADEL---GDRAIALQADVTDREQVQAMFATATEHFGkPITTVVNNALADfSFDGDAR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 102 TEPAQ--WERL---IAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARH 176
Cdd:PRK08642  101 KKADDitWEDFqqqLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHDYTTAKAALLGLTRNLAAELGPY 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 177 DITVNVVCPGptetaLFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:PRK08642  181 GITVNMVSGG-----LLRTTDASAATPDEVFDLIAATTPLRKVTTPQEFADAVLFFASPWARAVTGQNLVVDGGLVMN 253
PRK07577 PRK07577
SDR family oxidoreductase;
62-250 5.03e-37

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 130.23  E-value: 5.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  62 CDITDRASVDAAVAAVeQELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIA 141
Cdd:PRK07577   48 CDLADIEQTAATLAQI-NEIHPVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNIC 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 142 SDAARvGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKQGAGNPEKLVEAftrSIPLGRIGQ 221
Cdd:PRK07577  127 SRAIF-GALDRTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRQTRPVGSEEEKRVLA---SIPMRRLGT 202

                         170       180
                  ....*....|....*....|....*....
gi 1444067332 222 PDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK07577  203 PEEVAAAIAFLLSDDAGFITGQVLGVDGG 231
PRK06484 PRK06484
short chain dehydrogenase; Validated
 25-255 8.38e-37

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 135.75  E-value: 8.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVLDLNPEAGERVAAQirdAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW-DVFRPFVKTE 103
Cdd:PRK06484  288 RFAAAGDRLLIIDRDAEGAKKLAEA---LGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVNNAGIaEVFKPSLEQS 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVV 183
Cdd:PRK06484  365 AEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTV 442

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444067332 184 CPGPTETALFEDYKQGAgnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMNG 255
Cdd:PRK06484  443 APGYIETPAVLALKASG---RADFDSIRRRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTVDGGWTAFG 511
PRK07069 PRK07069
short chain dehydrogenase; Validated
 21-251 1.54e-36

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 129.44  E-value: 1.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAG-ERVAAQIRDAGGR--ALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFR 97
Cdd:PRK07069   14 AIARRMAEQGAKVFLTDINDAAGlDAFAAEINAAHGEgvAFAAVQDVTDEAQWQALLAQAADAMGGLSVLVNNAGVGSFG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  98 PFVKTEPAQWERLIAINLTGA-LHMHHAvLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARH 176
Cdd:PRK07069   94 AIEQIELDEWRRVMAINVESIfLGCKHA-LPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVASLTKSIALDCARR 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 177 --DITVNVVCPGPTETALFEDYKQGAGNpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:PRK07069  173 glDVRCNSIHPTFIRTGIVDPIFQRLGE-EEATRKLARGVPLGRLGEPDDVAHAVLYLASDESRFVTGAELVIDGGI 248
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 26-252 1.67e-36

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


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 129.37  E-value: 1.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAGG-RALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:cd05352    28 LAEAGADVAIIYNSAPRAEEKAEELAKKYGvKTKAYKCDVSSQESVEKTFKQIQKDFGKIDILIANAGITVHKPALDYTY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVG--SSGEAVYAACKGGLVSFSKTIAREHARHDITVNV 182
Cdd:cd05352   108 EQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVnrPQPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNS 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 183 VCPGPTETALfedykqGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:cd05352   188 ISPGYIDTDL------TDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYTTGSDLIIDGGYT 251
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 1-254 1.72e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 129.66  E-value: 1.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK07478    1 MMRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAG-WDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASdaaRVGSS----GEAVY 155
Cdd:PRK07478   81 FGGLDIAFNNAGtLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTST---FVGHTagfpGMAAY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 156 AACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALfedYKQGAGNPEKLveAFTRSI-PLGRIGQPDDLPGAVLFFAG 234
Cdd:PRK07478  158 AASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPM---GRAMGDTPEAL--AFVAGLhALKRMAQPEEIAQAALFLAS 232

                         250       260
                  ....*....|....*....|
gi 1444067332 235 DDAAFITGQVLSVSGGLTMN 254
Cdd:PRK07478  233 DAASFVTGTALLVDGGVSIT 252
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 29-252 2.98e-36

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 129.36  E-value: 2.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  29 AGAAVGVLDLNPEAGErvaaqirdaGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV-KTEP--- 104
Cdd:PRK06171   32 NGANVVNADIHGGDGQ---------HENYQFVPTDVSSAEEVNHTVAEIIEKFGRIDGLVNNAGINIPRLLVdEKDPagk 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 -----AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK06171  103 yelneAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSEGQSCYAATKAALNSFTRSWAKELGKHNIR 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 180 VNVVCPGPTEtalfedyKQGAGNPE----------KLVEAF------TRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQ 243
Cdd:PRK06171  183 VVGVAPGILE-------ATGLRTPEyeealaytrgITVEQLragytkTSTIPLGRSGKLSEVADLVCYLLSDRASYITGV 255


                  ....*....
gi 1444067332 244 VLSVSGGLT 252
Cdd:PRK06171  256 TTNIAGGKT 264
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 21-218 3.16e-36

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: 128.51  E-value: 3.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd05339    14 LLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTILINNAGVVSGKKLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIARE--HARHD- 177
Cdd:cd05339    94 ELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFHESLRLElkAYGKPg 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1444067332 178 ITVNVVCPGPTETALFEDYKQGAG------NPEKLVEAFTRSIPLGR 218
Cdd:cd05339   174 IKTTLVCPYFINTGMFQGVKTPRPllapilEPEYVAEKIVRAILTNQ 220
PRK06123 PRK06123
SDR family oxidoreductase;
21-250 3.26e-36

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 128.74  E-value: 3.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDL-NPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFRPF 99
Cdd:PRK06123   17 ATALLAAERGYAVCLNYLrNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRLDALVNNAG--ILEAQ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTE---PAQWERLIAINLTGALHMHHAVLPGMVARKAGR---IVNIASDAARVGSSGEAV-YAACKGGLVSFSKTIARE 172
Cdd:PRK06123   95 MRLEqmdAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSPGEYIdYAASKGAIDTMTIGLAKE 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 173 HARHDITVNVVCPGptetALFEDYKQGAGNPEKlVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK06123  175 VAAEGIRVNAVRPG----VIYTEIHASGGEPGR-VDRVKAGIPMGRGGTAEEVARAILWLLSDEASYTTGTFIDVSGG 247
PRK07035 PRK07035
SDR family oxidoreductase;
27-252 3.74e-36

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 128.60  E-value: 3.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  27 ARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWD-VFRPFVKTEPA 105
Cdd:PRK07035   29 AQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRLDILVNNAAANpYFGHILDTDLG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 106 QWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCP 185
Cdd:PRK07035  109 AFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAAVISMTKAFAKECAPFGIRVNALLP 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 186 GPTET----ALFEDykqgagnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK07035  189 GLTDTkfasALFKN--------DAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTGECLNVDGGYL 251
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 21-192 4.29e-36

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 128.91  E-value: 4.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIrdagGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK07825   20 ATARALAALGARVAIGDLDEALAKETAAEL----GLVVGGPLDVTDPASFAAFLDAVEADLGPIDVLVNNAGVMPVGPFL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK07825   96 DEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVGFTDAARLELRGTGVHV 175

                         170
                  ....*....|..
gi 1444067332 181 NVVCPGPTETAL 192
Cdd:PRK07825  176 SVVLPSFVNTEL 187
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 23-253 4.31e-36

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: 128.74  E-value: 4.31e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  23 CLRFARAGAAVGVLDLNPEAGERVAAQIR-DAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVK 101
Cdd:cd05322    19 CHGLAEAGYDVAVADINSENAEKVADEINaEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVDLLVYSAGIAKSAKITD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 102 TEPAQWERLIAINLTGALHMHHAVLPGMVARK-AGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:cd05322    99 FELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEHGITV 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444067332 181 NVVCPG-----PTETALFEDYKQGAGNPEKLVEA-FTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:cd05322   179 NSLMLGnllksPMFQSLLPQYAKKLGIKESEVEQyYIDKVPLKRGCDYQDVLNMLLFYASPKASYCTGQSINITGGQVM 257
PRK07454 PRK07454
SDR family oxidoreductase;
21-194 4.52e-36

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 128.15  E-value: 4.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK07454   21 ATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDVLINNAGMAYTGPLL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK07454  101 EMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFTKCLAEEERSHGIRV 180

                         170
                  ....*....|....
gi 1444067332 181 NVVCPGPTETALFE 194
Cdd:PRK07454  181 CTITLGAVNTPLWD 194
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 21-254 5.18e-36

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: 128.34  E-value: 5.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQEL-GPIDVLVNNAGWDVFRPF 99
Cdd:cd05329    21 AIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFgGKLNILVNNAGTNIRKEA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:cd05329   101 KDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGALNQLTRSLACEWAKDNIR 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 180 VNVVCPGPTETALFEDYKQGAGNPEKLVEaftrSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:cd05329   181 VNAVAPWVIATPLVEPVIQQKENLDKVIE----RTPLKRFGEPEEVAALVAFLCMPAASYITGQIIAVDGGLTAN 251
PRK06114 PRK06114
SDR family oxidoreductase;
26-252 6.85e-36

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 127.98  E-value: 6.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAG-ERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:PRK06114   28 LAQAGADVALFDLRTDDGlAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAELGALTLAVNAAGIANANPAEEMEE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSG--EAVYAACKGGLVSFSKTIAREHARHDITVNV 182
Cdd:PRK06114  108 EQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNRGllQAHYNASKAGVIHLSKSLAMEWVGRGIRVNS 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444067332 183 VCPGPTETALfedykqgAGNPE--KLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK06114  188 ISPGYTATPM-------NTRPEmvHQTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAASFCTGVDLLVDGGFV 252
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 21-253 1.10e-35

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: 127.40  E-value: 1.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAqirdAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdvFRPFV 100
Cdd:cd05371    17 ATVERLLAQGAKVVILDLPNSPGETVAK----LGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIVVNCAG---IAVAA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KT---------EPAQWERLIAINLTGALHMHHAVLPGMVARKA------GRIVNIASDAARVGSSGEAVYAACKGGLVSF 165
Cdd:cd05371    90 KTynkkgqqphSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPdqggerGVIINTASVAAFEGQIGQAAYSASKGGIVGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 166 SKTIAREHARHDITVNVVCPGPTETALFedykqgAGNPEKLVEAFTRSIP-LGRIGQPDDLPGAVLFFAgdDAAFITGQV 244
Cdd:cd05371   170 TLPIARDLAPQGIRVVTIAPGLFDTPLL------AGLPEKVRDFLAKQVPfPSRLGDPAEYAHLVQHII--ENPYLNGEV 241


                  ....*....
gi 1444067332 245 LSVSGGLTM 253
Cdd:cd05371   242 IRLDGAIRM 250
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 1-255 1.48e-35

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 127.43  E-value: 1.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIrdaGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK08265    1 MIGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFRPFVKTEpAQWERLIAINLTGALHMHHAVLPGMVARkAGRIVNIASDAARVGSSGEAVYAACKG 160
Cdd:PRK08265   78 FGRVDILVNLACTYLDDGLASSR-ADWLAALDVNLVSAAMLAQAAHPHLARG-GGAIVNFTSISAKFAQTGRWLYPASKA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 161 GLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKQgaGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFI 240
Cdd:PRK08265  156 AIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSG--GDRAKADRVAAPFHLLGRVGDPEEVAQVVAFLCSDAASFV 233

                         250
                  ....*....|....*
gi 1444067332 241 TGQVLSVSGGLTMNG 255
Cdd:PRK08265  234 TGADYAVDGGYSALG 248
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 21-255 2.06e-35

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 127.84  E-value: 2.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEA-GERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:PRK06701   61 AVAVLFAKEGADIAIVYLDEHEdANETKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELGRLDILVNNAAFQYPQQS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VK--TEpAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHD 177
Cdd:PRK06701  141 LEdiTA-EQLDKTFKTNIYSYFHMTKAALPHL--KQGSAIINTGSITGYEGNETLIDYSATKGAIHAFTRSLAQSLVQKG 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 178 ITVNVVCPGPTETALFEdykqgAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMNG 255
Cdd:PRK06701  218 IRVNAVAPGPIWTPLIP-----SDFDEEKVSQFGSNTPMQRPGQPEELAPAYVFLASPDSSYITGQMLHVNGGVIVNG 290
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 21-250 4.00e-35

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: 125.99  E-value: 4.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRA---LSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFR 97
Cdd:cd05364    18 GTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEkkiLLVVADLTEEEGQDRIISTTLAKFGRLDILVNNAGILAKG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  98 PFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKaGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHD 177
Cdd:cd05364    98 GGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYCISKAALDQFTRCTALELAPKG 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 178 ITVNVVCPGPTETalfeDYKQGAGNPEKLVEAFTR----SIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:cd05364   177 VRVNSVSPGVIVT----GFHRRMGMPEEQYIKFLSrakeTHPLGRPGTVDEVAEAIAFLASDASSFITGQLLPVDGG 249
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 1-250 8.34e-35

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 125.78  E-value: 8.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK08277    5 LFSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILED 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAG-----------WDVFRPFVKT----EPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAA 145
Cdd:PRK08277   85 FGPCDILINGAGgnhpkattdneFHELIEPTKTffdlDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 146 RVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPG--PTE---TALF-EDykqgaGNPEKLVEAFTRSIPLGRI 219
Cdd:PRK08277  165 FTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGffLTEqnrALLFnED-----GSLTERANKILAHTPMGRF 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1444067332 220 GQPDDLPGAVLFFAGDDAA-FITGQVLSVSGG 250
Cdd:PRK08277  240 GKPEELLGTLLWLADEKASsFVTGVVLPVDGG 271
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 4-253 1.49e-34

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 124.84  E-value: 1.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVgVLDL--NPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQEL 81
Cdd:PRK08936    5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKV-VINYrsDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  82 GPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVAR-KAGRIVNIASDAARVGSSGEAVYAACKG 160
Cdd:PRK08936   84 GTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPLFVHYAASKG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 161 GLVSFSKTIAREHARHDITVNVVCPGPTETAL----FEDYKQGAGnpeklVEAFtrsIPLGRIGQPDDLPGAVLFFAGDD 236
Cdd:PRK08936  164 GVKLMTETLAMEYAPKGIRVNNIGPGAINTPInaekFADPKQRAD-----VESM---IPMGYIGKPEEIAAVAAWLASSE 235

                         250
                  ....*....|....*..
gi 1444067332 237 AAFITGQVLSVSGGLTM 253
Cdd:PRK08936  236 ASYVTGITLFADGGMTL 252
PRK06398 PRK06398
aldose dehydrogenase; Validated
 1-252 1.66e-34

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 124.56  E-value: 1.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNpEAGERVAAQIRdaggralsvrCDITDRASVDAAVAAVEQE 80
Cdd:PRK06398    1 DLGLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIK-EPSYNDVDYFK----------VDVSNKEQVIKGIDYVISK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKG 160
Cdd:PRK06398   70 YGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKH 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 161 GLVSFSKTIAREHARHdITVNVVCPGPTETALFE--DYKQGAGNPEKL---VEAFTRSIPLGRIGQPDDLPGAVLFFAGD 235
Cdd:PRK06398  150 AVLGLTRSIAVDYAPT-IRCVAVCPGSIRTPLLEwaAELEVGKDPEHVerkIREWGEMHPMKRVGKPEEVAYVVAFLASD 228

                         250
                  ....*....|....*..
gi 1444067332 236 DAAFITGQVLSVSGGLT 252
Cdd:PRK06398  229 LASFITGECVTVDGGLR 245
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 4-252 2.08e-34

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: 124.11  E-value: 2.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRAlsVRCDITDRASVDAAVAAVEQELGP 83
Cdd:cd05326     2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISF--VHCDVTVEADVRAAVDTAVARFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  84 IDVLVNNAGWDVFRPF--VKTEPAQWERLIAINLTGA-LHMHHAVlPGMVARKAGRIVNIASDAARVGSSGEAVYAACKG 160
Cdd:cd05326    80 LDIMFNNAGVLGAPCYsiLETSLEEFERVLDVNVYGAfLGTKHAA-RVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 161 GLVSFSKTIAREHARHDITVNVVCPGPTETALFedyKQGAGNPEKLVEAFTRSI--PLGRIGQPDDLPGAVLFFAGDDAA 238
Cdd:cd05326   159 AVLGLTRSAATELGEHGIRVNCVSPYGVATPLL---TAGFGVEDEAIEEAVRGAanLKGTALRPEDIAAAVLYLASDDSR 235

                         250
                  ....*....|....
gi 1444067332 239 FITGQVLSVSGGLT 252
Cdd:cd05326   236 YVSGQNLVVDGGLT 249
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 26-251 3.74e-34

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 123.58  E-value: 3.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAA-VGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:PRK06198   26 FAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRLDALVNAAGLTDRGTILDTSP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKA-GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVV 183
Cdd:PRK06198  106 ELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAAYCASKGALATLTRNAAYALLRNRIRVNGL 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 184 CPGPTETAlFEDYKQGA--GNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVL----SVSGGL 251
Cdd:PRK06198  186 NIGWMATE-GEDRIQREfhGAPDDWLEKAAATQPFGRLLDPDEVARAVAFLLSDESGLMTGSVIdfdqSVWGAY 258
PRK07814 PRK07814
SDR family oxidoreductase;
21-253 3.91e-34

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 123.74  E-value: 3.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK07814   25 AIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDIVVNNVGGTMPNPLL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARK-AGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHdIT 179
Cdd:PRK07814  105 STSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYGTAKAALAHYTRLAALDLCPR-IR 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 180 VNVVCPGPTETALFEDYkqgAGNPEkLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK07814  184 VNAIAPGSILTSALEVV---AANDE-LRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKTLEVDGGLTF 253
PRK12743 PRK12743
SDR family oxidoreductase;
21-255 5.79e-34

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 123.22  E-value: 5.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAG-ERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:PRK12743   17 ACALLLAQQGFDIGITWHSDEEGaKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRIDVLVNNAGAMTKAPF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGA-LHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK12743   97 LDMDFDEWRKIFTVDVDGAfLCSQIAARHMVKQGQGGRIINITSVHEHTPLPGASAYTAAKHALGGLTKAMALELVEHGI 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 179 TVNVVCPGPTETALfedYKQGAGNPEklvEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMNG 255
Cdd:PRK12743  177 LVNAVAPGAIATPM---NGMDDSDVK---PDSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSLIVDGGFMLAN 247
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 27-252 6.23e-34

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 122.95  E-value: 6.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  27 ARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQ 106
Cdd:PRK07523   31 AQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDILVNNAGMQFRTPLEDFPADA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 107 WERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPG 186
Cdd:PRK07523  111 FERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAPG 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 187 ----PTETALFEDykqgagnpeklvEAFT----RSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK07523  191 yfdtPLNAALVAD------------PEFSawleKRTPAGRWGKVEELVGACVFLASDASSFVNGHVLYVDGGIT 252
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-251 2.99e-33

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 120.67  E-value: 2.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVrcDITDRASVDAAVAAVEQE 80
Cdd:PRK12828    2 EHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGI--DLVDPQAARRAVDEVNRQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKG 160
Cdd:PRK12828   80 FGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 161 GLVSFSKTIAREHARHDITVNVVCPGPTETALFEdykqgagnPEKLVEAFTRSIplgrigQPDDLPGAVLFFAGDDAAFI 240
Cdd:PRK12828  160 GVARLTEALAAELLDRGITVNAVLPSIIDTPPNR--------ADMPDADFSRWV------TPEQIAAVIAFLLSDEAQAI 225

                         250
                  ....*....|.
gi 1444067332 241 TGQVLSVSGGL 251
Cdd:PRK12828  226 TGASIPVDGGV 236
PRK06949 PRK06949
SDR family oxidoreductase;
27-251 1.39e-32

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 119.48  E-value: 1.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  27 ARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQ 106
Cdd:PRK06949   30 AQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGTIDILVNNSGVSTTQKLVDVTPAD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 107 WERLIAINLTGALHMHHAVLPGMVAR--------KAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK06949  110 FDFVFDTNTRGAFFVAQEVAKRMIARakgagntkPGGRIINIASVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGI 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 179 TVNVVCPGPTETALFEDYKQGAGNpEKLVEAFTRSiplgRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:PRK06949  190 NVNAICPGYIDTEINHHHWETEQG-QKLVSMLPRK----RVGKPEDLDGLLLLLAADESQFINGAIISADDGF 257
PRK05867 PRK05867
SDR family oxidoreductase;
24-252 1.64e-32

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 119.37  E-value: 1.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  24 LRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTE 103
Cdd:PRK05867   27 LAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDIAVCNAGIITVTPMLDMP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMHHAVLPGMVAR-KAGRIVNIASDAARVGSSGEAV--YAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK05867  107 LEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGHIINVPQQVshYCASKAAVIHLTKAMAVELAPHKIRV 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 181 NVVCPGPTETALFE---DYKQgagnpeklveAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK05867  187 NSVSPGYILTELVEpytEYQP----------LWEPKIPLGRLGRPEELAGLYLYLASEASSYMTGSDIVIDGGYT 251
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 2-250 7.31e-32

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: 117.94  E-value: 7.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   2 QGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQEL 81
Cdd:cd08935     1 FSLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  82 GPIDVLVNNAG--------------WDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARV 147
Cdd:cd08935    81 GTVDILINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNAFS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 148 GSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALFED--YKQgAGNPEKLVEAFTRSIPLGRIGQPDDL 225
Cdd:cd08935   161 PLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKllINP-DGSYTDRSNKILGRTPMGRFGKPEEL 239

                         250       260
                  ....*....|....*....|....*.
gi 1444067332 226 PGAVLFFAGDDAA-FITGQVLSVSGG 250
Cdd:cd08935   240 LGALLFLASEKASsFVTGVVIPVDGG 265
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
21-253 7.59e-32

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 117.42  E-value: 7.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVgVLDLNPEAGERVA--AQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRP 98
Cdd:PRK12938   18 SICQRLHKDGFKV-VAGCGPNSPRRVKwlEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDVLVNNAGITRDVV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK12938   97 FRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIHGFTMSLAQEVATKGV 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 179 TVNVVCPGPTETALFEDYKQgagnpeKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK12938  177 TVNTVSPGYIGTDMVKAIRP------DVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGADFSLNGGLHM 245
PRK09730 PRK09730
SDR family oxidoreductase;
21-250 9.47e-32

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 116.87  E-value: 9.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGV-LDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:PRK09730   16 ATALLLAQEGYTVAVnYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLAALVNNAGILFTQCT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQ-WERLIAINLTGALHMHHAVLPGMVAR---KAGRIVNIASDAARVGSSGEAV-YAACKGGLVSFSKTIAREHA 174
Cdd:PRK09730   96 VENLTAErINRVLSTNVTGYFLCCREAVKRMALKhggSGGAIVNVSSAASRLGAPGEYVdYAASKGAIDTLTTGLSLEVA 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444067332 175 RHDITVNVVCPGPTETALFEDykqgAGNPEKlVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK09730  176 AQGIRVNCVRPGFIYTEMHAS----GGEPGR-VDRVKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTGSFIDLAGG 246
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 21-252 1.02e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 116.74  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIrdaGGRALSVrcDITDRASVDAAVaaveQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK07060   24 ACAVALAQRGARVVAAARNAAALDRLAGET---GCEPLRL--DVGDDAAIRAAL----AAAGAFDGLVNCAGIASLESAL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVA-RKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK07060   95 DMTAEGFDRVMAVNARGAALVARHVARAMIAaGRGGSIVNVSSQAALVGLPDHLAYCASKAALDAITRVLCVELGPHGIR 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 180 VNVVCPGPTETALFEdykQGAGNPEKlVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK07060  175 VNSVNPTVTLTPMAA---EAWSDPQK-SGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLPVDGGYT 243
PRK09242 PRK09242
SDR family oxidoreductase;
21-255 1.47e-31

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 116.77  E-value: 1.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDA--GGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRP 98
Cdd:PRK09242   24 AIAREFLGLGADVLIVARDADALAQARDELAEEfpEREVHGLAADVSDDEDRRAILDWVEDHWDGLHILVNNAGGNIRKA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK09242  104 AIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKAALLQMTRNLAVEWAEDGI 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 179 TVNVVCPGPTETALFEDYKQgagNPEKLVEAFTRSiPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMNG 255
Cdd:PRK09242  184 RVNAVAPWYIRTPLTSGPLS---DPDYYEQVIERT-PMRRVGEPEEVAAAVAFLCMPAASYITGQCIAVDGGFLRYG 256
PRK06181 PRK06181
SDR family oxidoreductase;
21-203 1.60e-31

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 117.00  E-value: 1.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK06181   16 ALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDILVNNAGITMWSRFD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTE-PAQWERLIAINLTGALHMHHAVLPGMVARKaGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK06181   96 ELTdLSVFERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGYAASKHALHGFFDSLRIELADDGVA 174

                         170       180
                  ....*....|....*....|....
gi 1444067332 180 VNVVCPGPTETALFEDYKQGAGNP 203
Cdd:PRK06181  175 VTVVCPGFVATDIRKRALDGDGKP 198
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 41-194 3.04e-31

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: 115.43  E-value: 3.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  41 EAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALH 120
Cdd:cd08939    40 EAVEEIEAEANASGQKVSYISADLSDYEEVEQAFAQAVEKGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLN 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 121 MHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALFE 194
Cdd:cd08939   120 VAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFE 193
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 21-195 3.14e-31

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 115.48  E-value: 3.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW--DVFRP 98
Cdd:cd05323    15 ATAKLLLKKGAKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDILINNAGIldEKSYL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKA---GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREH-A 174
Cdd:cd05323    95 FAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKGgkgGVIVNIGSVAGLYPAPQFPVYSASKHGVVGFTRSLADLLeY 174

                         170       180
                  ....*....|....*....|.
gi 1444067332 175 RHDITVNVVCPGPTETALFED 195
Cdd:cd05323   175 KTGVRVNAICPGFTNTPLLPD 195
PRK07856 PRK07856
SDR family oxidoreductase;
25-250 7.05e-31

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 114.65  E-value: 7.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVLDLNPEAgervaaqirDAGGRALS-VRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTE 103
Cdd:PRK07856   25 AFLAAGATVVVCGRRAPE---------TVDGRPAEfHAADVRDPDQVAALVDAIVERHGRLDVLVNNAGGSPYALAAEAS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMHHAVLPGMVARKA-GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARhDITVNV 182
Cdd:PRK07856   96 PRFHEKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNLTRSLAVEWAP-KVRVNA 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 183 VCPGPTETALFEDYKQGAGNpeklVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK07856  175 VVVGLVRTEQSELHYGDAEG----IAAVAATVPLGRLATPADIAWACLFLASDLASYVSGANLEVHGG 238
PRK06128 PRK06128
SDR family oxidoreductase;
21-251 1.15e-30

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 115.34  E-value: 1.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVgVLDLNPEA---GERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFR 97
Cdd:PRK06128   70 ATAIAFAREGADI-ALNYLPEEeqdAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGLDILVNIAGKQTAV 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  98 PFV-KTEPAQWERLIAINLTGALHMHHAVLPGMVArkAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARH 176
Cdd:PRK06128  149 KDIaDITTEQFDATFKTNVYAMFWLCKAAIPHLPP--GASIINTGSIQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEK 226

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 177 DITVNVVCPGPTETALfedyKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:PRK06128  227 GIRVNAVAPGPVWTPL----QPSGGQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLASQESSYVTGEVFGVTGGL 297
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 21-254 1.23e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 114.39  E-value: 1.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK07677   16 AMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDALINNAAGNFICPAE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKA-GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHAR-HDI 178
Cdd:PRK07677   96 DLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIkGNIINMVATYAWDAGPGVIHSAAAKAGVLAMTRTLAVEWGRkYGI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 179 TVNVVCPGPTETA-----LFEDykqgagnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK07677  176 RVNAIAPGPIERTggadkLWES--------EEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYINGTCITMDGGQWL 247


                  .
gi 1444067332 254 N 254
Cdd:PRK07677  248 N 248
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 21-250 1.91e-30

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 113.77  E-value: 1.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAG--GRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFR- 97
Cdd:cd05330    18 ATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIApdAEVLLIKADVSDEAQVEAYVDATVEQFGRIDGFFNNAGIEGKQn 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  98 PFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHD 177
Cdd:cd05330    98 LTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVVGLTRNSAVEYGQYG 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 178 ITVNVVCPGPTETALFED-YKQ-GAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:cd05330   178 IRINAIAPGAILTPMVEGsLKQlGPENPEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDDAGYVNAAVVPIDGG 252
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 21-253 6.06e-30

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 112.36  E-value: 6.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAG-ERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFR-- 97
Cdd:PRK12745   17 GIARALAAAGFDLAINDRPDDEElAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRIDCLVNNAGVGVKVrg 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  98 PFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGR------IVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAR 171
Cdd:PRK12745   97 DLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelphrsIVFVSSVNAIMVSPNRGEYCISKAGLSMAAQLFAA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 172 EHARHDITVNVVCPGPTETALfedykqGAGNPEKLVEAFTRSI-PLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK12745  177 RLAEEGIGVYEVRPGLIKTDM------TAPVTAKYDALIAKGLvPMPRWGEPEDVARAVAALASGDLPYSTGQAIHVDGG 250


                  ...
gi 1444067332 251 LTM 253
Cdd:PRK12745  251 LSI 253
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
27-250 9.81e-30

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 112.14  E-value: 9.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  27 ARAGAAVGVLDLNPEAGErVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQ 106
Cdd:PRK06935   36 AKAGADIIITTHGTNWDE-TRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDILVNNAGTIRRAPLLEYKDED 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 107 WERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPG 186
Cdd:PRK06935  115 WNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPG 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 187 PTETA----LFEDYKQgagNPEKLveaftRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK06935  195 YIKTAntapIRADKNR---NDEIL-----KRIPAGRWGEPDDLMGAAVFLASRASDYVNGHILAVDGG 254
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 26-255 1.14e-29

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: 111.86  E-value: 1.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAG-GRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDV-FRPFVKTE 103
Cdd:cd08933    29 FVENGAKVVFCARGEAAGQALESELNRAGpGSCKFVPCDVTKEEDIKTLISVTVERFGRIDCLVNNAGWHPpHQTTDETS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMHHAVLPGMVARKaGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVV 183
Cdd:cd08933   109 AQEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLSSLVGSIGQKQAAPYVATKGAITAMTKALAVDESRYGVRVNCI 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444067332 184 CPGPTETALFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGdDAAFITGQVLSVSGGLTMNG 255
Cdd:cd08933   188 SPGNIWTPLWEELAAQTPDTLATIKEGELAQLLGRMGTEAESGLAALFLAA-EATFCTGIDLLLSGGAELGY 258
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 21-250 1.20e-29

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 111.65  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDL---------NPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAaveQELGPIDVLVNNA 91
Cdd:cd05353    20 AYALAFAERGAKVVVNDLggdrkgsgkSSSAADKVVDEIKAAGGKAVANYDSVEDGEKIVKTAI---DAFGRVDILVNNA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  92 GWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAR 171
Cdd:cd05353    97 GILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGNFGQANYSAAKLGLLGLSNTLAI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 172 EHARHDITVNVVCPGP----TETALfedykqgagnPEKLVEAFtrsiplgrigQPDDLPGAVLFFAGDDAAfITGQVLSV 247
Cdd:cd05353   177 EGAKYNITCNTIAPAAgsrmTETVM----------PEDLFDAL----------KPEYVAPLVLYLCHESCE-VTGGLFEV 235


                  ...
gi 1444067332 248 SGG 250
Cdd:cd05353   236 GAG 238
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
21-253 4.30e-29

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 110.19  E-value: 4.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDL-NPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:PRK08063   19 AIALRLAEEGYDIAVNYArSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLDVFVNNAASGVLRPA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIAS-DAARVGSSGEAVyAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK08063   99 MELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSlGSIRYLENYTTV-GVSKAALEALTRYLAVELAPKGI 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 179 TVNVVCPGPTETalfeDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK08063  178 AVNAVSGGAVDT----DALKHFPNREELLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMIRGQTIIVDGGRSL 248
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 21-250 5.38e-29

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: 109.87  E-value: 5.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQirDAGGRALSVrcDITDRASVDAAVAAveqeLGPIDVLVNNAGWDVFRPFV 100
Cdd:cd05351    22 ATVKALAKAGARVVAVSRTQADLDSLVRE--CPGIEPVCV--DLSDWDATEEALGS----VGPVDLLVNNAAVAILQPFL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKA-GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:cd05351    94 EVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQRALTNHTVYCSTKAALDMLTKVMALELGPHKIR 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 180 VNVVCPGPTETALFEDykqGAGNPEKLVEAFTRsIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:cd05351   174 VNSVNPTVVMTDMGRD---NWSDPEKAKKMLNR-IPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDGG 240
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-253 5.96e-29

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 109.28  E-value: 5.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAgervaaqirDAGGRALSVRCDITDRASVDAavaaveQELGPIDVLVNNAG-WDVFRPFVKTEP 104
Cdd:PRK06550   25 FLAQGAQVYGVDKQDKP---------DLSGNFHFLQLDLSDDLEPLF------DWVPSVDILCNTAGiLDDYKPLLDTSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVC 184
Cdd:PRK06550   90 EEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGFTKQLALDYAKDGIQVFGIA 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 185 PGPTETAL----FEdykqgagnPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK06550  170 PGAVKTPMtaadFE--------PGGLADWVARETPIKRWAEPEEVAELTLFLASGKADYMQGTIVPIDGGWTL 234
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 24-255 6.01e-29

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 110.04  E-value: 6.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  24 LRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTE 103
Cdd:PRK07576   27 QAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPIDVLVSGAAGNFPAPAAGMS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMHHAVLPGMvARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVV 183
Cdd:PRK07576  107 ANGFKTVVDIDLLGTFNVLKAAYPLL-RRPGASIIQISAPQAFVPMPMQAHVCAAKAGVDMLTRTLALEWGPEGIRVNSI 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444067332 184 CPGPTETAlfEDYKQGAGNPEkLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMNG 255
Cdd:PRK07576  186 VPGPIAGT--EGMARLAPSPE-LQAAVAQSVPLKRNGTKQDIANAALFLASDMASYITGVVLPVDGGWSLGG 254
PRK07832 PRK07832
SDR family oxidoreductase;
21-194 6.15e-29

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 110.13  E-value: 6.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGR-ALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:PRK07832   15 ATALRLAAQGAELFLTDRDADGLAQTVADARALGGTvPEHRALDISDYDAVAAFAADIHAAHGSMDVVMNIAGISAWGTV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMV-ARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK07832   95 DRLTHEQWRRMVDVNLMGPIHVIETFVPPMVaAGRGGHLVNVSSAAGLVALPWHAAYSASKFGLRGLSEVLRFDLARHGI 174

                         170
                  ....*....|....*.
gi 1444067332 179 TVNVVCPGPTETALFE 194
Cdd:PRK07832  175 GVSVVVPGAVKTPLVN 190
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 21-250 8.10e-29

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: 109.40  E-value: 8.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRdAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd08943    16 AIAKRLAAEGAAVVVADIDPEIAEKVAEAAQ-GGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIVVSNAGIATSSPIA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGM-VARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:cd08943    95 ETSLEDWNRSMDINLTGHFLVSREAFRIMkSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLARCLALEGGEDGIR 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 180 VNVVCP-------GPTETALFEDYkqgAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:cd08943   175 VNTVNPdavfrgsKIWEGVWRAAR---AKAYGLLEEEYRTRNLLKREVLPEDVAEAVVAMASEDFGKTTGAIVTVDGG 249
PRK05855 PRK05855
SDR family oxidoreductase;
15-190 1.96e-28

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 113.15  E-value: 1.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  15 GGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWD 94
Cdd:PRK05855  324 GSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDIVVNNAGIG 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  95 VFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVAR-KAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREH 173
Cdd:PRK05855  404 MAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERgTGGHIVNVASAAAYAPSRSLPAYATSKAAVLMLSECLRAEL 483

                         170
                  ....*....|....*..
gi 1444067332 174 ARHDITVNVVCPGPTET 190
Cdd:PRK05855  484 AAAGIGVTAICPGFVDT 500
PRK06947 PRK06947
SDR family oxidoreductase;
21-250 2.20e-28

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 108.35  E-value: 2.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDL-NPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDV-FRP 98
Cdd:PRK06947   17 ATAVLAAARGWSVGINYArDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRLDALVNNAGIVApSMP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALhmhhavlpgMVARKAGR------------IVNIASDAARVGSSGEAV-YAACKGGLVSF 165
Cdd:PRK06947   97 LADMDAARLRRMFDTNVLGAY---------LCAREAARrlstdrggrggaIVNVSSIASRLGSPNEYVdYAGSKGAVDTL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 166 SKTIAREHARHDITVNVVCPGPTETalfeDYKQGAGNPEKlVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVL 245
Cdd:PRK06947  168 TLGLAKELGPHGVRVNAVRPGLIET----EIHASGGQPGR-AARLGAQTPLGRAGEADEVAETIVWLLSDAASYVTGALL 242


                  ....*
gi 1444067332 246 SVSGG 250
Cdd:PRK06947  243 DVGGG 247
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 21-253 2.77e-28

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: 108.32  E-value: 2.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDL-NPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDV--FR 97
Cdd:cd05337    16 AIATELAARGFDIAINDLpDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDCLVNNAGIAVrpRG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  98 PFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKA------GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAR 171
Cdd:cd05337    96 DLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSINAYLVSPNRGEYCISKAGLSMATRLLAY 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 172 EHARHDITVNVVCPGPTETALFEDYKQgagNPEKLVEAftRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:cd05337   176 RLADEGIAVHEIRPGLIHTDMTAPVKE---KYDELIAA--GLVPIRRWGQPEDIAKAVRTLASGLLPYSTGQPINIDGGL 250


                  ..
gi 1444067332 252 TM 253
Cdd:cd05337   251 SM 252
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 26-190 3.16e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 108.46  E-value: 3.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAgAAVGVLDlnpeAGERVAAQIRDA----------GGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDV 95
Cdd:PRK06180   16 FGRA-LAQAALA----AGHRVVGTVRSEaaradfealhPDRALARLLDVTDFDAIDAVVADAEATFGPIDVLVNNAGYGH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  96 FRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHAR 175
Cdd:PRK06180   91 EGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKEVAP 170

                         170
                  ....*....|....*
gi 1444067332 176 HDITVNVVCPGPTET 190
Cdd:PRK06180  171 FGIHVTAVEPGSFRT 185
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 26-229 3.31e-28

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 107.06  E-value: 3.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAgervAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPA 105
Cdd:cd08932    20 LARDGYRVSLGLRNPED----LAALSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHNAGIGRPTTLREGSDA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 106 QWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCP 185
Cdd:cd08932    96 ELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHALRQEGWDHGVRVSAVCP 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1444067332 186 GPTETALFEdykqgagnpeklVEAFTRSIPLGRIGQPDDLPGAV 229
Cdd:cd08932   176 GFVDTPMAQ------------GLTLVGAFPPEEMIQPKDIANLV 207
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 26-250 5.06e-28

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 107.18  E-value: 5.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIrDAGGRALSVRCDI-TDRASVDAAVAAVEQElGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:cd08942    26 FLEAGARVIISARKAEACADAAEEL-SAYGECIAIPADLsSEEGIEALVARVAERS-DRLDVLVNNAGATWGAPLEAFPE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPgmVARKAG------RIVNIASDAARVGSSGEAV-YAACKGGLVSFSKTIAREHARHD 177
Cdd:cd08942   104 SGWDKVMDINVKSVFFLTQALLP--LLRAAAtaenpaRVINIGSIAGIVVSGLENYsYGASKAAVHQLTRKLAKELAGEH 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 178 ITVNVVCPGPTETALFEDykqgAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:cd08942   182 ITVNAIAPGRFPSKMTAF----LLNDPAALEAEEKSIPLGRWGRPEDMAGLAIMLASRAGAYLTGAVIPVDGG 250
PRK07326 PRK07326
SDR family oxidoreductase;
1-231 5.70e-28

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 106.63  E-value: 5.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRdAGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK07326    1 MMSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELN-NKGNVLGLAADVRDEADVQRAVDAIVAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMvARKAGRIVNIASDAARVGSSGEAVYAACKG 160
Cdd:PRK07326   80 FGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL-KRGGGYIINISSLAGTNFFAGGAAYNASKF 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 161 GLVSFSKTIAREHARHDITVNVVCPGPTETAlFEDYKQGAGNPEKLveaftrsiplgrigQPDDLPGAVLF 231
Cdd:PRK07326  159 GLVGFSEAAMLDLRQYGIKVSTIMPGSVATH-FNGHTPSEKDAWKI--------------QPEDIAQLVLD 214
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 21-233 7.33e-28

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: 106.98  E-value: 7.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDA-GGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdvfrpF 99
Cdd:cd05346    15 ATARRFAKAGAKLILTGRRAERLQELADELGAKfPVKVLPLQLDVSDRESIEAALENLPEEFRDIDILVNNAG------L 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VK-TEPAQ------WERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIARE 172
Cdd:cd05346    89 ALgLDPAQeadledWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQFSLNLRKD 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 173 HARHDITVNVVCPGPTETAL----FEDYKQGAGNPEKLVEAFTrsiplgrigqPDDLPGAVLFFA 233
Cdd:cd05346   169 LIGTGIRVTNIEPGLVETEFslvrFHGDKEKADKVYEGVEPLT----------PEDIAETILWVA 223
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 21-252 7.77e-28

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: 106.51  E-value: 7.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDaggRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd09761    16 QICLDFLEAGDKVVFADIDEERGADFAEAEGP---NLFFVHGDVADETLVKFVVYAMLEKLGRIDVLVNNAARGSKGILS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKaGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARhDITV 180
Cdd:cd09761    93 SLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAASKGGLVALTHALAMSLGP-DIRV 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444067332 181 NVVCPGPTETAlfedyKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:cd09761   171 NCISPGWINTT-----EQQEFTAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIVDGGMT 237
PRK07831 PRK07831
SDR family oxidoreductase;
21-248 8.09e-28

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 107.04  E-value: 8.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNP----EAGERVAAQirDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVF 96
Cdd:PRK07831   33 ATARRALEEGARVVISDIHErrlgETADELAAE--LGLGRVEAVVCDVTSEAQVDALIDAAVERLGRLDVLVNNAGLGGQ 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  97 RPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARK-AGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHAR 175
Cdd:PRK07831  111 TPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGhGGVIVNNASVLGWRAQHGQAHYAAAKAGVMALTRCSALEAAE 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 176 HDITVNVVCPgptETALFEDYKQGAgnPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVS 248
Cdd:PRK07831  191 YGVRINAVAP---SIAMHPFLAKVT--SAELLDELAAREAFGRAAEPWEVANVIAFLASDYSSYLTGEVVSVS 258
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 45-250 1.02e-27

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 106.79  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  45 RVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHA 124
Cdd:PRK12859   58 QLQEELLKNGVKVSSMELDLTQNDAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQ 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 125 VLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETA-LFEDYKQGagnp 203
Cdd:PRK12859  138 FARGFDKKSGGRIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGwMTEEIKQG---- 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1444067332 204 ekLVEAFtrsiPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK12859  214 --LLPMF----PFGRIGEPKDAARLIKFLASEEAEWITGQIIHSEGG 254
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 21-195 2.23e-27

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 105.39  E-value: 2.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAgerVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd05374    15 ALALALAAQGYRVIATARNPDK---LESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNNAGYGLFGPLE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:cd05374    92 ETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESLRLELAPFGIKV 171

                         170
                  ....*....|....*
gi 1444067332 181 NVVCPGPTETALFED 195
Cdd:cd05374   172 TIIEPGPVRTGFADN 186
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 21-250 4.21e-27

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 105.16  E-value: 4.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGE-----------RVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVN 89
Cdd:PRK12748   22 AVCRRLAAKGIDIFFTYWSPYDKTmpwgmhdkepvLLKEEIESYGVRCEHMEIDLSQPYAPNRVFYAVSERLGDPSILIN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  90 NAGWDVFRPFVKTEPAQWERLIAIN------LTGALHMHHAVLPGmvarkaGRIVNIASDAARVGSSGEAVYAACKGGLV 163
Cdd:PRK12748  102 NAAYSTHTRLEELTAEQLDKHYAVNvratmlLSSAFAKQYDGKAG------GRIINLTSGQSLGPMPDELAYAATKGAIE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 164 SFSKTIAREHARHDITVNVVCPGPTETALFEdykqgagnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQ 243
Cdd:PRK12748  176 AFTKSLAPELAEKGITVNAVNPGPTDTGWIT---------EELKHHLVPKFPQGRVGEPVDAARLIAFLVSEEAKWITGQ 246


                  ....*..
gi 1444067332 244 VLSVSGG 250
Cdd:PRK12748  247 VIHSEGG 253
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 21-194 5.04e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 106.54  E-value: 5.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK07109   23 ATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGPIDTWVNNAMVTVFGPFE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIARE--HARHDI 178
Cdd:PRK07109  103 DVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFTDSLRCEllHDGSPV 182

                         170
                  ....*....|....*.
gi 1444067332 179 TVNVVCPGPTETALFE 194
Cdd:PRK07109  183 SVTMVQPPAVNTPQFD 198
PRK07062 PRK07062
SDR family oxidoreductase;
21-251 5.08e-27

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 105.12  E-value: 5.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIR--DAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRP 98
Cdd:PRK07062   23 ATVELLLEAGASVAICGRDEERLASAEARLRekFPGARLLAARCDVLDEADVAAFAAAVEARFGGVDMLVNNAGQGRVST 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK07062  103 FADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAARAGLLNLVKSLATELAPKGV 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444067332 179 TVNVVCPGPTETALFEDYKQGAGNPEKLVEAFT------RSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:PRK07062  183 RVNSILLGLVESGQWRRRYEARADPGQSWEAWTaalarkKGIPLGRLGRPDEAARALFFLASPLSSYTTGSHIDVSGGF 261
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 21-250 5.42e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 104.60  E-value: 5.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAV-----GVLDLNPEAGERVAAQIRDAGGRALSVRcditdrasvdaavaAVEQELGPIDVLVNNAGWDV 95
Cdd:PRK06523   24 ATVARLLEAGARVvttarSRPDDLPEGVEFVAADLTTAEGCAAVAR--------------AVLERLGGVDILVHVLGGSS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  96 FRP--FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASdAARVGSSGEAV--YAACKGGLVSFSKTIAR 171
Cdd:PRK06523   90 APAggFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTS-IQRRLPLPESTtaYAAAKAALSTYSKSLSK 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 172 EHARHDITVNVVCPGPTET----ALFEDYKQGAGNPE----KLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQ 243
Cdd:PRK06523  169 EVAPKGVRVNTVSPGWIETeaavALAERLAEAAGTDYegakQIIMDSLGGIPLGRPAEPEEVAELIAFLASDRAASITGT 248


                  ....*..
gi 1444067332 244 VLSVSGG 250
Cdd:PRK06523  249 EYVIDGG 255
PRK12746 PRK12746
SDR family oxidoreductase;
1-253 9.64e-27

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 103.96  E-value: 9.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGV-LDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQ 79
Cdd:PRK12746    1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  80 EL------GPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPgmVARKAGRIVNIASDAARVGSSGEA 153
Cdd:PRK12746   81 ELqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLP--LLRAEGRVINISSAEVRLGFTGSI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 154 VYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETalfeDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFA 233
Cdd:PRK12746  159 AYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKT----DINAKLLDDPEIRNFATNSSVFGRIGQVEDIADAVAFLA 234

                         250       260
                  ....*....|....*....|
gi 1444067332 234 GDDAAFITGQVLSVSGGLTM 253
Cdd:PRK12746  235 SSDSRWVTGQIIDVSGGFCL 254
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 21-194 9.89e-27

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: 103.62  E-value: 9.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd05360    15 ATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTWVNNAGVAVFGRFE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIARE--HARHDI 178
Cdd:cd05360    95 DVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESLRAElaHDGAPI 174

                         170
                  ....*....|....*.
gi 1444067332 179 TVNVVCPGPTETALFE 194
Cdd:cd05360   175 SVTLVQPTAMNTPFFG 190
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
15-251 1.08e-26

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 108.39  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  15 GGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAgGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWD 94
Cdd:PRK08324  431 AGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGP-DRALGVACDVTDEAAVQAAFEEAALAFGGVDIVVSNAGIA 509

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  95 VFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAG-RIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREH 173
Cdd:PRK08324  510 ISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGgSIVFIASKNAVNPGPNFGAYGAAKAAELHLVRQLALEL 589

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 174 ARHDITVNVVCP----------------------GPTETALFEDYKQgagnpeklveaftRSIpLGRIGQPDDLPGAVLF 231
Cdd:PRK08324  590 GPDGIRVNGVNPdavvrgsgiwtgewiearaaayGLSEEELEEFYRA-------------RNL-LKREVTPEDVAEAVVF 655

                         250       260
                  ....*....|....*....|
gi 1444067332 232 FAGDDAAFITGQVLSVSGGL 251
Cdd:PRK08324  656 LASGLLSKTTGAIITVDGGN 675
PRK08628 PRK08628
SDR family oxidoreductase;
24-252 3.06e-26

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 102.73  E-value: 3.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  24 LRFARAGAAVGVLDLNPEAGErVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAG----------W 93
Cdd:PRK08628   25 LRLAEEGAIPVIFGRSAPDDE-FAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGLVNNAGvndgvgleagR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  94 DVFRpfvktepAQWERliaiNLTGALHMHHAVLPGMVARKaGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREH 173
Cdd:PRK08628  104 EAFV-------ASLER----NLIHYYVMAHYCLPHLKASR-GAIVNISSKTALTGQGGTSGYAAAKGAQLALTREWAVAL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 174 ARHDITVNVVCPGPTETALFEDYKQGAGNPEKLVEAFTRSIPLG-RIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK08628  172 AKDGVRVNAVIPAEVMTPLYENWIATFDDPEAKLAAITAKIPLGhRMTTAEEIADTAVFLLSERSSHTTGQWLFVDGGYV 251
PRK09135 PRK09135
pteridine reductase; Provisional
 79-254 6.05e-26

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 101.93  E-value: 6.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  79 QELGPIDVLVNNAgwDVFRP--FVKTEPAQWERLIAINLTGALHMHHAVLPgMVARKAGRIVNIASDAARVGSSGEAVYA 156
Cdd:PRK09135   81 AAFGRLDALVNNA--SSFYPtpLGSITEAQWDDLFASNLKAPFFLSQAAAP-QLRKQRGAIVNITDIHAERPLKGYPVYC 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 157 ACKGGLVSFSKTIAREHARHdITVNVVCPGP-----TETALFEDYKQgagnpeklveAFTRSIPLGRIGQPDDLPGAVLF 231
Cdd:PRK09135  158 AAKAALEMLTRSLALELAPE-VRVNAVAPGAilwpeDGNSFDEEARQ----------AILARTPLKRIGTPEDIAEAVRF 226

                         170       180
                  ....*....|....*....|...
gi 1444067332 232 FAgDDAAFITGQVLSVSGGLTMN 254
Cdd:PRK09135  227 LL-ADASFITGQILAVDGGRSLT 248
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 21-231 2.46e-25

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: 99.50  E-value: 2.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNpeaGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:cd08929    15 ATARLLHAEGYRVGICARD---EARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNAGVGVMKPVE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:cd08929    92 ELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAAMLDLREANIRV 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 181 NVVCPGPTETALfedykqgAGNPEklveaftrsiPLGRIGQPDDLPGAVLF 231
Cdd:cd08929   172 VNVMPGSVDTGF-------AGSPE----------GQAWKLAPEDVAQAVLF 205
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 39-208 3.15e-25

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: 99.23  E-value: 3.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  39 NPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAG--WDVFRPFVKTEpAQWERLIAINLT 116
Cdd:cd05324    34 DVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDILVNNAGiaFKGFDDSTPTR-EQARETMKTNFF 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 117 GALHMHHAVLPGMVARKAGRIVNIASdaaRVGSSGEAvYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALfedy 196
Cdd:cd05324   113 GTVDVTQALLPLLKKSPAGRIVNVSS---GLGSLTSA-YGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDM---- 184

                         170
                  ....*....|..
gi 1444067332 197 kqGAGNPEKLVE 208
Cdd:cd05324   185 --GGGKAPKTPE 194
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 25-198 3.67e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 100.81  E-value: 3.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVLDLNPEAGERVAAQIRDaGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:PRK05872   28 RLHARGAKLALVDLEEAELAALAAELGG-DDRVLTVVADVTDLAAMQAAAEEAVERFGGIDVVVANAGIASGGSVAQVDP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKaGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVC 184
Cdd:PRK05872  107 DAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPGMAAYCASKAGVEAFANALRLEVAHHGVTVGSAY 185

                         170
                  ....*....|....
gi 1444067332 185 PGPTETALFEDYKQ 198
Cdd:PRK05872  186 LSWIDTDLVRDADA 199
PRK07985 PRK07985
SDR family oxidoreductase;
21-250 4.08e-25

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 100.45  E-value: 4.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGV--LDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRP 98
Cdd:PRK07985   64 AAAIAYAREGADVAIsyLPVEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALGGLDIMALVAGKQVAIP 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKT-EPAQWERLIAINLTGALHMHHAVLPgmVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHD 177
Cdd:PRK07985  144 DIADlTSEQFQKTFAINVFALFWLTQEAIP--LLPKGASIITTSSIQAYQPSPHLLDYAATKAAILNYSRGLAKQVAEKG 221

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 178 ITVNVVCPGPTETALfedyKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK07985  222 IRVNIVAPGPIWTAL----QISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQESSYVTAEVHGVCGG 290
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-250 4.71e-25

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 100.63  E-value: 4.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNP-EAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVeQELG 82
Cdd:PRK07792   10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASaLDASDVLDEIRAAGAKAVAVAGDISQRATADELVATA-VGLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  83 PIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGA-LHMHHAVLPGMVARKA------GRIVNIASDAARVGSSGEAVY 155
Cdd:PRK07792   89 GLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHfLLTRNAAAYWRAKAKAaggpvyGRIVNTSSEAGLVGPVGQANY 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 156 AACKGGLVSFSKTIAREHARHDITVNVVCPgPTETALFEDYKQGAgnPEKLVEAFTrsiPLGrigqPDDLPGAVLFFAGD 235
Cdd:PRK07792  169 GAAKAGITALTLSAARALGRYGVRANAICP-RARTAMTADVFGDA--PDVEAGGID---PLS----PEHVVPLVQFLASP 238

                         250
                  ....*....|....*
gi 1444067332 236 DAAFITGQVLSVSGG 250
Cdd:PRK07792  239 AAAEVNGQVFIVYGP 253
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 21-250 7.68e-25

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: 98.50  E-value: 7.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVgVLDLNPEAGE--RVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFRP 98
Cdd:cd05357    15 AIAEALAAEGYRV-VVHYNRSEAEaqRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCDVLVNNAS--AFYP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEP--AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARh 176
Cdd:cd05357    92 TPLGQGseDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLTRSAALELAP- 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 177 DITVNVVCPGPTetaLFEDykqgaGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAgdDAAFITGQVLSVSGG 250
Cdd:cd05357   171 NIRVNGIAPGLI---LLPE-----DMDAEYRENALRKVPLKRRPSAEEIADAVIFLL--DSNYITGQIIKVDGG 234
PRK07775 PRK07775
SDR family oxidoreductase;
21-192 9.01e-25

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 99.06  E-value: 9.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK07775   25 ATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLVSGAGDTYFGKLH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK07775  105 EISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTNLQMELEGTGVRA 184

                         170
                  ....*....|..
gi 1444067332 181 NVVCPGPTETAL 192
Cdd:PRK07775  185 SIVHPGPTLTGM 196
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 21-255 3.69e-24

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 97.10  E-value: 3.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGV-LDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:PRK06077   21 AIAVRLAKEGSLVVVnAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVADILVNNAGLGLFSPF 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHdIT 179
Cdd:PRK06077  101 LNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSIYGAMKAAVINLTKYLALELAPK-IR 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1444067332 180 VNVVCPGPTETALFEDYKQGAGNPEKlvEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAafITGQVLSVSGGLTMNG 255
Cdd:PRK06077  178 VNAIAPGFVKTKLGESLFKVLGMSEK--EFAEKFTLMGKILDPEEVAEFVAAILKIES--ITGQVFVLDSGESLKG 249
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 26-249 4.45e-24

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 99.91  E-value: 4.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLnPEAGERVAAQIRDAGGRALSvrCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPA 105
Cdd:PRK08261  230 LARDGAHVVCLDV-PAAGEALAAVANRVGGTALA--LDITAPDAPARIAEHLAERHGGLDIVVHNAGITRDKTLANMDEA 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 106 QWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCP 185
Cdd:PRK08261  307 RWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAERGITINAVAP 386

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 186 GPTETALfedykqGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSG 249
Cdd:PRK08261  387 GFIETQM------TAAIPFATREAGRRMNSLQQGGLPVDVAETIAWLASPASGGVTGNVVRVCG 444
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 26-206 5.62e-24

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: 96.89  E-value: 5.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAGG-RALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:cd05332    23 LARLGARLVLSARREERLEEVKSECLELGApSPHVVPLDMSDLEDAEQVVEEALKLFGGLDILINNAGISMRSLFHDTSI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVC 184
Cdd:cd05332   103 DVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVVC 182

                         170       180
                  ....*....|....*....|....*..
gi 1444067332 185 PGPTET-----ALFEDYKQGAGNPEKL 206
Cdd:cd05332   183 PGLIDTniamnALSGDGSMSAKMDDTT 209
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 21-250 1.14e-23

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: 96.07  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVF-RPF 99
Cdd:cd08936    25 AIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGVDILVSNAAVNPFfGNI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:cd08936   105 LDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIR 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 180 VNVVCPGPTET----ALFEDykqgagnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:cd08936   185 VNCLAPGLIKTsfssALWMD--------KAVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASYITGETVVVGGG 251
PRK09072 PRK09072
SDR family oxidoreductase;
21-192 2.44e-23

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 95.01  E-value: 2.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIrDAGGRALSVRCDITDRASVDAAVAAVEQeLGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK09072   20 ALAEALAAAGARLLLVGRNAEKLEALAARL-PYPGRHRWVVADLTSEAGREAVLARARE-MGGINVLINNAGVNHFALLE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK09072   98 DQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALRGFSEALRRELADTGVRV 177

                         170
                  ....*....|..
gi 1444067332 181 NVVCPGPTETAL 192
Cdd:PRK09072  178 LYLAPRATRTAM 189
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 25-193 2.99e-23

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 94.37  E-value: 2.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVLDLNPEAGERVAAQI-RDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTE 103
Cdd:cd05373    18 RFAAEGFSVALAARREAKLEALLVDIiRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEVLVYNAGANVWFPILETT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV-NV 182
Cdd:cd05373    98 PRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRALAQSMARELGPKGIHVaHV 177

                         170
                  ....*....|.
gi 1444067332 183 VCPGPTETALF 193
Cdd:cd05373   178 IIDGGIDTDFI 188
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 1-250 5.15e-23

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 94.74  E-value: 5.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDL---------NPEAGERVAAQIRDAGGRALSVRCDITDRASVD 71
Cdd:PRK07791    1 MGLLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIgvgldgsasGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  72 AAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTG-ALHMHHAVLPGMVARKAG-----RIVNIASDAA 145
Cdd:PRK07791   81 NLVDAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGhFATLRHAAAYWRAESKAGravdaRIINTSSGAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 146 RVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCP----GPTETALFEdykQGAGNPEKLVEAFTrsiplgrigq 221
Cdd:PRK07791  161 LQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPaartRMTETVFAE---MMAKPEEGEFDAMA---------- 227

                         250       260
                  ....*....|....*....|....*....
gi 1444067332 222 PDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK07791  228 PENVSPLVVWLGSAESRDVTGKVFEVEGG 256
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 21-245 7.27e-23

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: 93.61  E-value: 7.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGV------LDLNPEAG------ERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLV 88
Cdd:cd05338    18 AIALRLAKAGATVVVaaktasEGDNGSAKslpgtiEETAEEIEAAGGQALPIVVDVRDEDQVRALVEATVDQFGRLDILV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  89 NNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKT 168
Cdd:cd05338    98 NNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARGDVAYAAGKAGMSRLTLG 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 169 IAREHARHDITVNVVCPGP-TETALFEDYkqgagnpeklveaFTRSIPlGRIGQPDDLPGAVLFFAGDDAAFITGQVL 245
Cdd:cd05338   178 LAAELRRHGIAVNSLWPSTaIETPAATEL-------------SGGSDP-ARARSPEILSDAVLAILSRPAAERTGLVV 241
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 21-213 1.07e-22

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


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 92.51  E-value: 1.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIrdAGGRALSVRCDITDRAS-VDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:cd08931    15 ETALLFARNGWFVGLYDIDEDGLAALAAEL--GAENVVAGALDVTDRAAwAAALADFAAATGGRLDALFNNAGVGRGGPF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:cd08931    93 EDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEALDVEWARHGIR 172

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1444067332 180 VNVVCPGPTETALFEDYKQGAGNPEKLVEAFTRS 213
Cdd:cd08931   173 VADVWPWFVDTPILTKGETGAAPKKGLGRVLPVS 206
PRK07201 PRK07201
SDR family oxidoreductase;
21-179 1.50e-22

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 96.17  E-value: 1.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK07201  386 ATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDYLVNNAGRSIRRSVE 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPA--QWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK07201  466 NSTDRfhDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNAPRFSAYVASKAALDAFSDVAASETLSDGI 545


                  .
gi 1444067332 179 T 179
Cdd:PRK07201  546 T 546
PRK05866 PRK05866
SDR family oxidoreductase;
21-183 2.22e-22

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 93.27  E-value: 2.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPfV 100
Cdd:PRK05866   55 AAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILINNAGRSIRRP-L 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQW---ERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGE-AVYAACKGGLVSFSKTIAREHARH 176
Cdd:PRK05866  134 AESLDRWhdvERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATWGVLSEASPLfSVYNASKAALSAVSRVIETEWGDR 213


                  ....*..
gi 1444067332 177 DITVNVV 183
Cdd:PRK05866  214 GVHSTTL 220
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-250 2.30e-22

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 92.24  E-value: 2.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGA-AVGVLDLNP-EAGERVAAqirdAGGRALSVRCDITDRASVDAAVAAVEQEL 81
Cdd:PRK08993    8 LEGKVAVVTGCDTGLGQGMALGLAEAGCdIVGINIVEPtETIEQVTA----LGRRFLSLTADLRKIDGIPALLERAVAEF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  82 GPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVAR-KAGRIVNIASDAARVGSSGEAVYAACKG 160
Cdd:PRK08993   84 GHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMLSFQGGIRVPSYTASKS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 161 GLVSFSKTIAREHARHDITVNVVCPGPTETalfEDYKQGAGNPEKLVEAFTRsIPLGRIGQPDDLPGAVLFFAGDDAAFI 240
Cdd:PRK08993  164 GVMGVTRLMANEWAKHNINVNAIAPGYMAT---NNTQQLRADEQRSAEILDR-IPAGRWGLPSDLMGPVVFLASSASDYI 239

                         250
                  ....*....|
gi 1444067332 241 TGQVLSVSGG 250
Cdd:PRK08993  240 NGYTIAVDGG 249
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 21-251 5.12e-22

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: 91.40  E-value: 5.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEageRVAAQIRDAGGRALSVRcDITDRASvdaavaaveqelGPIDVLVNNAGWDVfrpfv 100
Cdd:cd05328    14 ATAELLEDAGHTVIGIDLREA---DVIADLSTPEGRAAAIA-DVLARCS------------GVLDGLVNCAGVGG----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 ktePAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAA---------------------------RVGSSGEA 153
Cdd:cd05328    73 ---TTVAGLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGagwaqdklelakalaagtearavalaeHAGQPGYL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 154 VYAACKGGLVSFSKTIARE-HARHDITVNVVCPGPTETALFEDYKQGAGNPEKlVEAFTRsiPLGRIGQPDDLPGAVLFF 232
Cdd:cd05328   150 AYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRGGES-VDAFVT--PMGRRAEPDEIAPVIAFL 226

                         250
                  ....*....|....*....
gi 1444067332 233 AGDDAAFITGQVLSVSGGL 251
Cdd:cd05328   227 ASDAASWINGANLFVDGGL 245
PRK08267 PRK08267
SDR family oxidoreductase;
21-192 6.25e-22

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 91.15  E-value: 6.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIrdAGGRALSVRCDITDRASVDAAVAAVEQEL-GPIDVLVNNAGWDVFRPF 99
Cdd:PRK08267   16 ATALLFAAEGWRVGAYDINEAGLAALAAEL--GAGNAWTGALDVTDRAAWDAALADFAAATgGRLDVLFNNAGILRGGPF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK08267   94 EDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEALDLEWRRHGIR 173

                         170
                  ....*....|...
gi 1444067332 180 VNVVCPGPTETAL 192
Cdd:PRK08267  174 VADVMPLFVDTAM 186
PRK06482 PRK06482
SDR family oxidoreductase;
41-191 6.44e-22

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 91.72  E-value: 6.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  41 EAGERVAAQIRDAG---------GRALSV-RCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQWERL 110
Cdd:PRK06482   24 ARGDRVAATVRRPDalddlkaryGDRLWVlQLDVTDSAAVRAVVDRAFAALGRIDVVVSNAGYGLFGAAEELSDAQIRRQ 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 111 IAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTET 190
Cdd:PRK06482  104 IDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPART 183


                  .
gi 1444067332 191 A 191
Cdd:PRK06482  184 N 184
PRK12742 PRK12742
SDR family oxidoreductase;
25-250 7.21e-22

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 90.59  E-value: 7.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVG-VLDLNPEAGERVAAQirdAGGRAlsVRCDITDRASVDAAVaaveQELGPIDVLVNNAGWDVFRPFVKTE 103
Cdd:PRK12742   25 RFVTDGANVRfTYAGSKDAAERLAQE---TGATA--VQTDSADRDAVIDVV----RKSGALDILVVNAGIAVFGDALELD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 104 PAQWERLIAINLTGALHMhhAVLPGMVARKAGRIVNIAS-DAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNV 182
Cdd:PRK12742   96 ADDIDRLFKINIHAPYHA--SVEAARQMPEGGRIIIIGSvNGDRMPVAGMAAYAASKSALQGMARGLARDFGPRGITINV 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 183 VCPGPTETalfeDYKQGAGNPEKLVEAFtrsIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK12742  174 VQPGPIDT----DANPANGPMKDMMHSF---MAIKRHGRPEEVAGMVAWLAGPEASFVTGAMHTIDGA 234
PLN02253 PLN02253
xanthoxin dehydrogenase
 26-252 1.32e-21

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 91.04  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAGGrALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW------DVfrpf 99
Cdd:PLN02253   38 FHKHGAKVCIVDLQDDLGQNVCDSLGGEPN-VCFFHCDVTVEDDVSRAVDFTVDKFGTLDIMVNNAGLtgppcpDI---- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALH-MHHAVLPgMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PLN02253  113 RNVELSEFEKVFDVNVKGVFLgMKHAARI-MIPLKKGSIVSLCSVASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGI 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 179 TVNVVCPGPTETAL--------------FEDYKQGAGNpeklvEAFTRSIPLgrigQPDDLPGAVLFFAGDDAAFITGQV 244
Cdd:PLN02253  192 RVNCVSPYAVPTALalahlpedertedaLAGFRAFAGK-----NANLKGVEL----TVDDVANAVLFLASDEARYISGLN 262


                  ....*...
gi 1444067332 245 LSVSGGLT 252
Cdd:PLN02253  263 LMIDGGFT 270
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 82-253 2.36e-21

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 89.56  E-value: 2.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  82 GPIDVLVNNAGWD-VFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKG 160
Cdd:cd05361    71 GAIDVLVSNDYIPrPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 161 GLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKQGAGNPEkLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFI 240
Cdd:cd05361   151 AAVALAESLAKELSRDNILVYAIGPNFFNSPTYFPTSDWENNPE-LRERVKRDVPLGRLGRPDEMGALVAFLASRRADPI 229

                         170
                  ....*....|...
gi 1444067332 241 TGQVLSVSGGLTM 253
Cdd:cd05361   230 TGQFFAFAGGYLP 242
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 4-253 1.12e-20

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


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 87.79  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPeagERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGP 83
Cdd:cd05348     2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSA---EKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  84 IDVLVNNAG-WDVFRPFVKTEPAQ----WERLIAINLTGALHMHHAVLPGMVARKaGRIVNIASDAARVGSSGEAVYAAC 158
Cdd:cd05348    79 LDCFIGNAGiWDYSTSLVDIPEEKldeaFDELFHINVKGYILGAKAALPALYATE-GSVIFTVSNAGFYPGGGGPLYTAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 159 KGGLVSFSKTIAREHARHdITVNVVCPGPTETALFEDYKQGAGNPEK----LVEAFTRSIPLGRIGQPDDLPGAVLFFAG 234
Cdd:cd05348   158 KHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLRGPASLGQGETSIstppLDDMLKSILPLGFAPEPEDYTGAYVFLAS 236

                         250       260
                  ....*....|....*....|
gi 1444067332 235 -DDAAFITGQVLSVSGGLTM 253
Cdd:cd05348   237 rGDNRPATGTVINYDGGMGV 256
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 26-192 1.51e-20

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: 87.00  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQI-RDAGGRALSVrCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:cd05350    18 FAKAGYNVALAARRTDRLDELKAELlNPNPSVEVEI-LDVTDEERNQLVIAELEAELGGLDLVIINAGVGKGTSLGDLSF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVC 184
Cdd:cd05350    97 KAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSLAESLRYDVKKRGIRVTVIN 176


                  ....*...
gi 1444067332 185 PGPTETAL 192
Cdd:cd05350   177 PGFIDTPL 184
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 1-192 3.41e-20

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 86.93  E-value: 3.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK05876    1 MDGFPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVAR-KAGRIVNIASDAARVGSSGEAVYAACK 159
Cdd:PRK05876   81 LGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQgTGGHVVFTASFAGLVPNAGLGAYGVAK 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1444067332 160 GGLVSFSKTIAREHARHDITVNVVCPGPTETAL 192
Cdd:PRK05876  161 YGVVGLAETLAREVTADGIGVSVLCPMVVETNL 193
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 21-233 4.53e-20

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: 85.73  E-value: 4.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRalSVRCDITDRASVDAAVAAVEQELG--PIDVLVNNAGWDVFRP 98
Cdd:cd05356    16 AYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGV--ETKTIAADFSAGDDIYERIEKELEglDIGILVNNVGISHSIP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 --FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARH 176
Cdd:cd05356    94 eyFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDFFSRALYEEYKSQ 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 177 DITVNVVCPGPTETALFEDYKQGAGNPEKlvEAFTRSIpLGRIGQPDDLPG----AVLFFA 233
Cdd:cd05356   174 GIDVQSLLPYLVATKMSKIRKSSLFVPSP--EQFVRSA-LNTLGLSKRTTGywshALQGWV 231
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 1-255 8.41e-20

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 85.78  E-value: 8.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   1 MQGLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPeagERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQE 80
Cdd:PRK06200    1 MGWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSA---EKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAG-WDVFRPFVKTEPAQ----WERLIAINLTGALHMHHAVLPGMVARKaGRIVNIASDAARVGSSGEAVY 155
Cdd:PRK06200   78 FGKLDCFVGNAGiWDYNTSLVDIPAETldtaFDEIFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYPGGGGPLY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 156 AACKGGLVSFSKTIAREHARhDITVNVVCPGPTETALFEDYKQGAG--------NPEKLVEAFTrsiPLGRIGQPDDLPG 227
Cdd:PRK06200  157 TASKHAVVGLVRQLAYELAP-KIRVNGVAPGGTVTDLRGPASLGQGetsisdspGLADMIAAIT---PLQFAPQPEDHTG 232

                         250       260
                  ....*....|....*....|....*....
gi 1444067332 228 AVLFFAGD-DAAFITGQVLSVSGGLTMNG 255
Cdd:PRK06200  233 PYVLLASRrNSRALTGVVINADGGLGIRG 261
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 41-193 1.69e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 85.09  E-value: 1.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  41 EAGERVAAQIRDA----------GGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQWERL 110
Cdd:PRK08263   25 ERGDRVVATARDTatladlaekyGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVNNAGYGLFGMIEEVTESEARAQ 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 111 IAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTET 190
Cdd:PRK08263  105 IDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWALEGMSEALAQEVAEFGIKVTLVEPGGYST 184


                  ...
gi 1444067332 191 ALF 193
Cdd:PRK08263  185 DWA 187
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 85-233 1.77e-19

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 82.95  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  85 DVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVS 164
Cdd:cd02266    33 DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDG 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444067332 165 FSKTIAREHARHDITVNVVCPGPTETALFEdykQGAGNPEklvEAFTRSIPLGRIGQPDDLPGAVLFFA 233
Cdd:cd02266   113 LAQQWASEGWGNGLPATAVACGTWAGSGMA---KGPVAPE---EILGNRRHGVRTMPPEEVARALLNAL 175
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 3-255 2.12e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 84.33  E-value: 2.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   3 GLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGraLSVRCDITDRASVDAAVAAVEqELG 82
Cdd:PRK06125    4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHG--VDVAVHALDLSSPEAREQLAA-EAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  83 PIDVLVNNAG-------WDVfrpfvktEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIasdaarVGSSGEAV- 154
Cdd:PRK06125   81 DIDILVNNAGaipggglDDV-------DDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV------IGAAGENPd 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 155 --Y---AACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALFED-YKQGA----GNPEKLVEaFTRSIPLGRIGQPDD 224
Cdd:PRK06125  148 adYicgSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTlLKGRAraelGDESRWQE-LLAGLPLGRPATPEE 226

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1444067332 225 LPGAVLFFAGDDAAFITGQVLSVSGGLTMNG 255
Cdd:PRK06125  227 VADLVAFLASPRSGYTSGTVVTVDGGISARG 257
PRK06914 PRK06914
SDR family oxidoreductase;
22-202 2.30e-19

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 84.69  E-value: 2.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  22 TCLRFARAGAAVGVLDLNPEAGERVAAQIRDAG--GRALSVRCDITDrASVDAAVAAVEQELGPIDVLVNNAGWdVFRPF 99
Cdd:PRK06914   19 TTLELAKKGYLVIATMRNPEKQENLLSQATQLNlqQNIKVQQLDVTD-QNSIHNFQLVLKEIGRIDLLVNNAGY-ANGGF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQ-WERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK06914   97 VEEIPVEeYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYALEGFSESLRLELKPFGI 176

                         170       180
                  ....*....|....*....|....
gi 1444067332 179 TVNVVCPGPTETALFEDYKQGAGN 202
Cdd:PRK06914  177 DVALIEPGSYNTNIWEVGKQLAEN 200
PRK09134 PRK09134
SDR family oxidoreductase;
21-250 2.83e-19

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 84.21  E-value: 2.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGV-LDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAG---WDVF 96
Cdd:PRK09134   24 AIALDLAAHGFDVAVhYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARASAALGPITLLVNNASlfeYDSA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  97 RPFvktEPAQWERLIAINLTG----ALHMHHAvLPgmvARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIARE 172
Cdd:PRK09134  104 ASF---TRASWDRHMATNLRApfvlAQAFARA-LP---ADARGLVVNMIDQRVWNLNPDFLSYTLSKAALWTATRTLAQA 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 173 HARhDITVNVVCPGPTetalfedyKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAgdDAAFITGQVLSVSGG 250
Cdd:PRK09134  177 LAP-RIRVNAIGPGPT--------LPSGRQSPEDFARQHAATPLGRGSTPEEIAAAVRYLL--DAPSVTGQMIAVDGG 243
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
24-250 5.73e-19

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 83.03  E-value: 5.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  24 LRFARAGA-AVGVldlNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKT 102
Cdd:PRK12481   26 IGLAKAGAdIVGV---GVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDILINNAGIIRRQDLLEF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 103 EPAQWERLIAINLTGALHMHHAVLPGMVAR-KAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVN 181
Cdd:PRK12481  103 GNKDWDDVININQKTVFFLSQAVAKQFVKQgNGGKIINIASMLSFQGGIRVPSYTASKSAVMGLTRALATELSQYNINVN 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444067332 182 VVCPGPTETalfeDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK12481  183 AIAPGYMAT----DNTAALRADTARNEAILERIPASRWGTPDDLAGPAIFLSSSASDYVTGYTLAVDGG 247
PRK05717 PRK05717
SDR family oxidoreductase;
30-252 7.35e-19

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 83.01  E-value: 7.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  30 GAAVGVLDLNPEAGERVAAQIrdaGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFRPFVKT----EPA 105
Cdd:PRK05717   34 GWQVVLADLDRERGSKVAKAL---GENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALVCNAA--IADPHNTTleslSLA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 106 QWERLIAINLTGALHMHHAVLPGMVARKaGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARhDITVNVVCP 185
Cdd:PRK05717  109 HWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSEPDTEAYAASKGGLLALTHALAISLGP-EIRVNAVSP 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 186 GPTETAlfedyKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK05717  187 GWIDAR-----DPSQRRAEPLSEADHAQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFVVDGGMT 248
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 44-233 2.57e-18

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 81.34  E-value: 2.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  44 ERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDV-FRPFVKTEPAQWERLIAINLTGALHMH 122
Cdd:PRK10538   35 ERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAGLALgLEPAHKASVEDWETMIDTNNKGLVYMT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 123 HAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKqGAGN 202
Cdd:PRK10538  115 RAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSNVR-FKGD 193

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1444067332 203 PEKLVEAFTRSIPLgrigQPDDLPGAVLFFA 233
Cdd:PRK10538  194 DGKAEKTYQNTVAL----TPEDVSEAVWWVA 220
PRK06194 PRK06194
hypothetical protein; Provisional
 24-197 1.82e-17

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 79.67  E-value: 1.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  24 LRFARAGAAVG---VL-DLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:PRK06194   20 LAFARIGAALGmklVLaDVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHLLFNNAGVGAGGLV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKA------GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKT----I 169
Cdd:PRK06194  100 WENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEkdpayeGHIVNTASMAGLLAPPAMGIYNVSKHAVVSLTETlyqdL 179

                         170       180
                  ....*....|....*....|....*...
gi 1444067332 170 AREHARhdITVNVVCPGPTETALFEDYK 197
Cdd:PRK06194  180 SLVTDQ--VGASVLCPYFVPTGIWQSER 205
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 26-250 5.60e-17

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 77.97  E-value: 5.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAAVGVLDLNPEAGERVAAQIRDAGGRALS-VRCDITDRASVDAAVAAVeQELGPIDVLVNNAGWDVFRPFVKTEP 104
Cdd:PRK08339   28 LARAGADVILLSRNEENLKKAREKIKSESNVDVSyIVADLTKREDLERTVKEL-KNIGEPDIFFFSTGGPKPGYFMEMSM 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 105 AQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVC 184
Cdd:PRK08339  107 EDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRISMAGLVRTLAKELGPKGITVNGIM 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332 185 PGPTETA----LFEDYKQGAGNP-EKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK08339  187 PGIIRTDrviqLAQDRAKREGKSvEEALQEYAKPIPLGRLGEPEEIGYLVAFLASDLGSYINGAMIPVDGG 257
PRK06182 PRK06182
short chain dehydrogenase; Validated
 21-190 6.01e-17

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 78.08  E-value: 6.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVldlnpeAGERVA--AQIRDAGGRALSVrcDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRP 98
Cdd:PRK06182   18 ATARRLAAQGYTVYG------AARRVDkmEDLASLGVHPLSL--DVTDEASIKAAVDTIIAEEGRIDVLVNNAGYGSYGA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  99 FVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDI 178
Cdd:PRK06182   90 IEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDALRLEVAPFGI 169

                         170
                  ....*....|..
gi 1444067332 179 TVNVVCPGPTET 190
Cdd:PRK06182  170 DVVVIEPGGIKT 181
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 4-250 1.08e-16

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 77.04  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLN-PEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQEL- 81
Cdd:PRK12747    2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNrKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELq 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  82 -----GPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYA 156
Cdd:PRK12747   82 nrtgsTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDFIAYS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 157 ACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKQgagnpEKLVEAFTRSI-PLGRIGQPDDLPGAVLFFAGD 235
Cdd:PRK12747  160 MTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLS-----DPMMKQYATTIsAFNRLGEVEDIADTAAFLASP 234

                         250
                  ....*....|....*
gi 1444067332 236 DAAFITGQVLSVSGG 250
Cdd:PRK12747  235 DSRWVTGQLIDVSGG 249
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 21-192 3.23e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 75.71  E-value: 3.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAavgvldlnpeageRVAAQIRDAGGRALS-----VRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDV 95
Cdd:PRK06179   19 ATAEKLARAGY-------------RVFGTSRNPARAAPIpgvelLELDVTDDASVQAAVDEVIARAGRIDVLVNNAGVGL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  96 FRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHAR 175
Cdd:PRK06179   86 AGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKHAVEGYSESLDHEVRQ 165

                         170
                  ....*....|....*..
gi 1444067332 176 HDITVNVVCPGPTETAL 192
Cdd:PRK06179  166 FGIRVSLVEPAYTKTNF 182
PRK12744 PRK12744
SDR family oxidoreductase;
25-252 4.79e-16

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 75.16  E-value: 4.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVLDLNPEAG----ERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK12744   27 DLAAQGAKAVAIHYNSAASkadaEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAAFGRPDIAINTVGKVLKKPIV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGA-LHMHHAvlpGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:PRK12744  107 EISEAEYDEMFAVNSKSAfFFIKEA---GRHLNDNGKIVTLVTSLLGAFTPFYSAYAGSKAPVEHFTRAASKEFGARGIS 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444067332 180 VNVVCPGPTETALFedYkqGAGNPEKLveAFTRSI----PLGRIG--QPDDLPGAVLFFAgDDAAFITGQVLSVSGGLT 252
Cdd:PRK12744  184 VTAVGPGPMDTPFF--Y--PQEGAEAV--AYHKTAaalsPFSKTGltDIEDIVPFIRFLV-TDGWWITGQTILINGGYT 255
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 24-247 4.20e-15

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: 72.86  E-value: 4.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  24 LRFARAGAAVGVLDLNPEAGER-VAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQEL-GPIDVLVNNA-------GWD 94
Cdd:cd09763    21 LQLGEAGATVYITGRTILPQLPgTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQqGRLDILVNNAyaavqliLVG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  95 VFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAvYAACKGGLVSFSKTIAREHA 174
Cdd:cd09763   101 VAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVA-YGVGKAAIDRMAADMAHELK 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1444067332 175 RHDITVNVVCPGPTETALFEDYKQgagNPEKLVEAFTRSIplGRIGQPDDLPG-AVLFFAGD-DAAFITGQVLSV 247
Cdd:cd09763   180 PHGVAVVSLWPGFVRTELVLEMPE---DDEGSWHAKERDA--FLNGETTEYSGrCVVALAADpDLMELSGRVLIT 249
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 4-245 6.65e-15

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: 71.84  E-value: 6.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRA---LSVRCDITDRASVDAAVAAVEQE 80
Cdd:cd05340     2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQpqwFILDLLTCTSENCQQLAQRIAVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNAGWDVFR-PFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACK 159
Cdd:cd05340    82 YPRLDGVLHNAGLLGDVcPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 160 GGLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKQGAgNPEKLveaftrsiplgriGQPDDLPGAVLFFAGDDAAF 239
Cdd:cd05340   162 FATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTE-DPQKL-------------KTPADIMPLYLWLMGDDSRR 227


                  ....*.
gi 1444067332 240 ITGQVL 245
Cdd:cd05340   228 KTGMTF 233
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 27-250 9.69e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 71.76  E-value: 9.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  27 ARAGAAVGVLDLNPEAGERVAAQIRDAGGRAlSVR---CDITDRASVDAAVAAVEQELGPIDVLVNNAGW-DVFRPFVKT 102
Cdd:PRK05875   28 VAAGAAVMIVGRNPDKLAAAAEEIEALKGAG-AVRyepADVTDEDQVARAVDAATAWHGRLHGVVHCAGGsETIGPITQI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 103 EPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNV 182
Cdd:PRK05875  107 DSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNS 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 183 VCPGPTETALFEDYKQGagnpEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGG 250
Cdd:PRK05875  187 IRPGLIRTDLVAPITES----PELSADYRACTPLPRVGEVEDVANLAMFLLSDAASWITGQVINVDGG 250
PRK08416 PRK08416
enoyl-ACP reductase;
135-252 1.42e-14

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 71.34  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 135 GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTET-AL--FEDYKQGAGNPEKLVeaft 211
Cdd:PRK08416  145 GSIISLSSTGNLVYIENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTdALkaFTNYEEVKAKTEELS---- 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1444067332 212 rsiPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK08416  221 ---PLNRMGQPEDLAGACLFLCSEKASWLTGQTIVVDGGTT 258
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 24-183 4.75e-14

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: 69.42  E-value: 4.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  24 LRFARAGAAVGVLDLNPEAGERVAAQIRDAGGralsVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFRPF-VKT 102
Cdd:COG3967    23 KRLHARGNTVIITGRREEKLEEAAAANPGLHT----IVLDVADPASIAALAEQVTAEFPDLNVLINNAG--IMRAEdLLD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 103 EPAQW---ERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIaREHARhDIT 179
Cdd:COG3967    97 EAEDLadaEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAALHSYTQSL-RHQLK-DTS 174


                  ....
gi 1444067332 180 VNVV 183
Cdd:COG3967   175 VKVI 178
PRK06139 PRK06139
SDR family oxidoreductase;
21-195 5.07e-14

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 70.52  E-value: 5.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK06139   22 ATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAASFGGRIDVWVNNVGVGAVGRFE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARH-DIT 179
Cdd:PRK06139  102 ETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFGLRGFSEALRGELADHpDIH 181

                         170
                  ....*....|....*.
gi 1444067332 180 VNVVCPGPTETALFED 195
Cdd:PRK06139  182 VCDVYPAFMDTPGFRH 197
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 47-190 9.50e-14

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: 68.48  E-value: 9.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  47 AAQIRDAGGRALSVRC---DITDRASVDAAVAAVEQELGPIDVLVNNAG-WDVFRPFVKTEPAQWERLIAINLTGALHMH 122
Cdd:cd05325    36 ATELAALGASHSRLHIlelDVTDEIAESAEAVAERLGDAGLDVLINNAGiLHSYGPASEVDSEDLLEVFQVNVLGPLLLT 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 123 HAVLPGMVARKAGRIVNIASdaaRVGSSGE------AVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTET 190
Cdd:cd05325   116 QAFLPLLLKGARAKIINISS---RVGSIGDntsggwYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRT 186
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 25-194 1.08e-13

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 68.10  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  25 RFARAGAAVGVLDLNPEAGERVAAQIrdagGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFRPF----V 100
Cdd:cd05370    24 KFLEAGNTVIITGRREERLAEAKKEL----PNIHTIVLDVGDAESVEALAEALLSEYPNLDILINNAG--IQRPIdlrdP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKtiAREHARHDITV 180
Cdd:cd05370    98 ASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAALHSYTL--ALRHQLKDTGV 175

                         170
                  ....*....|....*.
gi 1444067332 181 NVV--CPGPTETALFE 194
Cdd:cd05370   176 EVVeiVPPAVDTELHE 191
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 15-193 1.58e-13

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: 68.41  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  15 GGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRAL--SVRCDITDRASVDAAVAAVEQELGPIDVLVNNAG 92
Cdd:cd05327    10 NSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAKveVIQLDLSSLASVRQFAEEFLARFPRLDILINNAG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  93 wdVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGS--------------SGEAVYAAC 158
Cdd:cd05327    90 --IMAPPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPidfndldlennkeySPYKAYGQS 167

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1444067332 159 KGGLVSFSKTIAREHARHDITVNVVCPGPTETALF 193
Cdd:cd05327   168 KLANILFTRELARRLEGTGVTVNALHPGVVRTELL 202
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
82-251 2.64e-13

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 67.33  E-value: 2.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  82 GPIDVLVNNAGwdvfrpFVKTEPAqwERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDA--------------ARV 147
Cdd:PRK12428   47 GRIDALFNIAG------VPGTAPV--ELVARVNFLGLRHLTEALLPRM--APGGAIVNVASLAgaewpqrlelhkalAAT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 148 GS--SGEAVYAA---CKGGLVSFSK------TIAREH---ARHDITVNVVCPGPTETALFEDYKQGAGnpEKLVEAFTRs 213
Cdd:PRK12428  117 ASfdEGAAWLAAhpvALATGYQLSKealilwTMRQAQpwfGARGIRVNCVAPGPVFTPILGDFRSMLG--QERVDSDAK- 193

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1444067332 214 iPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGL 251
Cdd:PRK12428  194 -RMGRPATADEQAAVLVFLCSDAARWINGVNLPVDGGL 230
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 34-208 3.27e-13

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: 67.69  E-value: 3.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  34 GVLDLNPEAGERVAaqiRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDV--LVNNAGWDVFrpfvkTEPAQW---- 107
Cdd:cd09805    30 GCLTKNGPGAKELR---RVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLwgLVNNAGILGF-----GGDEELlpmd 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 108 --ERLIAINLTGALHMHHAVLPgMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCP 185
Cdd:cd09805   102 dyRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAFSDSLRRELQPWGVKVSIIEP 180

                         170       180
                  ....*....|....*....|...
gi 1444067332 186 GptetalfeDYKQGAGNPEKLVE 208
Cdd:cd09805   181 G--------NFKTGITGNSELWE 195
PRK09291 PRK09291
SDR family oxidoreductase;
21-222 4.61e-13

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 66.95  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVgvldlnpEAGERVAAQIR----DAGGRALSVRC---DITDrasvdaaVAAVEQELG-PIDVLVNNAG 92
Cdd:PRK09291   17 EVALRLARKGHNV-------IAGVQIAPQVTalraEAARRGLALRVeklDLTD-------AIDRAQAAEwDVDVLLNNAG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  93 -------WDVfrpfvktePAQWER-LIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVS 164
Cdd:PRK09291   83 igeagavVDI--------PVELVReLFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHALEA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 165 FSKTIAREHARHDITVNVVCPGPTETAlFEDykQGAGNPEKLVEAFTRSIPLGRIGQP 222
Cdd:PRK09291  155 IAEAMHAELKPFGIQVATVNPGPYLTG-FND--TMAETPKRWYDPARNFTDPEDLAFP 209
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 84-185 6.93e-12

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 64.12  E-value: 6.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  84 IDVLVNNAG--WDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGE--AVYAACK 159
Cdd:PLN02780  133 VGVLINNVGvsYPYARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSDPlyAVYAATK 212

                          90       100
                  ....*....|....*....|....*.
gi 1444067332 160 GGLVSFSKTIAREHARHDITVNVVCP 185
Cdd:PLN02780  213 AYIDQFSRCLYVEYKKSGIDVQCQVP 238
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 84-195 7.34e-12

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 63.63  E-value: 7.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  84 IDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLV 163
Cdd:cd09806    80 VDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKFALE 159

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1444067332 164 SFSKTIAREHARHDITVNVVCPGPTETAlFED 195
Cdd:cd09806   160 GLCESLAVQLLPFNVHLSLIECGPVHTA-FME 190
PRK08219 PRK08219
SDR family oxidoreductase;
80-209 1.69e-11

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 61.87  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  80 ELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKaGRIVNIASDAARVGSSGEAVYAACK 159
Cdd:PRK08219   68 QLGRLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAASK 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 160 GGLVSFSKTIaREHARHDITVNVVCPGPTETALFEDYKQGAG---NPEKLVEA 209
Cdd:PRK08219  147 FALRALADAL-REEEPGNVRVTSVHPGRTDTDMQRGLVAQEGgeyDPERYLRP 198
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 79-213 1.86e-11

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 61.77  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  79 QELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVArkAGRIVNIASDAARVGSSGEAVYAAC 158
Cdd:cd11730    62 QELGPLDLLVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAA--GARLVFLGAYPELVMLPGLSAYAAA 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 159 KGGLVSFSKTIAREHARHDITvnVVCPGPTETALFEDYKQ---GAGNPEKLVEAFTRS 213
Cdd:cd11730   140 KAALEAYVEVARKEVRGLRLT--LVRPPAVDTGLWAPPGRlpkGALSPEDVAAAILEA 195
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 21-255 3.49e-11

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: 61.44  E-value: 3.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW----DVF 96
Cdd:cd05372    18 GIAKALHEAGAELAFTYQPEALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKLDGLVHSIAFapkvQLK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  97 RPFVKTEPAQWerLIAINLTG-ALH-MHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHA 174
Cdd:cd05372    98 GPFLDTSRKGF--LKALDISAySLVsLAKAALPIM--NPGGSIVTLSYLGSERVVPGYNVMGVAKAALESSVRYLAYELG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 175 RHDITVNVVCPGPTETALfedyKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTMN 254
Cdd:cd05372   174 RKGIRVNAISAGPIKTLA----ASGITGFDKMLEYSEQRAPLGRNVTAEEVGNTAAFLLSDLSSGITGEIIYVDGGYHIM 249


                  .
gi 1444067332 255 G 255
Cdd:cd05372   250 G 250
PRK09186 PRK09186
flagellin modification protein A; Provisional
 3-253 8.74e-11

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 60.39  E-value: 8.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   3 GLEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQI-RDAGGRALSV-RCDITDRASVDAAVAAVEQE 80
Cdd:PRK09186    1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLgKEFKSKKLSLvELDITDQESLEEFLSKSAEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  81 LGPIDVLVNNA-----GWDvfRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIAS------------D 143
Cdd:PRK09186   81 YGKIDGAVNCAyprnkDYG--KKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSiygvvapkfeiyE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 144 AARVGSSGEavYAACKGGLVSFSKTIAREHARHDITVNVVCPG------PteTALFEDYKQGAGNPEKLveaftrsiplg 217
Cdd:PRK09186  159 GTSMTSPVE--YAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGgildnqP--EAFLNAYKKCCNGKGML----------- 223

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1444067332 218 rigQPDDLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:PRK09186  224 ---DPDDICGTLVFLLSDQSKYITGQNIIVDDGFSL 256
PRK08017 PRK08017
SDR family oxidoreductase;
87-199 9.45e-11

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 60.48  E-value: 9.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  87 LVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFS 166
Cdd:PRK08017   78 LFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWS 157

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1444067332 167 KTIAREHARHDITVNVVCPGPTETALFEDYKQG 199
Cdd:PRK08017  158 DALRMELRHSGIKVSLIEPGPIRTRFTDNVNQT 190
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 21-231 1.59e-10

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: 59.45  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRAL-SVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPF 99
Cdd:cd05343    21 AVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLfPYQCDLSNEEQILSMFSAIRTQHQGVDVCINNAGLARPEPL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 100 VKTEPAQWERLIAINLTGALHMHHAVLPGMVARKA--GRIVNIAS-DAARVGSSGEA-VYAACKGGLVSFSKTIARE--H 173
Cdd:cd05343   101 LSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSmSGHRVPPVSVFhFYAATKHAVTALTEGLRQElrE 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 174 ARHDITVNVVCPGPTETALFEDYKQgagNPEKLVEAFTRSIPlgrIGQPDDLPGAVLF 231
Cdd:cd05343   181 AKTHIRATSISPGLVETEFAFKLHD---NDPEKAAATYESIP---CLKPEDVANAVLY 232
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 17-242 2.02e-10

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 60.32  E-value: 2.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  17 GIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGG--RALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWD 94
Cdd:COG3347   436 GIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGadAVDATDVDVTAEAAVAAAFGFAGLDIGGSDIGVANAGIA 515

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  95 VFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARK-AGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREH 173
Cdd:COG3347   516 SSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGlGGSSVFAVSKNAAAAAYGAAAAATAKAAAQHLLRALAAEG 595

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1444067332 174 ARHDITVNVVCPGPTETALF--------EDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITG 242
Cdd:COG3347   596 GANGINANRVNPDAVLDGSAiwasaaraERAAAYGIGNLLLEEVYRKRVALAVLVLAEDIAEAAAFFASDGGNKATG 672
PRK07024 PRK07024
SDR family oxidoreductase;
21-192 2.06e-10

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 59.17  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAQIRdAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFRPFV 100
Cdd:PRK07024   17 ALAREYARQGATLGLVARRTDALQAFAARLP-KAARVSVYAADVRDADALAAAAADFIAAHGLPDVVIANAG--ISVGTL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQ---WERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHD 177
Cdd:PRK07024   94 TEEREDlavFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLESLRVELRPAG 173

                         170
                  ....*....|....*
gi 1444067332 178 ITVNVVCPGPTETAL 192
Cdd:PRK07024  174 VRVVTIAPGYIRTPM 188
PRK07041 PRK07041
SDR family oxidoreductase;
17-250 3.69e-10

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 58.12  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  17 GIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIrDAGGRALSVRCDITDRASVDAAVaaveQELGPIDVLVNNAGWDVF 96
Cdd:PRK07041    8 GIGLALARAFAAEGARVTIASRSRDRLAAAARAL-GGGAPVRTAALDITDEAAVDAFF----AEAGPFDHVVITAADTPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  97 RPFVKTEPAQWERLIAINLTGALHmhhavlpgmVARKA-----GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAR 171
Cdd:PRK07041   83 GPVRALPLAAAQAAMDSKFWGAYR---------VARAAriapgGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLAL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444067332 172 EHArhDITVNVVCPGPTETALFEDYKQGAgnPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDdaAFITGQVLSVSGG 250
Cdd:PRK07041  154 ELA--PVRVNTVSPGLVDTPLWSKLAGDA--REAMFAAAAERLPARRVGQPEDVANAILFLAAN--GFTTGSTVLVDGG 226
PRK08278 PRK08278
SDR family oxidoreductase;
21-185 2.15e-09

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 56.45  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGER-------VAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW 93
Cdd:PRK08278   21 AIALRAARDGANIVIAAKTAEPHPKlpgtihtAAEEIEAAGGQALPLVGDVRDEDQVAAAVAKAVERFGGIDICVNNASA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  94 DVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIAS--DAARVGSSGEAVYAACKGGLVSFSKTIAR 171
Cdd:PRK08278  101 INLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPplNLDPKWFAPHTAYTMAKYGMSLCTLGLAE 180

                         170
                  ....*....|....
gi 1444067332 172 EHARHDITVNVVCP 185
Cdd:PRK08278  181 EFRDDGIAVNALWP 194
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 41-246 3.30e-09

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: 55.76  E-value: 3.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  41 EAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGwdVFRPFVK---TEPAQWERLIAINLTG 117
Cdd:cd05367    35 EEPLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDLLINNAG--SLGPVSKiefIDLDELQKYFDLNLTS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 118 ALHMHHAVLPGMVARKA-GRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHArhDITVNVVCPGPTETALFEDY 196
Cdd:cd05367   113 PVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAARDMFFRVLAAEEP--DVRVLSYAPGVVDTDMQREI 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1444067332 197 KQGAGNPEkLVEAFTRsipLGRIGQ---PDDlPGAVLFFAGDDAAFITGQVLS 246
Cdd:cd05367   191 RETSADPE-TRSRFRS---LKEKGElldPEQ-SAEKLANLLEKDKFESGAHVD 238
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 21-249 3.71e-09

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 55.41  E-value: 3.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDL--NPEAGERVAaqIRDAGG---RALSVRCDITDRAsvdaavaaveqelGPIDVLVNNAG-WD 94
Cdd:cd05334    16 AVVQAFKSRGWWVASIDLaeNEEADASII--VLDSDSfteQAKQVVASVARLS-------------GKVDALICVAGgWA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  95 VFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREH- 173
Cdd:cd05334    81 GGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHL--LSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENs 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 174 -ARHDITVNVVCPGPTETalfedykqgAGNPEKLVEA-FTRSIPlgrigqPDDLPGAVLFFAGDDAAFITGQVLSVSG 249
Cdd:cd05334   159 gLPAGSTANAILPVTLDT---------PANRKAMPDAdFSSWTP------LEFIAELILFWASGAARPKSGSLIPVVT 221
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 21-255 8.64e-09

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


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 54.64  E-value: 8.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERV---AAQIrdagGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW---- 93
Cdd:COG0623    22 GIAKALHEEGAELAFTYQGEALKKRVeplAEEL----GSALVLPCDVTDDEQIDALFDEIKEKWGKLDFLVHSIAFapke 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  94 DVFRPFVKTEPAQWER--------LIAinltgalhMHHAVLPGMvaRKAGRIVNIASDAARVGSSGEAVYAACKGGLVSF 165
Cdd:COG0623    98 ELGGRFLDTSREGFLLamdisaysLVA--------LAKAAEPLM--NEGGSIVTLTYLGAERVVPNYNVMGVAKAALEAS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 166 SKTIAREHARHDITVNVVCPGPTET-ALfedykQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAAFITGQV 244
Cdd:COG0623   168 VRYLAADLGPKGIRVNAISAGPIKTlAA-----SGIPGFDKLLDYAEERAPLGRNVTIEEVGNAAAFLLSDLASGITGEI 242

                         250
                  ....*....|.
gi 1444067332 245 LSVSGGLTMNG 255
Cdd:COG0623   243 IYVDGGYHIMG 253
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 21-157 9.39e-09

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 53.64  E-value: 9.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   21 ATCLRFARAGAAVGVL----DLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVF 96
Cdd:smart00822  15 ALARWLAERGARRLVLlsrsGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLTGVIHAAGVLDD 94

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1444067332   97 RPFVKTEPAQWERLIAINLTGALHMHHAVLPgmvaRKAGRIVNIASDAARVGSSGEAVYAA 157
Cdd:smart00822  95 GVLASLTPERFAAVLAPKAAGAWNLHELTAD----LPLDFFVLFSSIAGVLGSPGQANYAA 151
PRK08264 PRK08264
SDR family oxidoreductase;
42-192 1.97e-08

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 53.35  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  42 AGERVAAQIRDAGGRALSVRCDITDRASVDAAVaaveQELGPIDVLVNNAGwdVFR---PFVKTEPAQWERLIAINLTGA 118
Cdd:PRK08264   36 AAARDPESVTDLGPRVVPLQLDVTDPASVAAAA----EAASDVTILVNNAG--IFRtgsLLLEGDEDALRAEMETNYFGP 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1444067332 119 LHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETAL 192
Cdd:PRK08264  110 LAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDM 183
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 26-214 3.65e-08

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: 52.41  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  26 FARAGAA---VGVLDLnpeagERVAAQIRDAGGRALSVRCDITDRASVDAAVaaveQELGPIDVLVNNAGwdVFRPFVKT 102
Cdd:cd05354    23 LLAHGAKkvyAAVRDP-----GSAAHLVAKYGDKVVPLRLDVTDPESIKAAA----AQAKDVDVVINNAG--VLKPATLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 103 EPAQWERL---IAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDIT 179
Cdd:cd05354    92 EEGALEALkqeMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSLTQGLRAELAAQGTL 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1444067332 180 VNVVCPGPTETALFEDYKQGAGNPEKLVEAFTRSI 214
Cdd:cd05354   172 VLSVHPGPIDTRMAAGAGGPKESPETVAEAVLKAL 206
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 15-245 6.71e-08

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 51.80  E-value: 6.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  15 GGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGR-ALSVRCDI--TDRASVDAAVAAVEQELGPIDVLVNNA 91
Cdd:PRK08945   21 GDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPqPAIIPLDLltATPQNYQQLADTIEEQFGRLDGVLHNA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  92 G-WDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIA 170
Cdd:PRK08945  101 GlLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYAVSKFATEGMMQVLA 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444067332 171 REHARHDITVNVVCPGPTETAL----FEDYkqgagNPEKLveaftrsiplgriGQPDDLPGAVLFFAGDDAAFITGQVL 245
Cdd:PRK08945  181 DEYQGTNLRVNCINPGGTRTAMrasaFPGE-----DPQKL-------------KTPEDIMPLYLYLMGDDSRRKNGQSF 241
PRK08340 PRK08340
SDR family oxidoreductase;
27-252 1.17e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 51.34  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  27 ARAGAAVGVLDLNPEAGERVAAQIRDAGGrALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAgwdvfrPFVKTEPAQ 106
Cdd:PRK08340   21 LKKGARVVISSRNEENLEKALKELKEYGE-VYAVKADLSDKDDLKNLVKEAWELLGGIDALVWNA------GNVRCEPCM 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 107 WERLIAIN-LTGALHmhHAVLPGMVA----------RKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHAR 175
Cdd:PRK08340   94 LHEAGYSDwLEAALL--HLVAPGYLTtlliqawlekKMKGVLVYLSSVSVKEPMPPLVLADVTRAGLVQLAKGVSRTYGG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 176 HDITVNVVCPGPTET--ALFEDYKQGAGNPEKLVEAFTRSI----PLGRIGQPDDLPGAVLFFAGDDAAFITGQVLSVSG 249
Cdd:PRK08340  172 KGIRAYTVLLGSFDTpgARENLARIAEERGVSFEETWEREVlertPLKRTGRWEELGSLIAFLLSENAEYMLGSTIVFDG 251


                  ...
gi 1444067332 250 GLT 252
Cdd:PRK08340  252 AMT 254
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 21-141 3.93e-07

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 49.75  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGER-------VAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGW 93
Cdd:cd09762    18 AIALKAARDGANVVIAAKTAEPHPKlpgtiytAAEEIEAAGGKALPCIVDIRDEDQVRAAVEKAVEKFGGIDILVNNASA 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1444067332  94 DVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIA 141
Cdd:cd09762    98 ISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLS 145
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 82-253 4.82e-07

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


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 49.54  E-value: 4.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  82 GPIDVLVNNAGWDVFRPFV-----------KTEPAQWERLIAINLTGALHMHHAV---LPGMVARKAGR---IVNIASDA 144
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPLLrgdagegvgdkKSLEVQVAELFGSNAIAPYFLIKAFaqrQAGTRAEQRSTnlsIVNLCDAM 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 145 ARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGpteTALFEDykqgaGNPEKLVEAFTRSIPLG-RIGQPD 223
Cdd:TIGR02685 163 TDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPG---LSLLPD-----AMPFEVQEDYRRKVPLGqREASAE 234

                         170       180       190
                  ....*....|....*....|....*....|
gi 1444067332 224 DLPGAVLFFAGDDAAFITGQVLSVSGGLTM 253
Cdd:TIGR02685 235 QIADVVIFLVSPKAKYITGTCIKVDGGLSL 264
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 6-193 1.35e-06

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 48.23  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   6 GKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIR-DAGGRALSVR-CDITDRASVDAAVAAVEQELGP 83
Cdd:cd09807     1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRrDTLNHEVIVRhLDLASLKSIRAFAAEFLAEEDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  84 IDVLVNNAGwdVFR-PFVKTEPAqWERLIAINltgalHMHHAVLP----GMVARKA-GRIVNIASDAARVGS-------- 149
Cdd:cd09807    81 LDVLINNAG--VMRcPYSKTEDG-FEMQFGVN-----HLGHFLLTnlllDLLKKSApSRIVNVSSLAHKAGKinfddlns 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1444067332 150 ----SGEAVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALF 193
Cdd:cd09807   153 eksyNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELG 200
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 36-157 1.81e-06

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: 48.52  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  36 LDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINL 115
Cdd:cd08953   241 LPPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKV 320

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1444067332 116 TGALHMHHAVlpgmVARKAGRIVNIASDAARVGSSGEAVYAA 157
Cdd:cd08953   321 DGLLNLAQAL----ADEPLDFFVLFSSVSAFFGGAGQADYAA 358
PRK07806 PRK07806
SDR family oxidoreductase;
21-91 3.12e-06

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 47.02  E-value: 3.12e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1444067332  21 ATCLRFARAGAAVGVLDLN-PEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNA 91
Cdd:PRK07806   21 DTAKILAGAGAHVVVNYRQkAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGLDALVLNA 92
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 29-252 7.46e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 46.17  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  29 AGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVeQELGPIDVLVNNAGwdvfrpfVKTEPAQWE 108
Cdd:PRK06940   23 AGKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATA-QTLGPVTGLVHTAG-------VSPSQASPE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 109 RLIAINLTGAlhmhhAVLP---GMVARKAGRIVNIAS-------------------------------DAARVGSSGEAv 154
Cdd:PRK06940   95 AILKVDLYGT-----ALVLeefGKVIAPGGAGVVIASqsghrlpaltaeqeralattpteellslpflQPDAIEDSLHA- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 155 YAACKGGLVSFSKTIAREHARHDITVNVVCPGPTETALFEDYKQGAgnpeklVEAFTRSI----PLGRIGQPDDLPGAVL 230
Cdd:PRK06940  169 YQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAQDELNGP------RGDGYRNMfaksPAGRPGTPDEIAALAE 242

                         250       260
                  ....*....|....*....|..
gi 1444067332 231 FFAGDDAAFITGQVLSVSGGLT 252
Cdd:PRK06940  243 FLMGPRGSFITGSDFLVDGGAT 264
PRK05693 PRK05693
SDR family oxidoreductase;
21-216 7.94e-06

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 45.94  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  21 ATCLRFARAGAAVGVLDLNPEAGERVAAqirdAGGRAlsVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFV 100
Cdd:PRK05693   16 ALADAFKAAGYEVWATARKAEDVEALAA----AGFTA--VQLDVNDGAALARLAEELEAEHGGLDVLINNAGYGAMGPLL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 101 KTEPAQWERLIAINLTGALHMHHAVLPGMvARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHDITV 180
Cdd:PRK05693   90 DGGVEAMRRQFETNVFAVVGVTRALFPLL-RRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDALRLELAPFGVQV 168

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1444067332 181 NVVCPGPTETALFEDYKQGAgnpEKLVEAFTRSIPL 216
Cdd:PRK05693  169 MEVQPGAIASQFASNASREA---EQLLAEQSPWWPL 201
PRK07023 PRK07023
SDR family oxidoreductase;
86-176 9.26e-06

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 45.39  E-value: 9.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  86 VLVNNAGwdVFRPFVKTE---PAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIASDAARVGSSGEAVYAACKGGL 162
Cdd:PRK07023   80 LLINNAG--TVEPIGPLAtldAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAAL 157

                          90
                  ....*....|....
gi 1444067332 163 VSFSKTIAREHARH 176
Cdd:PRK07023  158 DHHARAVALDANRA 171
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 38-157 9.36e-06

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: 44.86  E-value: 9.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  38 LNPEAGERVAAqIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTG 117
Cdd:pfam08659  37 PRPDAQALIAE-LEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTG 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1444067332 118 ALHMHHAVLPgmvaRKAGRIVNIASDAARVGSSGEAVYAA 157
Cdd:pfam08659 116 TWNLHEATPD----EPLDFFVLFSSIAGLLGSPGQANYAA 151
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
87-230 9.38e-06

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 45.44  E-value: 9.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  87 LVNNAGW-DVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAG-RIVNIASDAARVGSSGEAVYAACKGGLVS 164
Cdd:PRK06924   84 LINNAGMvAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVDkRVINISSGAAKNPYFGWSAYCSSKAGLDM 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1444067332 165 FSKTIAREHARHDITVNVVC--PGPTETALFEDYKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVL 230
Cdd:PRK06924  164 FTQTVATEQEEEEYPVKIVAfsPGVMDTNMQAQIRSSSKEDFTNLDRFITLKEEGKLLSPEYVAKALR 231
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 60-214 5.31e-05

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: 42.95  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  60 VRCDITDRASVDAAVaaveQELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVN 139
Cdd:cd11731    35 YQVDITDEASIKALF----EKVGHFDAIVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSITL 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1444067332 140 IASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARhDITVNVVCPGPTETAL--FEDYKQG--AGNPEKLVEAFTRSI 214
Cdd:cd11731   109 TSGILAQRPIPGGAAAATVNGALEGFVRAAAIELPR-GIRINAVSPGVVEESLeaYGDFFPGfePVPAEDVAKAYVRSV 186
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 40-186 6.72e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 43.45  E-value: 6.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  40 PEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGPIDVLVNnagwDVF--RPFVKTEPAQWERliaiNLTG 117
Cdd:PRK08303   52 PETIEETAELVTAAGGRGIAVQVDHLVPEQVRALVERIDREQGRLDILVN----DIWggEKLFEWGKPVWEH----SLDK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 118 ALHM------------HHAvLPGMVARKAGRIVNIASDAARVGSSG---EAVYAACKGGLVSFSKTIAREHARHDITVNV 182
Cdd:PRK08303  124 GLRMlrlaidthlitsHFA-LPLLIRRPGGLVVEITDGTAEYNATHyrlSVFYDLAKTSVNRLAFSLAHELAPHGATAVA 202


                  ....
gi 1444067332 183 VCPG 186
Cdd:PRK08303  203 LTPG 206
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-250 7.75e-05

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 42.83  E-value: 7.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRcDITDRASVDAAVAAVEQELGP 83
Cdd:PRK05786    3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIHYVVG-DVSSTESARNVIEKAAKVLNA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  84 IDVLVNNAGWDVFRPFvkTEPAQWERLIAINLTGALHMHHAVLPGMvaRKAGRIVNIAS-DAARVGSSGEAVYAACKGGL 162
Cdd:PRK05786   82 IDGLVVTVGGYVEDTV--EEFSGLEEMLTNHIKIPLYAVNASLRFL--KEGSSIVLVSSmSGIYKASPDQLSYAVAKAGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 163 VSFSKTIAREHARHDITVNVVCPGptetalfedYKQGAGNPEKlveAFTRSIPLGRIGQ-PDDLPGAVLFFAGDDAAFIT 241
Cdd:PRK05786  158 AKAVEILASELLGRGIRVNGIAPT---------TISGDFEPER---NWKKLRKLGDDMApPEDFAKVIIWLLTDEADWVD 225


                  ....*....
gi 1444067332 242 GQVLSVSGG 250
Cdd:PRK05786  226 GVVIPVDGG 234
PRK08251 PRK08251
SDR family oxidoreductase;
63-190 2.38e-04

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 41.46  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  63 DITDRASVDAAVAAVEQELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGALHMHHAVLPGMVARKAGRIVNIAS 142
Cdd:PRK08251   61 DVNDHDQVFEVFAEFRDELGGLDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISS 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1444067332 143 DAARVGSSGE-AVYAACKGGLVSFSKTIAREHARHDITVNVVCPGPTET 190
Cdd:PRK08251  141 VSAVRGLPGVkAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRS 189
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 48-250 2.60e-04

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 41.07  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  48 AQIRDAGgrALSVRCDITDRASVDAAVAAVEQELGPIDVLVNNAG-WDVFRPfvKTEPAQ-WERLIAINLTGALHMHHAV 125
Cdd:PRK06483   41 DGLRQAG--AQCIQADFSTNAGIMAFIDELKQHTDGLRAIIHNASdWLAEKP--GAPLADvLARMMQIHVNAPYLLNLAL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 126 LPGM--VARKAGRIVNIASDAARVGSSGEAVYAACKGGLVSFSKTIAREHARHdITVNVVCPGpteTALF-----EDYKQ 198
Cdd:PRK06483  117 EDLLrgHGHAASDIIHITDYVVEKGSDKHIAYAASKAALDNMTLSFAAKLAPE-VKVNSIAPA---LILFnegddAAYRQ 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1444067332 199 gagnpeklvEAFTRSIpLGRIGQPDDLPGAVLFFAgdDAAFITGQVLSVSGG 250
Cdd:PRK06483  193 ---------KALAKSL-LKIEPGEEEIIDLVDYLL--TSCYVTGRSLPVDGG 232
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
159-251 3.45e-04

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 41.08  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332 159 KGGLVSFSKTIAREHARHDITVNVVCPGPTETALfedyKQGAGNPEKLVEAFTRSIPLGRIGQPDDLPGAVLFFAGDDAA 238
Cdd:PRK07533  166 KAALESSVRYLAAELGPKGIRVHAISPGPLKTRA----ASGIDDFDALLEDAAERAPLRRLVDIDDVGAVAAFLASDAAR 241

                          90
                  ....*....|...
gi 1444067332 239 FITGQVLSVSGGL 251
Cdd:PRK07533  242 RLTGNTLYIDGGY 254
PRK06720 PRK06720
hypothetical protein; Provisional
 4-92 6.52e-04

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 39.57  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332   4 LEGKTVIVTGGGGGIGGATCLRFARAGAAVGVLDLNPEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVEQELGP 83
Cdd:PRK06720   14 LAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVISITLNAFSR 93


                  ....*....
gi 1444067332  84 IDVLVNNAG 92
Cdd:PRK06720   94 IDMLFQNAG 102
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 40-157 3.01e-03

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: 38.52  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444067332  40 PEAGERVAAQIRDAGGRALSVRCDITDRASVDAAVAAVeQELGPIDVLVNNAGWDVFRPFVKTEPAQWERLIAINLTGAL 119
Cdd:cd05274   187 APRAAARAALLRAGGARVSVVRCDVTDPAALAALLAEL-AAGGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGAL 265

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1444067332 120 HMHHAVLPGMVArkagRIVNIASDAARVGSSGEAVYAA 157
Cdd:cd05274   266 NLHELTPDLPLD----FFVLFSSVAALLGGAGQAAYAA 299
 
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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