1FDU,1IOL,1FDW,1FDS,1EQU,1A27


Conserved Protein Domain Family
type1_17beta-HSD-like_SDR_c

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cd09806: type1_17beta-HSD-like_SDR_c 
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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.
Statistics
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PSSM-Id: 187666
View PSSM: cd09806
Aligned: 10 rows
Threshold Bit Score: 439.203
Threshold Setting Gi: 157831055
Created: 21-Jan-2011
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                     
1FDU_A      3 TVVLITGCSSGIGLHLAVRLASDPsqsFKVYATLRDLKTQgRLWEAARalacppgslETLQLDVRdsKSVAAARERVteg 82  human
1IOL_A      3 TVVLITGCSSGIGLHLAVRLASDPsqsFKVYATLRDLKTQgRLWEAARalacppgslETLQLDVRdsKSVAAARERVteg 82  human
1FDW_A      3 TVVLITGCSSGIGLHLAVRLASDPsqsFKVYATLRDLKTQgRLWEAARalacppgslETLQLDVRdsKSVAAARERVteg 82  human
1FDS_A      3 TVVLITGCSSGIGLHLAVRLASDPsqsFKVYATLRDLKTQgRLWEAARalacppgslETLQLDVRdsKSVAAARERVteg 82  human
1EQU_A      3 TVVLITGCSSGIGLHLAVRLASDPsqsFKVYATLRDLKTQgRLWEAARalacppgslETLQLDVRdsKSVAAARERVteg 82  human
1A27_A      3 TVVLITGCSSGIGLHLAVRLASDPsqsFKVYATLRDLKTQgRLWEAARalacppgslETLQLDVRdsKSVAAARERVteg 82  human
AAH82456    6 KTVLITGCSSGIGLAIAAKLARDEqkrFKVYATMRNLAKKdDLVGATEgylg--ktmEIKEMDVCseDSIRNCVRSIpdr 83  African clawed frog
AAP74566    8 KVVLITGCSSGIGLRIAVLLARDEqkrYHVIATMRDLKKKdRLVEAAGevyg--qtlTLLPLDICsdESVRQCVNSVkdr 85  zebrafish
NP_990168  11 TTVLITGCSSGIGLGLAVRLAADAarrFKVFATMRDLAKGeQLLERLGgrcp--dtlELLQLDVTdpRSLAAAVRCMrgr 88  chicken
Q9NYR8      6 RTVLISGCSSGIGLELAVQLAHDPkkrYQVVATMRDLGKKeTLEAAAGealg--qtlTVAQLDVCsdESVAQCLSCIqg- 82  human
Feature 1                                    #                           #            #   #   
1FDU_A     83 rVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRgSGRVLVTGSVGGLMGLPfNDVYCASKFAL 162 human
1IOL_A     83 rVDVLVCNAGLGLLGPLEALGEDAVASVLEVNVVGTVRMLQAFLPDMKRRgSGRVLVTGSVGGLMGLPfNDVYCASKFAL 162 human
1FDW_A     83 rVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRgSGRVLVTGSVGGLMGLPfNDVYCASKFAL 162 human
1FDS_A     83 rVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRgSGRVLVTGSVGGLMGLPfNDVYCASKFAL 162 human
1EQU_A     83 rVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRgSGRVLVTGSVGGLMGLPfNDVYCASKFAL 162 human
1A27_A     83 rVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRgSGRVLVTGSVGGLMGLPfNDVYCASKFAL 162 human
AAH82456   84 hIDILVSNAGVGLIGPIECQTIDEMKTVMDTNFFGLVRLLKEILPDMKKRkSGHIVIISSVMGIQGILfNDVYAASKFAV 163 African clawed frog
AAP74566   86 hIDVLINNAGVGLLGPVESISMDEMKRVFETNFFGTVRMIKEVMPDMKKRqAGHIIVMSSVMGLQGVVfNDVYTASKFAI 165 zebrafish
NP_990168  89 hPDVLVCNAGVGLMAPLEMCSEQAMRAVFEVNVFGTARTIQAFLPAMKRHrAGRILVSSSVGGLQGLPfNAVYCASKFAL 168 chicken
Q9NYR8     83 eVDVLVNNAGMGLVGPLEGLSLAAMQNVFDTNFFGAVRLVKAVLPGMKRRrQGHIVVISSVMGLQGVIfNDVYAASKFAL 162 human
Feature 1                                                                                     
1FDU_A    163 EGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLgspeevldrt--dihtfhrfyqYLALSKQVFreaaQNPEEVAEVF 240 human
1IOL_A    163 EGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLgspeevldrt--dihtfhrfyqYLAHSKQVFreaaQNPEEVAEVF 240 human
1FDW_A    163 EGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLgspeevldrt--dihtfhrfyqYLAQSKQVFreaaQNPEEVAEVF 240 human
1FDS_A    163 EGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLgspeevldrt--dihtfhrfyqYLAHSKQVFreaaQNPEEVAEVF 240 human
1EQU_A    163 EGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLgspeevldrt--dihtfhrfyqYLAHSKQVFreaaQNPEEVAEVF 240 human
1A27_A    163 EGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLgspeevldrt--dihtfhrfyqYLAHSKQVFreaaQNPEEVAEVF 240 human
AAH82456  164 EGFCESLAIQALKFKLQLSLIEPGPVITEFEKKVFedgmkmdlsaadketadmftniYLKNYKSIFqslgQTAEDVAEHT 243 African clawed frog
AAP74566  166 EGFCESMAVQLLKFNVKLSLIEPGPVHTEFETKMMeevakmeypgadpdtvryfkdvYVPSSIDIFeamgQTPDDIAKCT 245 zebrafish
NP_990168 169 EGLCESLAIVLRPFNIHMTLVECGPVHTAFMDNAWradpdgrelraldaetqqlyrrYLQHCTQLFldaaQEVDEVLQVF 248 chicken
Q9NYR8    163 EGFFESLAIQLLQFNIFISLVEPGPVVTEFEGKLLaqvsmaefpgtdpetlhyfrdlYLPASRKLFcsvgQNPQDVVQAI 242 human
Feature 1                         
1FDU_A    241 LTALRapkPTLRYFTTERFL 260 human
1IOL_A    241 LTALRapkPTLRYFTTERFL 260 human
1FDW_A    241 LTALRapkPTLRYFTTERFL 260 human
1FDS_A    241 LTALRapkPTLRYFTTERFL 260 human
1EQU_A    241 LTALRapkPTLRYFTTERFL 260 human
1A27_A    241 LTALRapkPTLRYFTTERFL 260 human
AAH82456  244 MKIVLsenPPFRHQTNTLYT 263 African clawed frog
AAP74566  246 KKVIEtsqPRFRNLTNSLYT 265 zebrafish
NP_990168 249 LEAIAaprPPLRCITARLPA 268 chicken
Q9NYR8    243 VNVISstrPPLRRQTNIRYS 262 human

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