Conserved Protein Domain Family
hydroxyacyl_CoA_DH

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cd08254: hydroxyacyl_CoA_DH 
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members
This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.
Statistics
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PSSM-Id: 176216
View PSSM: cd08254
Aligned: 37 rows
Threshold Bit Score: 256.019
Threshold Setting Gi: 111223437
Created: 29-Apr-2009
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
Feature 1:putative NAD(P) binding site [chemical binding site]
Evidence:
  • Comment:MDR family binds NAD(P) as a cofactor
  • Comment:defined by comparison to MDR alcohol dehydrogenase like family

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                  ###  #                     
YP_463072          14 VAPWRKnketgekipgqlqlteiPVPELke-----------gDVLVKIAGCGVCHTDLGFFfdavp--tvtkpPLTLGHE 80  Syntrophus...
NP_713534           6 MKAAVLesgkki-----leirdvSVPQLra-----------eQVKVRIKACGICGSDVHLVvhgtl--kckhfPRVPGHE 67  Leptospira...
CAI78859            1 MKAVVFhgkdag-----lkiediPVPQIkg-----------dQILVKVAACGVCHTDLHYIehgvp--tfkkpPIVLGHE 62  uncultured...
YP_421507          21 ISAYRWmmtgvgqp-mvkeameiAAPGAg-------------EVLVEVAGCGVCHTDLDYYyngvr--tnhalPLALGHE 84  Magnetospi...
YP_704875           5 MRAQRFhadtkt-----iavedvPIPEPgp-----------gEVLVKVEFCGICHSDLSLIdgtfp---tllpEVTQGHE 65  Rhodococcu...
YP_001840634        1 MKAAVLpsgsrsle--iqeldlpPLPPN--------------QVKVKVKACGICGSDIHFIlhgkm--katysPCVPGHE 62  Leptospira...
ZP_06348637         3 IAAYRWvm--------------tSVGEPlirqsfelgapaagEVTVEIAGCGVCHTDLGYYydgvr--tnqplPLTLGHE 66  Rhodomicro...
NP_821749           4 MLAGRFhldskkf---aveevpvPVPGPg-------------EVLIEVKAAGVCLSDVHLIdgslvplfatsdTVTVGHE 67  Streptomyc...
REF_jgi:Gbem_1431   3 KSAYRWsmtavgep--mqkgefaPAPGAg-------------EVVVEVAGCGVCHTDLGFYysgvr--fnhpaPLTLGHE 65  Geobacter ...
NP_624954           4 MLAARLhvpsrt-----lrleevPRPQPgp-----------gEVLVKVEAAGVCLSDVHLIdgtltplllrgdTVTLGHE 67  Streptomyc...
Feature 1                                                                                             
YP_463072          81 VSGTVVAGDPKW-----IGKEVlipavlpCRKCELCKTGRGNRClnqmfigcshgiyGGNSDYIPVpSLDLCEIKNRps- 154 Syntrophus...
NP_713534          68 SSGIIEEVGENVrr-frKGDRVviaagtsCGVCSYCKEGKENLCkdlgvf--gfdrdGSFAEFNIVeERYLYSLPDE--- 141 Leptospira...
CAI78859           63 ASGIVEKAGANVtn-vkPGQRVlipavltCGHCPACRQGRENICsnmtml--gnhfdGAYAEYVAVpAKDVLGLPEA--- 136 uncultured...
YP_421507          85 ISGRVIQAGAGAes--wVGKAViisavipCGQCDLCKRGKGTICrsqkmp--gndlqGGFATHITVpANGLCAVDEArlk 160 Magnetospi...
YP_704875          66 ASGTIAKLGAGVtg-wsEGDRVvpsagrpCFGCRNCRRGDLTNClniqlm--afaydGAWAEYTVAqAGGLTRIPDN--- 139 Rhodococcu...
YP_001840634       63 TSGVVAEIGDQVtk-fkLGDRVvvsagtsCGKCKHCLAGRENLCenigvi--gfnqrGGFAEFIQTeERYLHLLPEE--- 136 Leptospira...
ZP_06348637        67 ISGRVVAAGTGAeh--wLGRAViipavipCGTCDACKRGKGTICakqvmp--gndieGGFASHITVpSFGLCAVNENrle 142 Rhodomicro...
NP_821749          68 VSGVIHTLGPDLkrgltVGTRVtleagktCGQCAGCVRSRPCTQmrtag----idydGGWAQYTVArEDTLIPIPDN--- 140 Streptomyc...
REF_jgi:Gbem_1431  66 ISGRVVTAGEGAgq--wVGKAVlipavipCGECDLCLSSHGTICraqqmp--gndihGGFASHIVVpAKTLCPVDEKrla 141 Geobacter ...
NP_624954          68 VSGTVAGTGAGVta-wsPGQRVvl----hAGERRDGVTYTRGVDy-----------dGGWAEYALCaADAMTPLPDA--- 128 Streptomyc...
Feature 1                          #   #                    ######                 ##    #            
YP_463072         155 --tRPLENYSVASDAVTTPYQAMIKAKvGIGDNVIVIGATGGVGLYTAQIAKAMGAdvVIGIDIaeqKLQKMLNYGCDFV 232 Syntrophus...
NP_713534         142 ---IPFDQGAILADAVSTPYHAIRYRGnIQESDTVAIFGCGGLGIHAVAIARAMTKgkVIALDVdsgALENATKYGADEV 218 Leptospira...
CAI78859          137 ---IPLQEASIIADAISTPYHAVKNRAqVKPGDTVVVFGCGGVGINAVQMASAAGGy-VIAVDInprKLEWAREFGAAKT 212 uncultured...
YP_421507         161 aagLELSEVSVVADALTTPYQAAVQAG-IGQGDLVIVIGCGGVGGYSVQVASAMGAt-VVALDIdpvKLEAVKAAGAKLT 238 Magnetospi...
YP_704875         140 ---VPFEQAAILADAVSTPFGAVVRTGkVVVGETVGVWGVGGVGTHIVQLARLVGAvpVIAFDInpaVRERALELGADYA 216 Rhodococcu...
YP_001840634      137 ---IPFAEGAILADAVSTPYHAIKYQGeLKAGESVAIIGCGGLGIHAVAIAKALGAakIYAIDIdsgSLENAKAYGADEL 213 Leptospira...
ZP_06348637       143 aagLKLSDVSVVADAVTTPYQAVIQAG-VGPGTLCIVIGVGGVGGHCAQVASAFGGt-VVAIDVddvKLAAIAAHGVAKT 220 Rhodomicro...
NP_821749         141 ---LPFDQAAIIPDAVSTPYAAVVTTAgVRPAQSVGVWGVGGVGAHNVRLARLAGAapIIAVDPlpsARERALAFGADFA 217 Streptomyc...
REF_jgi:Gbem_1431 142 aagLELADISVVADAVTTPYQAAVQAE-VQPGDVAIVIGVGGVGGYAVQVANALGAt-VIAIDVdpvKLENVGKHGAALT 219 Geobacter ...
NP_624954         129 ---IPFEQGAIIPDAVSTPWGAITETGeVRPAEAVGVWGVGGLGVHAVQLLRAIGAcpVVAVDPspvARERALAAGADLA 205 Streptomyc...
Feature 1               #                               ## #                   ##                     
YP_463072         233 IMNKdksnkdvmgeyr-aickanalpnyGWKIFEVSGNkfGQALALDLLSfTGTMVQIGYGLGSIDFnv-srLMAFDAQI 310 Syntrophus...
NP_713534         219 VNLKevrnsgkv---------lkevskgVDLLADFSGYmsNVEDSIRAMNpGGRIVLVGIGRQPLKFqipfiLIEKMISV 289 Leptospira...
CAI78859          213 VDASkvdrvske--------ikkltgggADIAMEVIGNprTIEQAFECVRvGGRLCVVGYTHEAISIva-gkIMFKELEI 283 uncultured...
YP_421507         239 LNPKdfpstreikkeigafakaqglrstEWIIMECSGSvpGQQSAFDLMVhGCTICVVGYTMNKAEFrl-snLMAFHARA 317 Magnetospi...
YP_704875         217 FDSRdenlkekv--------aeatggrmLDVAFDAAGLkvTFEQALDCLTvGGRLVAVGLSAQEASVgttaqFGLSQKQV 288 Rhodococcu...
YP_001840634      214 ILVEknmqvgkv---------lkeksggIDLLCDFTGYmpNIESSVRAMNrGGRIVLVGIGRNKLEIpmpffLIERQIRI 284 Leptospira...
ZP_06348637       221 FNARrvdpkalkkeia-gfakenglstrEWVIFECSGTaaGQSTAWSLLVhGATLAVVGFTMDKVEVrl-snLMAFHARA 298 Rhodomicro...
NP_821749         218 LDPAaddfadqi--------raatagrgLDFAFDCAGVpaVREQAAAALGlGGVLILVGISPRPLTItegltFNYLGKQV 289 Streptomyc...
REF_jgi:Gbem_1431 220 LNSReiagkelkkain-dfvkakglkqtCWKIFECSGStpGQETAFSLLTyGATLSVVGFTMDKIELrl-snLMAFHARA 297 Geobacter ...
NP_624954         206 LDSAdpefrqkv--------gaatggagLAAAFDFAGVppVREQAVSVLApKGRLVLAGLTDKPLTVtdgtrFSYLQQRI 277 Streptomyc...
Feature 1               ###                                                       
YP_463072         311 IGTWACLp-eYYPHVLSLIHSGKIQIdp-fLEVRPMSTIAATYDEVHKAGspEKRIVLKP 368 Syntrophus aciditrophicus SB
NP_713534         290 SGSYGSDr-rAIPELIELYLKGKINLshsiTSHHPLEELNECLEALDQRKgnPIRFIVEP 348 Leptospira interrogans serovar...
CAI78859          284 VGSLGCRp-vDYVPLIRMVEQGKIDLkrqvTHRFGLDELGQAFEVMKEGL--SLRSIVIP 340 uncultured bacterium
YP_421507         318 LGNWGCPp-dLYPGALDLVLSGKINVkn-fVERRPLDSINDTFAAVHDHKl-SRRAVLCP 374 Magnetospirillum magneticum AMB-1
YP_704875         289 LGHLGYKn-vDIETLAELVSRGRLDLsrsiSEIVPLEDVAKGIEKLANHEgdPIRILVKP 347 Rhodococcus sp. RHA1
YP_001840634      285 TGSYGSDr-rAIPELIQLYQEKKLNLtksiSGIHKLEDTNEFLHALEEKKgnPIRFIINP 343 Leptospira biflexa serovar Pat...
ZP_06348637       299 LGNWGCAt-eLYPGALDLVLDRKIELaa-fIERHPLDSINEIFAMAHEHKl-TRRAILVP 355 Rhodomicrobium vannielii ATCC ...
NP_821749         290 RGHYGGSp-eSVTELVRLAEVGRLDLapsiTDHLPLAEAADAVNRLENKIgdPIRLILVP 348 Streptomyces avermitilis MA-4680
REF_jgi:Gbem_1431 298 LGNWGCLt-eLYPAALDLVLDGKVALtp-fIEKHPLDNINQVFASAHAHKl-TRRAILVP 354 Geobacter bemidjiensis Bem
NP_624954         278 LGHYGSDmpvALPQLLRLIQGGRLDFsgsvSGVLPLAEAAEAVARLEKKEgdPIRLVLRP 337 Streptomyces coelicolor A3(2)

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