1IYZ,2CF2


Conserved Protein Domain Family
QOR1

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cd08241: QOR1 
Click on image for an interactive view with Cn3D
Quinone oxidoreductase (QOR)
QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 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 has 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: 176203
View PSSM: cd08241
Aligned: 88 rows
Threshold Bit Score: 269.754
Threshold Setting Gi: 93279105
Created: 21-Jul-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
NAD(P) binding
Conserved site includes 23 residues -Click on image for an interactive view with Cn3D
Feature 1:NAD(P) binding site [chemical binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                       ##                                
1IYZ_A          1 MKAWVLKRLGGP-----LELVDL--PEPEae--eGEVVLRVEAVGLNFADHLMRLGAYLt---rLHPPFIPGMEVVGVV- 67   Thermus therm...
2CF2_D          1 MKAWVLKRLGGP-----LELVDL--PEPEae--eGEVVLRVEAVGLNFADHLMRLGAYLt---rLHPPFIPGMEVVGVV- 67   pig
XP_756192       1 MRAFYLHKDIAPsellsTLVNDA--PEPKvtagsNEVLVDVHSAAFNFFDILAVQGKYQv---kTPHPYVPGVEMAGIIs 75   Ustilago mayd...
EAA61908        1 MRAIQVKEYVKGpl--dLTVSTL--PTPSps--pSAYLIEIHSAGTNFFDLLQIRGKYQh---qPPLPWISGSEFAGTIa 71   Aspergillus n...
XP_001877727    1 MRAFVIKKLSHPsn--iSLSIDV--PEPQpd--qRQVIVDVYSAGLNFFDILQAQGKYQn---kPALPFTLGSEFAGRIa 71   Laccaria bico...
XP_002108074   30 YRAAFCAQTNKP-----LVIKKVy-DTKQlg--pSELRIRIRACAINFADILMCQGAYQe---kPNLPFIPGTEIAGDIi 98   Trichoplax ad...
XP_001791528  272 MKAVKVDSFVTDlt--vLQPKDVptPTPSs---kDELTIKITHAAITHVDLLYAQGLHQnnkrhVQPPFILGNEFSGIVt 346  Phaeosphaeria...
EEY17872        1 MKAIVIDEFVTKle--qIHTTEVptPTPAq----DGFLIEVEAAGVNFVDILYAQGKHQnnrslVRPPFTLGLELAGTIl 74   Verticillium ...
NP_294785      64 MKAIVVERIGTPd---vMELREV--PRPApr--aGQVLLRVEAVGVNFADALSVGGQYLt---aTKVPYVPGMELAGTVv 133  Deinococcus r...
YP_589271       1 MKALLVEQLGKLe---sLALRDV--PDPQvk--pDRVVVNIEAAGVNFADISSSMGKYPg----VKVPYIAGREFAGTVe 69   Acidobacteria...
Feature 1                                                                #   #                    
1IYZ_A         68 -------------EGRRYAAlvpqGGLAERVAVPKg-aLLPLPEGLSPeeAAAFPVSFLTAYLALK-RAQA--------R 124  Thermus therm...
2CF2_D         68 -------------EGRRYAAlvpqGGLAERVAVPKg-aLLPLPEGLSPeeAAAFPVSFLTAYLALK-RAQA--------R 124  pig
XP_756192      76 kdspipegcdfipGKTRVFGaa-qGAYGEKTKADYw-qLMEVPEGITLeqAAGLFVTWPTSYAALKfRADV--------Q 145  Ustilago mayd...
EAA61908       72 avptts-gpwkykVGDRVFGat-qGAYATHVLAPEs-aLLPVPQGWSFedAAGLFVTAPTSYGGLVhRANV--------Q 140  Aspergillus n...
XP_001877727   72 knspip-kgcpykAGDRVFGas-qGAFADKVSVDWe-rLITLPDNVSFdqGAGLFITWPTSYEALVgRAEL--------K 140  Laccaria bico...
XP_002108074   99 eigsn---vttfkKGDKVLAlvnlHGFAEQCITDVd-aTWKIPNTVSYatAATLVVSYATAYMAFDrRAEL--------K 166  Trichoplax ad...
XP_001791528  347 sspp----tssfkPGTKVFGgg-lGSYAESICVPEa-aVRRVPAQWSLaeACAVGASGAVSYGALVsVAQV--------K 412  Phaeosphaeria...
EEY17872       75 saps----rstfkPGDKVFAgh-tGAYSEVIALPStavVRRIPSSWDVsgAAGIAATLPVAYGAFV-RAGL--------Q 140  Verticillium ...
NP_294785     134 elgeg---vtnvqVGQRVAAlggtGGLAEYAAVPAa-gVVPVPESFTPaqAAAFPVSFMTAYHALKtLGRG--------E 201  Deinococcus r...
YP_589271      70 ------------gTGERVMGytqmGAFAEKIAIPRa-fIWPQPQGWTSveSAAFPVNFFTAYLVYW-KAGLtadafepaA 135  Acidobacteria...
Feature 1                    #  ###                   ##   #               #                      
1IYZ_A        125 PGEK---VLVQAAAGALGTAAVQVAR-AMGLRVLAAASRpEKLALPLAl-GAEEAATYa---eVPERAKa---------- 186  Thermus therm...
2CF2_D        125 PGEK---VLVQAAAGALGTAAVQVAR-AMGLRVLAAASRpEKLALPLAl-GAEEAATYa---eVPERAKa---------- 186  pig
XP_756192     146 PDEW---VLVHAGAGGVGICAIQIAK-AMGAKVIATAGSdDKLRVCKQfgGADYAVNYrd-kdWQAQVKki-------te 213  Ustilago mayd...
EAA61908      141 PGEW---VLVHAAAGGVGLAAVQIAK-ARGATVIATAGTeRKREVAKAf-GADYVIDYrd-kaWPEKVKalcaehrsgng 214  Aspergillus n...
XP_001877727  141 PGEW---VLVTAAAGGVGIAAVQIAK-ALGAKVIAAAGSeAKLDVAKRigGADYGVDYskpawYKEVLEit--------g 208  Laccaria bico...
XP_002108074  167 KGET---VLVTAAAGGTGLAAVDLGAnVFGANVIGAAGSaEKTALAKVk-GAMHAINY-----REQDIKtevl---sitk 234  Trichoplax ad...
XP_001791528  413 SGET---VLVLGASGGLGVMAIQIAK-GLGAKVIAVVGSaEKARVVREi-GADGVVDYrd-gkWEDGVKalt------qd 480  Phaeosphaeria...
EEY17872      141 PGQT---VLVHAAAGGLGIMAVQVAK-AMGCRVIGTAGSaEKCAVARKy-GAEACINYsdekeWWKRVLdl-------tg 208  Verticillium ...
NP_294785     202 AGEW---VLVQAAAGALGTASVQLAK-ALGMNVIALASTeEKLQLARNl-GADVTILQdd-pdRVQKVRda-------ag 268  Deinococcus r...
YP_589271     136 PSKSprrALIHAVAGGVGTAAVQIGK-LLGIETIGTSSSdEKLEKAKAl-GLTHGINYsh-ddYQQRVMel-------tn 205  Acidobacteria...
Feature 1                  #                     ## ##                      ###                   
1IYZ_A        187 WGGLDLVLEVRGKe-VEESLGLLAHGGRLVYIGAAEGevap--ippLRLMRRNLAVLGFWLTpllreg---alveeaLGF 260  Thermus therm...
2CF2_D        187 WGGLDLVLEVRGKe-VEESLGLLAHGGRLVYIAPIPP---------LRLMRRNLAVLGFWLTpllre-----galveEAL 251  pig
XP_756192     214 GHGVDVVYDPVGM--IVPSLKVIAWNGRIIVVGFAAGtiek--ipaNLILLKNVAVTGVHWGayvrnepdkigetweALL 289  Ustilago mayd...
EAA61908      215 KAGVDVVYDPVGM--IDLSLKCVAWNARLLVIGFAAGsiek--valNRVLLKNVSIVGLHWGqyakfetetvgavwkGIF 290  Aspergillus n...
XP_001877727  209 GKGVDVIYDPVGL--INDSLKCIAWKGRALVVGFAAGtiek--vpmNLVLLKNVSLVGVHWGaytikesgripvvwkELL 284  Laccaria bico...
XP_002108074  235 RKGVDVVFDAVGGdtFEKCLRCTGFGGRLLTIGYASGsi-----pkGSYRFKDPKLYKHSID---------------SVV 294  Trichoplax ad...
XP_001791528  481 GEGVDVVYDGIGA--VESGLKCLKYRGRLVVVGFAARggnienvraNRILLKSAMVHGYRFGedgrhdprrtkdgweAFM 558  Phaeosphaeria...
EEY17872      209 GDGVDVVFDPVGL--LNLSLKCTAHFGKLLIVGFAGGeien--vpaNRLLLKQASLIGYRFGetlrrspeedevlwsGLQ 284  Verticillium ...
NP_294785     269 GKGVPLLLEVVGGsrFDESLKMVAPLGRIIFIGNASReevs--mnpAALMKRNVSVIGLWLTslmldae-vsaaasqGLA 345  Deinococcus r...
YP_589271     206 GEGVDCVFEMLGGehTKRSTRCTREFGRVILYGTATGerpe--fdtLTMYSKSISVHGLWLStlannre-viaaawiALK 282  Acidobacteria...
Feature 1                                            # # #     
1IYZ_A        261 LLPRLGRElRPVvg---pVFPFAEAe-AAFRALLDRGHTGKVVVR 301  Thermus thermophilus
2CF2_D        252 GFLLPRLG-RELrpvvgpVFPFAEAe-AAFRALLDRGHTGKVVVR 294  pig
XP_756192     290 DMFKTKKV-TPTvfe-hiYEGLESVp-EGLKDLADRKTWGKAVVR 331  Ustilago maydis 521
EAA61908      291 DLIAQGKF-RGTafrdesFVGLESVp-RALQALGGRETWGKVVVR 333  Aspergillus nidulans FGSC A4
XP_001877727  285 DLFASNRV-KPVtf--tkVYALDEVt-NGLAALERRETWGKAVVR 325  Laccaria bicolor S238N-H82
XP_002108074  295 RLLGEGKI-HPHvg---aSFPLNKIn-EAFQFIKDRKSTGKIAIT 334  Trichoplax adhaerens
XP_001791528  559 KMVDQGKI-KPViyk-edYRGLESVs-RALEDAKTHKAWGRAILR 600  Phaeosphaeria nodorum SN15
EEY17872      285 SLIDSGAV-VPV------VYDTRYSglDSVPQAGSPRHDGQEAEP 322  Verticillium albo-atrum VaMs.102
NP_294785     346 PLIASGKV-VPQvg---pSYGLADSs-RAFQDILDRKTTGKVVIE 385  Deinococcus radiodurans R1
YP_589271     283 PWVEAGQL-KPEvg---hVMPMANAs-EAYKLMLNRKNYGKIILT 322  Acidobacteria bacterium Ellin345

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