1QOR,1WLY,3JYL


Conserved Protein Domain Family
QOR2

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cd05286: QOR2 
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Quinone oxidoreductase (QOR)
Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. 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 actin 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. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. 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: 176189
View PSSM: cd05286
Aligned: 133 rows
Threshold Bit Score: 321.697
Threshold Setting Gi: 116622335
Created: 1-Aug-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
NADP bindingdimer interface
Conserved site includes 27 residues -Click on image for an interactive view with Cn3D
Feature 1:NADP binding site [chemical binding site]
Evidence:
  • Structure:1QOR_A: Escherichia coli quinone oxidoreductase binds to NADPH, contacts at 4A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                              ##   #                                    
1QOR_A         3 TRIEFHKHGGPEVLQAVefTPADPAENEIQVENKAIGINFIDTYIRSGLYPpp------sLPSGLGTEAAGIVSKVGsgv 76  Escherichia coli
NP_966679      3 RAIQIKKTGGPEVLEFVdkSIGEPKGEEVLVRHTTIGLNRYDLEHRKGTRKik------nLPSVLGVEAVGVIEKLGkki 76  Wolbachia endos...
YP_154093      6 KAVVIDRNGDAGVLKYVdvDVGEPGKGEVLIEHTAIGLNRYDVEYRTGTRKvp------sFPAVLGVEAVGVVRQLGpgv 79  Anaplasma margi...
YP_303262      3 KIIVIDKTGGTEVFKYVdhNIGEPKDDEVLIQHTVIGLNRYDLECRNGMRKtr------kLPTVLGIEAVGVVERLGkdv 76  Ehrlichia canis...
YP_504872      3 RTVVIEKTGGPEVMQFVdvEIGEPGRGEVLVEHTAIGLSRFDVECRAGIRKvk------sLPYTPGVQAVGVVKKVGpdv 76  Anaplasma phago...
YP_506269      3 KALLIEKTGGPEVFKSVdiNFRAPKSDEALIRHTAIGINYIDIEQRSGFYNlhentsrrkLPAIVGCQGVGVIKELGega 82  Neorickettsia s...
YP_775944      8 TRIGIDRYGDAGVLRRVdaPVAPPGAGEVRIRQTAIGVNFVDIYFRTGAHPlp------aLPDALGVEAAGMVDAVGpgv 81  Burkholderia am...
YP_001416605   8 HEVRIAAYGAADALVLQevDLPAPGAGEVLVRQHAVGINFIDIYHRRGVFPip------hLPGAIGVEAAGVVEEVGpgv 81  Xanthobacter au...
YP_001892342   4 RLIQLGEPGPALGLQPAdqMLPPPGANVLTVRHTAVGVNFVDVYHRTGLYPvp------aFPAVLGVEGVGVVEAVGtdv 77  Ralstonia picke...
YP_003087784  13 GIVKIYKQGAPSVLGYEreTMTEPGPGQVRIRQEAIGLNFVDTYYRDGKFPvr------sFPYTPGVEAAGIIEAVGpwv 86  Dyadobacter fer...
Feature 1                                                          #   #  #                   #  
1QOR_A        77 k-hikAGDRVVYaqs---alGAYSSVHNIIAdkAAILPAaisfEQAAASFLKGLTVYYLLRKTyei--kpDEQFLFHAAA 150 Escherichia coli
NP_966679     77 sdglkVGDRVGYcta---ppGAYCEKRIIHQkyLIKIPDdisdEVAAAVLFKGMTAHYLVNQSykv--rpGAFVLVHGAN 151 Wolbachia endos...
YP_154093     80 e-alnVGDRVGYcta---pgGAYSETRLINQkyLFKIADdisdEVAAAVMLKAMAAHYLTHRIydi--rpGTFALVHGVS 153 Anaplasma margi...
YP_303262     77 e-vfnVGDRVGYctv---sgGAYSEKRIVNQkyLVRIPDdvtdQVAAAVLFKGMTAHYLTHIVyai--rpKTFALVHGAT 150 Ehrlichia canis...
YP_504872     77 e-alnIGDRVGYcta---sgGSYSEERIIDQkyLFKISDvvndEVAAACIFKAMTAHYLTHRVydv--rpGTFALVYGVS 150 Anaplasma phago...
YP_506269     83 vvdvqPGDRVCYati---pyGAYSEERVIKLkyLHKIPDflsdIDVAACLYSGMVSFYLTCRAylvmndfTVMVHAVDTD 159 Neorickettsia s...
YP_775944     82 t-alvPGQRVAYagl---ptGSYASLRTLPAerVVPVPDgvsdDAAAAGLLKGITVYMLLHRVrqv--gaGDTVLVHAAA 155 Burkholderia am...
YP_001416605  82 t-rlrAGDRVAYagp---pvGSYASARVLPEaaLVKLPDaisfEAAAALMLQGMTAHMLFTRVrrv--aaGDTVLVHAAA 155 Xanthobacter au...
YP_001892342  78 r-gfvVGQRVAWaglmdgapGGYASHRNIPAnrAIALPDalddETVAATLLRGITAHMLLTRVrqv--gvGDTVLVHAAA 154 Ralstonia picke...
YP_003087784  87 t-efhVGDRVGYhf----ipGAYAESRVVSTqqLVHIPDtmssEEAAALLVKGFTARMLVKEVhpv--kpGDVVLVHAAA 159 Dyadobacter fer...
Feature 1        ###                  ##   #              #                         ##           
1QOR_A       151 GGVGLIACQWAKALGAkLIGTVGTaQKAQSALkAGAWQVINYre--edLVERLKEItggKKVRVVYDSVGRdTWERSLDC 228 Escherichia coli
NP_966679    152 GGLGQIICQWAKDKKGvVIGSVSSdEKMKIALqSGCTYAINYnd--kdFVSKVMEItqnRRVGAVYDPIGYaTSKLSFES 229 Wolbachia endos...
YP_154093    154 GGVGQILCQWARYKGGkVIGVVESgARLGVAKeVGCAYVVNLkd--ddITKEVMTItgdRGVNVVYDPIGAaVSKMSFGV 231 Anaplasma margi...
YP_303262    151 GGVGQILCQWASYKGCkVIGVISSdDRANIALrSGCSYIVNCns--knFVEQVMEItqgTGVNVVYDSVGAlTSKESFAS 228 Ehrlichia canis...
YP_504872    151 GGVGNIICQWARHKGCeVIGVVGSdGYGVNIArDAGCSYVVNrsd-pgVAKEILSItkgKGVNVVYDPIGReVCHLSFSV 229 Anaplasma phago...
YP_506269    160 MGDMLCQWIRARAPGCkIIGTVGSmRKLELLKdIRCELLLNYledpevLREKVHKFtrgHGVNAVYDCIGKdTYMLSLNS 239 Neorickettsia s...
YP_775944    156 GGVGLLATQWARALGArVIGTVGSaAKAALVRaHGAEAVVDYre--edFVAAARAFgggAGVDYAIDGIGGdVLTRTLGA 233 Burkholderia am...
YP_001416605 156 GGLGLLLVQWAKALGArVIGTVGSpTKAEHALrAGCCDVILYke--qdFATETRRLtdgAGVDVVYEGLGGdVLLKSLDC 233 Xanthobacter au...
YP_001892342 155 GGLGVLLVQWAKRLGArVIGTVGSeAKAATALgHGADHVVLHrq--qdVREAVLQLtagEGVDYVIDGVGGpMLQTSLAV 232 Ralstonia picke...
YP_003087784 160 GGVGALVTKWAKALGAtVIGTTGSeEKKKVVLaNGADYVFLAec--reFVHSVLEItggRGVDVVFDGVGKdTFAHSLEL 237 Dyadobacter fer...
Feature 1                 #####                             ####                                 
1QOR_A       229 LqRRGLMVSFGNSSGa-------VTGVNLGiln--qkgSLYVTRPSLQGYItt-rEELTEASNELFSLIAsGVIKVDVae 298 Escherichia coli
NP_966679    230 LgRFGIYVSYGQISGn-------APISFSLls----srSLFATGTSIYHYKhd-rFTLVLTTMEIFEMIRkKLLTVRIn- 296 Wolbachia endos...
YP_154093    232 LgHFGLYISYGSISGr-------MPSVSMSmls---arSWFITSPTIQHYKrs-rLELGLTAMEIFEMLRrGHIRAEIn- 299 Anaplasma margi...
YP_303262    229 LgMFGIYVSYGQISGa-------VSNVSASmls---srSLFFTAPSVFHYKrs-sFDLAMTSMELFEVIRrNHIKVSIn- 296 Ehrlichia canis...
YP_504872    230 LgFFGLYISYGQISGp-------IRNINMStlg---trSWFVAAPQLQHYKrs-rLELALTAMEVFEVVRrGHIKVDVg- 297 Anaplasma phago...
YP_506269    240 LaRFGIYVLYEQRSGe-------IPPMSWKafr---arSLFFTHPSLFHYArn-hVESVLAVAEVFHHMRiKKVVPNIal 308 Neorickettsia s...
YP_775944    234 VrPFGMVASIGQVAAi-------GARQTIDldelgparSIALARPSVLGFIardvAGYREAARATLDRLA-DGMHVEIg- 304 Burkholderia am...
YP_001416605 234 LkPFGLAVNLGQVGEp-------LGAVELArlg--pqrSLTVAVPGVFSHLrt-lPDLQAGADEMFAMVTsGAVAPTVg- 302 Xanthobacter au...
YP_001892342 233 TrPFGMVASIGQAGDvsnvqtsaVDLAALGps-----rSIALARPGVFRYMtd-lSRYRVGAQAALQRML-EGVRVPVg- 304 Ralstonia picke...
YP_003087784 238 IgKGGKIVLYGSSSGq-------PEHIDHAllr---erSIIMATPTLSAYIsd-rDALDAYAADTFEAFH-NGIFGKLai 305 Dyadobacter fer...
Feature 1                        # #          
1QOR_A       299 qqKYPLKDAQRAHEILEsRATQGSSLLIP 327 Escherichia coli
NP_966679    297 -kKYKFDEIIQAHRDMEnRKASGLNIIKI 324 Wolbachia endosymbiont of Drosophila melanogaster
YP_154093    300 -kTYKFKDIAKAHKDLEdRKLSGLGVITM 327 Anaplasma marginale str. St. Maries
YP_303262    297 -kIYKFDDIVTAHQDLEnRKLTGSNIIVL 324 Ehrlichia canis str. Jake
YP_504872    298 -rVYSFQDIEKAHRDLEnRKLSGHCIIRM 325 Anaplasma phagocytophilum HZ
YP_506269    309 -rCSGLDDIPEAHRQIEvGNVNGASVVIF 336 Neorickettsia sennetsu str. Miyayama
YP_775944    305 -aRLPLERAADAHRLLEsRQTTGGVVLLP 332 Burkholderia ambifaria AMMD
YP_001416605 303 -lSLPLADAGEAHRRLEaGTTTGSLILIP 330 Xanthobacter autotrophicus Py2
YP_001892342 305 -gIYALADAAAAHAALEgGRTSGALLLRP 332 Ralstonia pickettii 12J
YP_003087784 306 -tRYPLSMAGQAQADLEaRKTIGSVILVP 333 Dyadobacter fermentans DSM 18053

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