ID QOR_SALTY Reviewed; 327 AA. AC P40783; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 13-DEC-2001, sequence version 2. DT 25-NOV-2008, entry version 54. DE RecName: Full=Quinone oxidoreductase; DE EC=1.6.5.5; DE AltName: Full=NADPH:quinone reductase; DE AltName: Full=Zeta-crystallin homolog protein; GN Name=qor; OrderedLocusNames=STM4245; OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=602; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., RA Waterston R., Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium RT LT2."; RL Nature 413:852-856(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168. RX MEDLINE=88227847; PubMed=2836367; RA Wong A., Kean L., Maurer R.; RT "Sequence of the dnaB gene of Salmonella typhimurium."; RL J. Bacteriol. 170:2668-2675(1988). CC -!- CATALYTIC ACTIVITY: NADPH + 2 quinone = NADP(+) + 2 semiquinone. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008898; AAL23069.1; -; Genomic_DNA. DR EMBL; J03390; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_463110.1; -. DR HSSP; P28304; 1QOR. DR SMR; P40783; 2-327. DR GeneID; 1255771; -. DR GenomeReviews; AE006468_GR; STM4245. DR KEGG; stm:STM4245; -. DR NMPDR; fig|99287.1.peg.4083; -. DR StyGene; SG10511; qor. DR HOGENOM; P40783; -. DR BioCyc; STYP99287:STM4245-MON; -. DR GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:InterPro. DR InterPro; IPR013154; AlcDHase_GroES-like. DR InterPro; IPR002085; AlcDHase_SF_Zn. DR InterPro; IPR013149; AlcDHase_Zn-bd. DR InterPro; IPR016040; NAD(P)-bd. DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; Oxidoreductase. FT CHAIN 1 327 Quinone oxidoreductase. FT /FTId=PRO_0000160902. FT CONFLICT 92 92 L -> V (in Ref. 2; J03390). FT CONFLICT 148 148 A -> R (in Ref. 2; J03390). SQ SEQUENCE 327 AA; 35151 MW; 602F4CB6E6A805F1 CRC64; MATRIEFHKH GGPEVLQTVE FTPAEPAEHE IQVENKAIGI NFIDTYIRSG LYPPPSLPAG LGTEAAGVVS KVGNGVEHIR VGDRVVYAQS TLGAYSSVHN VTADKAAILP DAISFEQAAA SFLKGLTVFY LLRKTYEVKP DEPFLFHAAA GGVGLIACQW AKALGAKLIG TVGSAQKAQR ALDAGAWQVI NYREESIVER VKEITGGKKV RVVYDSVGKD TWEASLDCLQ RRGLMVSFGN ASGPVTGVNL GILNQKGSLY ATRPSLQGYI TTREELTEAS NELFSLIASG VIKVDVAENQ RYALKDARRA HEVLESRATQ GSSLLIP //