ID QOR_PSEAE Reviewed; 325 AA. AC P43903; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 04-NOV-2026, entry version 145. DE RecName: Full=Quinone oxidoreductase; DE EC=1.6.5.5; DE AltName: Full=NADPH:quinone reductase; GN Name=qor; OrderedLocusNames=PA0023; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RA Hungerer C., Troup B., Jahn D.; RT "Cloning and regulation of the Pseudomonas aeruginosa hemF gene encoding RT oxygen-dependent coproporphyrinogen III oxidase."; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a quinone + NADPH + H(+) = 2 a 1,4-benzosemiquinone + CC NADP(+); Xref=Rhea:RHEA:14269, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225; CC EC=1.6.5.5; CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Quinone oxidoreductase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X85015; CAA59375.1; -; Genomic_DNA. DR EMBL; AE004091; AAG03413.1; -; Genomic_DNA. DR PIR; D83644; D83644. DR PIR; S52923; S52923. DR RefSeq; NP_248713.1; NC_002516.2. DR RefSeq; WP_003111202.1; NC_002516.2. DR AlphaFoldDB; P43903; -. DR SMR; P43903; -. DR FunCoup; P43903; 646. DR STRING; 208964.PA0023; -. DR PaxDb; 208964-PA0023; -. DR GeneID; 880685; -. DR KEGG; pae:PA0023; -. DR PATRIC; fig|208964.12.peg.22; -. DR PseudoCAP; PA0023; -. DR HOGENOM; CLU_026673_3_1_6; -. DR InParanoid; P43903; -. DR OMA; AAGTPYM; -. DR OrthoDB; 9805883at2; -. DR PhylomeDB; P43903; -. DR BioCyc; PAER208964:G1FZ6-23-MONOMER; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IBA:GO_Central. DR GO; GO:0003960; F:quinone reductase (NADPH) activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR CDD; cd05286; QOR2; 1. DR FunFam; 3.40.50.720:FF:000053; Quinone oxidoreductase 1; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR013154; ADH-like_N. DR InterPro; IPR020843; ER. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR047618; QOR-like. DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS. DR NCBIfam; NF008024; PRK10754.1; 1. DR PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-RELATED; 1. DR PANTHER; PTHR48106:SF13; QUINONE OXIDOREDUCTASE-RELATED; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1. PE 3: Inferred from homology; KW NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..325 FT /note="Quinone oxidoreductase" FT /id="PRO_0000160903" FT CONFLICT 10 FT /note="Y -> C (in Ref. 1; CAA59375)" FT /evidence="ECO:0000305" SQ SEQUENCE 325 AA; 35095 MW; 059A49962FA2CE2A CRC64; MAKRIQFAAY GGPEVLEYRD YQPAEPGPRE VRVRNRAIGL NFIDTYYRSG LYPAPGLPSG LGSEGAGEVE AVGSEVTRFK VGDRVAYATG PLGAYSELHV LAEEKLVHLP DGIDFEQAAA VMLKGLTTQY LLRQTYELRG GETILFHAAA GGVGLFACQW AKALGVQLIG TVSSPEKARL ARQHGAWETI DYSHENVARR VLELTDGKKC PVVYDSVGKD TWETSLDCVA PRGLLVSFGN ASGPVTGVNL GILSQKGSLY VTRPTLGSYA DTPEKLQAMA DELFGLIERG DIRIEINQRF ALAEAARAHT ELAARRTTGS TVLLP //