QOR_PSEAE
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 03-AUG-2022, entry version 131.
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; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC 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 / 1C /
RC 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 / 1C /
RC 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 + H(+) + NADPH = 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}.
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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; NZ_QZGE01000012.1.
DR AlphaFoldDB; P43903; -.
DR SMR; P43903; -.
DR STRING; 287.DR97_2976; -.
DR PaxDb; P43903; -.
DR PRIDE; P43903; -.
DR EnsemblBacteria; AAG03413; AAG03413; 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; THIATRE; -.
DR PhylomeDB; P43903; -.
DR BioCyc; PAER208964:G1FZ6-23-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IBA:GO_Central.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 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