QOR1_ECOLI
ID QOR1_ECOLI Reviewed; 327 AA.
AC P28304; Q2M6Q3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Quinone oxidoreductase 1;
DE EC=1.6.5.5;
DE AltName: Full=NADPH:quinone reductase 1;
DE AltName: Full=Zeta-crystallin homolog protein;
GN Name=qorA; Synonyms=hcz, qor, qor1; OrderedLocusNames=b4051, JW4011;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Dixon N.E., Lilley P.E.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
RX PubMed=7602590; DOI=10.1006/jmbi.1995.0337;
RA Thorn J.M., Barton J.D., Dixon N.E., Ollis D.L., Edwards K.J.;
RT "Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed
RT with NADPH.";
RL J. Mol. Biol. 249:785-799(1995).
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7602590}.
CC -!- INTERACTION:
CC P28304; P0A6Y8: dnaK; NbExp=2; IntAct=EBI-556687, EBI-542092;
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; L02312; AAA23691.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43145.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77021.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78053.1; -; Genomic_DNA.
DR PIR; S45529; S45529.
DR RefSeq; NP_418475.1; NC_000913.3.
DR RefSeq; WP_000235508.1; NZ_SSZK01000016.1.
DR PDB; 1QOR; X-ray; 2.20 A; A/B=1-327.
DR PDBsum; 1QOR; -.
DR AlphaFoldDB; P28304; -.
DR SMR; P28304; -.
DR BioGRID; 4260805; 36.
DR BioGRID; 852850; 2.
DR DIP; DIP-10631N; -.
DR IntAct; P28304; 5.
DR STRING; 511145.b4051; -.
DR jPOST; P28304; -.
DR PaxDb; P28304; -.
DR PRIDE; P28304; -.
DR EnsemblBacteria; AAC77021; AAC77021; b4051.
DR EnsemblBacteria; BAE78053; BAE78053; BAE78053.
DR GeneID; 948556; -.
DR KEGG; ecj:JW4011; -.
DR KEGG; eco:b4051; -.
DR PATRIC; fig|511145.12.peg.4169; -.
DR EchoBASE; EB1455; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_3_1_6; -.
DR InParanoid; P28304; -.
DR OMA; THIATRE; -.
DR PhylomeDB; P28304; -.
DR BioCyc; EcoCyc:QOR-MON; -.
DR EvolutionaryTrace; P28304; -.
DR PRO; PR:P28304; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..327
FT /note="Quinone oxidoreductase 1"
FT /id="PRO_0000160901"
FT BINDING 42..46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:7602590"
FT BINDING 130
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:7602590"
FT BINDING 152..153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:7602590"
FT BINDING 173..177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:7602590"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:7602590"
FT BINDING 216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:7602590"
FT BINDING 238..241
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:7602590"
FT BINDING 264..266
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:7602590"
FT BINDING 317
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:7602590"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 115..133
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1QOR"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:1QOR"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 273..288
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1QOR"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:1QOR"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:1QOR"
SQ SEQUENCE 327 AA; 35172 MW; A6355B12DBA513B2 CRC64;
MATRIEFHKH GGPEVLQAVE FTPADPAENE IQVENKAIGI NFIDTYIRSG LYPPPSLPSG
LGTEAAGIVS KVGSGVKHIK AGDRVVYAQS ALGAYSSVHN IIADKAAILP AAISFEQAAA
SFLKGLTVYY LLRKTYEIKP DEQFLFHAAA GGVGLIACQW AKALGAKLIG TVGTAQKAQS
ALKAGAWQVI NYREEDLVER LKEITGGKKV RVVYDSVGRD TWERSLDCLQ RRGLMVSFGN
SSGAVTGVNL GILNQKGSLY VTRPSLQGYI TTREELTEAS NELFSLIASG VIKVDVAEQQ
KYPLKDAQRA HEILESRATQ GSSLLIP
