NQOR_ECOLI
ID NQOR_ECOLI Reviewed; 198 AA.
AC P0A8G6; P30849; P75890; P77543;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000255|HAMAP-Rule:MF_01017};
DE EC=1.6.5.2 {ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000269|PubMed:16672604};
DE AltName: Full=Flavoprotein WrbA;
DE AltName: Full=NAD(P)H:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01017};
DE Short=NQO {ECO:0000255|HAMAP-Rule:MF_01017};
GN Name=wrbA; OrderedLocusNames=b1004, JW0989;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-19.
RC STRAIN=K12;
RX PubMed=8516330; DOI=10.1073/pnas.90.12.5796;
RA Yang W., Ni L., Somerville R.L.;
RT "A stationary-phase protein of Escherichia coli that affects the mode of
RT association between the trp repressor protein and operator-bearing DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5796-5800(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 PROTEIN SEQUENCE OF 2-11, FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX PubMed=9694845; DOI=10.1074/jbc.273.33.20960;
RA Grandori R., Khalifah P., Boice J.A., Fairman R., Giovanielli K., Carey J.;
RT "Biochemical characterization of WrbA, founding member of a new family of
RT multimeric flavodoxin-like proteins.";
RL J. Biol. Chem. 273:20960-20966(1998).
RN [6]
RP PROTEIN SEQUENCE OF 2-6, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND COFACTOR.
RX PubMed=16672604; DOI=10.1128/jb.188.10.3498-3506.2006;
RA Patridge E.V., Ferry J.G.;
RT "WrbA from Escherichia coli and Archaeoglobus fulgidus is an
RT NAD(P)H:quinone oxidoreductase.";
RL J. Bacteriol. 188:3498-3506(2006).
RN [7]
RP THERMOSTABILITY, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=17209564; DOI=10.1021/bi061769c;
RA Natalello A., Doglia S.M., Carey J., Grandori R.;
RT "Role of flavin mononucleotide in the thermostability and oligomerization
RT of Escherichia coli stress-defense protein WrbA.";
RL Biochemistry 46:543-553(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [9] {ECO:0007744|PDB:3B6I, ECO:0007744|PDB:3B6J, ECO:0007744|PDB:3B6K, ECO:0007744|PDB:3B6M}
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) IN COMPLEX WITH FMN; NAD; AMP AND
RP SUBSTRATE, AND SUBUNIT.
RX PubMed=17951395; DOI=10.1128/jb.01336-07;
RA Andrade S.L., Patridge E.V., Ferry J.G., Einsle O.;
RT "Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia
RT coli.";
RL J. Bacteriol. 189:9101-9107(2007).
RN [10] {ECO:0007744|PDB:2R96, ECO:0007744|PDB:2R97, ECO:0007744|PDB:2RG1}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH FMN, REACTION
RP MECHANISM, AND SUBUNIT.
RX PubMed=19665595; DOI=10.1016/j.bbapap.2009.08.001;
RA Wolfova J., Smatanova I.K., Brynda J., Mesters J.R., Lapkouski M., Kuty M.,
RA Natalello A., Chatterjee N., Chern S.Y., Ebbel E., Ricci A., Grandori R.,
RA Ettrich R., Carey J.;
RT "Structural organization of WrbA in apo- and holoprotein crystals.";
RL Biochim. Biophys. Acta 1794:1288-1298(2009).
CC -!- FUNCTION: It seems to function in response to environmental stress when
CC various electron transfer chains are affected or when the environment
CC is highly oxidizing. It reduces quinones to the hydroquinone state to
CC prevent interaction of the semiquinone with O2 and production of
CC superoxide. It prefers NADH over NADPH. {ECO:0000269|PubMed:16672604,
CC ECO:0000269|PubMed:9694845}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01017,
CC ECO:0000269|PubMed:16672604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01017,
CC ECO:0000269|PubMed:16672604};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01017,
CC ECO:0000269|PubMed:16672604, ECO:0000269|PubMed:9694845};
CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_01017,
CC ECO:0000269|PubMed:16672604, ECO:0000269|PubMed:9694845};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.8 uM for benzoquinone {ECO:0000269|PubMed:16672604};
CC KM=14 uM for NADH {ECO:0000269|PubMed:16672604};
CC -!- SUBUNIT: Homodimer and homotetramer; in equilibrium.
CC {ECO:0000269|PubMed:17209564, ECO:0000269|PubMed:17951395,
CC ECO:0000269|PubMed:19665595, ECO:0000269|PubMed:9694845}.
CC -!- INTERACTION:
CC P0A8G6; P0A8G6: wrbA; NbExp=2; IntAct=EBI-553971, EBI-553971;
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show no phenotypes,
CC however, N-trichloromethyl-mercapto-4-cyclohexene-1,2-dicarboximide and
CC 8-hydroxyquinoline significantly inhibit the growth of the wrbA
CC knockout relative to the wild-type, which is consistent with a role for
CC WrbA in protecting against environmental stressors through its quinone
CC reductase activity. {ECO:0000269|PubMed:17209564}.
CC -!- MISCELLANEOUS: FMN promotes WrbA association into tetramers, which are
CC more thermoresistant than dimers or monomers, suggesting that
CC multimerization underlies the FMN effect on WrbA thermostability.
CC {ECO:0000305|PubMed:9694845}.
CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000255|HAMAP-
CC Rule:MF_01017, ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:9694845) thought to enhance the
CC formation and/or stability of non-covalent complexes between the trp
CC repressor protein and operator-bearing DNA. However, WrbA does not
CC specifically influence the affinity or mode of binding of TrpR to its
CC operator. {ECO:0000305|PubMed:9694845}.
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DR EMBL; M99166; AAA24759.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74089.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35771.1; -; Genomic_DNA.
DR PIR; B64842; B64842.
DR RefSeq; NP_415524.1; NC_000913.3.
DR RefSeq; WP_001151437.1; NZ_STEB01000006.1.
DR PDB; 2R96; X-ray; 2.60 A; A/C=1-198.
DR PDB; 2R97; X-ray; 2.00 A; A/C=1-198.
DR PDB; 2RG1; X-ray; 1.85 A; A/B=1-198.
DR PDB; 3B6I; X-ray; 1.66 A; A/B=1-198.
DR PDB; 3B6J; X-ray; 2.05 A; A/B=1-198.
DR PDB; 3B6K; X-ray; 1.99 A; A/B=1-198.
DR PDB; 3B6M; X-ray; 1.85 A; A/B=1-198.
DR PDB; 3ZHO; X-ray; 1.20 A; A/B=2-198.
DR PDB; 4YQE; X-ray; 1.33 A; A/B=2-198.
DR PDB; 5F12; X-ray; 1.50 A; A/B=2-198.
DR PDBsum; 2R96; -.
DR PDBsum; 2R97; -.
DR PDBsum; 2RG1; -.
DR PDBsum; 3B6I; -.
DR PDBsum; 3B6J; -.
DR PDBsum; 3B6K; -.
DR PDBsum; 3B6M; -.
DR PDBsum; 3ZHO; -.
DR PDBsum; 4YQE; -.
DR PDBsum; 5F12; -.
DR AlphaFoldDB; P0A8G6; -.
DR SMR; P0A8G6; -.
DR BioGRID; 4259550; 24.
DR DIP; DIP-36231N; -.
DR IntAct; P0A8G6; 4.
DR MINT; P0A8G6; -.
DR STRING; 511145.b1004; -.
DR iPTMnet; P0A8G6; -.
DR SWISS-2DPAGE; P0A8G6; -.
DR jPOST; P0A8G6; -.
DR PaxDb; P0A8G6; -.
DR PRIDE; P0A8G6; -.
DR EnsemblBacteria; AAC74089; AAC74089; b1004.
DR EnsemblBacteria; BAA35771; BAA35771; BAA35771.
DR GeneID; 66670718; -.
DR GeneID; 947263; -.
DR KEGG; ecj:JW0989; -.
DR KEGG; eco:b1004; -.
DR PATRIC; fig|1411691.4.peg.1267; -.
DR EchoBASE; EB1502; -.
DR eggNOG; COG0655; Bacteria.
DR HOGENOM; CLU_051402_0_2_6; -.
DR InParanoid; P0A8G6; -.
DR OMA; KFADGNP; -.
DR PhylomeDB; P0A8G6; -.
DR BioCyc; EcoCyc:PD01343; -.
DR BioCyc; MetaCyc:PD01343; -.
DR BRENDA; 1.6.5.2; 2026.
DR SABIO-RK; P0A8G6; -.
DR EvolutionaryTrace; P0A8G6; -.
DR PRO; PR:P0A8G6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:EcoCyc.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0006979; P:response to oxidative stress; IEP:EcoCyc.
DR Gene3D; 3.40.50.360; -; 1.
DR HAMAP; MF_01017; NQOR; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR010089; Flavoprotein_WrbA-like.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR InterPro; IPR037513; NQO.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR01755; flav_wrbA; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Flavoprotein; FMN;
KW NAD; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16672604,
FT ECO:0000269|PubMed:8516330, ECO:0000269|PubMed:9694845"
FT CHAIN 2..198
FT /note="NAD(P)H dehydrogenase (quinone)"
FT /id="PRO_0000200746"
FT DOMAIN 4..189
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT BINDING 10..15
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017,
FT ECO:0000269|PubMed:17951395, ECO:0000269|PubMed:19665595"
FT BINDING 12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17951395"
FT BINDING 51
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17951395"
FT BINDING 78..80
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017,
FT ECO:0000269|PubMed:17951395, ECO:0000269|PubMed:19665595"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017,
FT ECO:0000305|PubMed:17951395"
FT BINDING 113..118
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017,
FT ECO:0000269|PubMed:17951395, ECO:0000269|PubMed:19665595"
FT BINDING 133
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017,
FT ECO:0000269|PubMed:17951395, ECO:0000269|PubMed:19665595"
FT BINDING 169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17951395"
FT MOD_RES 50
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT CONFLICT 142
FT /note="G -> A (in Ref. 1; AAA24759)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3ZHO"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3ZHO"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:3ZHO"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:3ZHO"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:3ZHO"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:3ZHO"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:3ZHO"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:3ZHO"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:3ZHO"
FT TURN 101..105
FT /evidence="ECO:0007829|PDB:3ZHO"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:3ZHO"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:3ZHO"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2R97"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:3B6M"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:3ZHO"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3ZHO"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5F12"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:4YQE"
FT HELIX 176..197
FT /evidence="ECO:0007829|PDB:3ZHO"
SQ SEQUENCE 198 AA; 20846 MW; BDE820C59DB7B88E CRC64;
MAKVLVLYYS MYGHIETMAR AVAEGASKVD GAEVVVKRVP ETMPPQLFEK AGGKTQTAPV
ATPQELADYD AIIFGTPTRF GNMSGQMRTF LDQTGGLWAS GALYGKLASV FSSTGTGGGQ
EQTITSTWTT LAHHGMVIVP IGYAAQELFD VSQVRGGTPY GATTIAGGDG SRQPSQEELS
IARYQGEYVA GLAVKLNG
