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Protein

NAD(P)H dehydrogenase (quinone)

Gene

wrbA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH.2 Publications

Catalytic activityi

NAD(P)H + a quinone = NAD(P)+ + a hydroquinone.UniRule annotation1 Publication

Cofactori

FMNUniRule annotation2 PublicationsNote: Binds 1 FMN per monomer.UniRule annotation2 Publications

Kineticsi

  1. KM=5.8 µM for benzoquinone1 Publication
  2. KM=14 µM for NADH1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei12 – 121NAD1 Publication
    Binding sitei51 – 511NAD; via carbonyl oxygen1 Publication
    Binding sitei98 – 981Substrate1 Publication
    Binding sitei133 – 1331FMN2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 146FMN2 Publications
    Nucleotide bindingi77 – 804FMN2 Publications
    Nucleotide bindingi112 – 1187FMN2 Publications

    GO - Molecular functioni

    • flavin adenine dinucleotide binding Source: UniProtKB-HAMAP
    • FMN binding Source: EcoCyc
    • identical protein binding Source: IntAct
    • NAD(P)H dehydrogenase (quinone) activity Source: EcoCyc
    • NAD binding Source: UniProtKB-HAMAP
    • NADP binding Source: UniProtKB-HAMAP

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN, NAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PD01343.
    ECOL316407:JW0989-MONOMER.
    MetaCyc:PD01343.
    BRENDAi1.6.5.2. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD(P)H dehydrogenase (quinone)UniRule annotation (EC:1.6.5.2UniRule annotation1 Publication)
    Alternative name(s):
    Flavoprotein WrbA
    NAD(P)H:quinone oxidoreductaseUniRule annotation
    Short name:
    NQOUniRule annotation
    Gene namesi
    Name:wrbA
    Ordered Locus Names:b1004, JW0989
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11540. wrbA.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    • membrane Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show no phenotypes, however, N-trichloromethyl-mercapto-4-cyclohexene-1,2-dicarboximide and 8-hydroxyquinoline significantly inhibit the growth of the wrbA knockout relative to the wild-type, which is consistent with a role for WrbA in protecting against environmental stressors through its quinone reductase activity.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved3 Publications
    Chaini2 – 198197NAD(P)H dehydrogenase (quinone)PRO_0000200746Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiP0A8G6.
    PaxDbiP0A8G6.
    PRIDEiP0A8G6.

    2D gel databases

    SWISS-2DPAGEP0A8G6.

    Interactioni

    Subunit structurei

    Homodimer and homotetramer; in equilibrium.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-553971,EBI-553971

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi4259550. 7 interactions.
    DIPiDIP-36231N.
    IntActiP0A8G6. 4 interactions.
    MINTiMINT-1272067.
    STRINGi511145.b1004.

    Structurei

    Secondary structure

    1
    198
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86Combined sources
    Beta strandi11 – 133Combined sources
    Helixi14 – 2714Combined sources
    Beta strandi33 – 386Combined sources
    Helixi45 – 506Combined sources
    Helixi64 – 685Combined sources
    Beta strandi70 – 778Combined sources
    Helixi85 – 917Combined sources
    Helixi95 – 1006Combined sources
    Turni101 – 1055Combined sources
    Beta strandi107 – 11711Combined sources
    Helixi120 – 13314Combined sources
    Beta strandi137 – 1393Combined sources
    Helixi142 – 1454Combined sources
    Helixi146 – 1483Combined sources
    Beta strandi149 – 1524Combined sources
    Beta strandi163 – 1653Combined sources
    Helixi176 – 19722Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R96X-ray2.60A/C1-198[»]
    2R97X-ray2.00A/C1-198[»]
    2RG1X-ray1.85A/B1-198[»]
    3B6IX-ray1.66A/B1-198[»]
    3B6JX-ray2.05A/B1-198[»]
    3B6KX-ray1.99A/B1-198[»]
    3B6MX-ray1.85A/B1-198[»]
    3ZHOX-ray1.20A/B2-198[»]
    ProteinModelPortaliP0A8G6.
    SMRiP0A8G6. Positions 2-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A8G6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 189186Flavodoxin-likeUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the WrbA family.UniRule annotationCurated
    Contains 1 flavodoxin-like domain.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105CS1. Bacteria.
    COG0655. LUCA.
    HOGENOMiHOG000030539.
    InParanoidiP0A8G6.
    KOiK03809.
    OMAiWMKGALV.
    OrthoDBiEOG6384K0.
    PhylomeDBiP0A8G6.

    Family and domain databases

    Gene3Di3.40.50.360. 1 hit.
    HAMAPiMF_01017. NQOR.
    InterProiIPR008254. Flavodoxin/NO_synth.
    IPR029039. Flavoprotein-like_dom.
    IPR010089. Flavoprotein_WrbA.
    IPR005025. FMN_Rdtase-like.
    [Graphical view]
    PfamiPF03358. FMN_red. 1 hit.
    [Graphical view]
    SUPFAMiSSF52218. SSF52218. 1 hit.
    TIGRFAMsiTIGR01755. flav_wrbA. 1 hit.
    PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A8G6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKVLVLYYS MYGHIETMAR AVAEGASKVD GAEVVVKRVP ETMPPQLFEK
    60 70 80 90 100
    AGGKTQTAPV ATPQELADYD AIIFGTPTRF GNMSGQMRTF LDQTGGLWAS
    110 120 130 140 150
    GALYGKLASV FSSTGTGGGQ EQTITSTWTT LAHHGMVIVP IGYAAQELFD
    160 170 180 190
    VSQVRGGTPY GATTIAGGDG SRQPSQEELS IARYQGEYVA GLAVKLNG
    Length:198
    Mass (Da):20,846
    Last modified:January 23, 2007 - v2
    Checksum:iBDE820C59DB7B88E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti142 – 1421G → A in AAA24759 (PubMed:8516330).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M99166 Genomic DNA. Translation: AAA24759.1.
    U00096 Genomic DNA. Translation: AAC74089.1.
    AP009048 Genomic DNA. Translation: BAA35771.1.
    PIRiB64842.
    RefSeqiNP_415524.1. NC_000913.3.
    WP_001151437.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74089; AAC74089; b1004.
    BAA35771; BAA35771; BAA35771.
    GeneIDi947263.
    KEGGiecj:JW0989.
    eco:b1004.
    PATRICi32117233. VBIEscCol129921_1040.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M99166 Genomic DNA. Translation: AAA24759.1.
    U00096 Genomic DNA. Translation: AAC74089.1.
    AP009048 Genomic DNA. Translation: BAA35771.1.
    PIRiB64842.
    RefSeqiNP_415524.1. NC_000913.3.
    WP_001151437.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R96X-ray2.60A/C1-198[»]
    2R97X-ray2.00A/C1-198[»]
    2RG1X-ray1.85A/B1-198[»]
    3B6IX-ray1.66A/B1-198[»]
    3B6JX-ray2.05A/B1-198[»]
    3B6KX-ray1.99A/B1-198[»]
    3B6MX-ray1.85A/B1-198[»]
    3ZHOX-ray1.20A/B2-198[»]
    ProteinModelPortaliP0A8G6.
    SMRiP0A8G6. Positions 2-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259550. 7 interactions.
    DIPiDIP-36231N.
    IntActiP0A8G6. 4 interactions.
    MINTiMINT-1272067.
    STRINGi511145.b1004.

    2D gel databases

    SWISS-2DPAGEP0A8G6.

    Proteomic databases

    EPDiP0A8G6.
    PaxDbiP0A8G6.
    PRIDEiP0A8G6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74089; AAC74089; b1004.
    BAA35771; BAA35771; BAA35771.
    GeneIDi947263.
    KEGGiecj:JW0989.
    eco:b1004.
    PATRICi32117233. VBIEscCol129921_1040.

    Organism-specific databases

    EchoBASEiEB1502.
    EcoGeneiEG11540. wrbA.

    Phylogenomic databases

    eggNOGiENOG4105CS1. Bacteria.
    COG0655. LUCA.
    HOGENOMiHOG000030539.
    InParanoidiP0A8G6.
    KOiK03809.
    OMAiWMKGALV.
    OrthoDBiEOG6384K0.
    PhylomeDBiP0A8G6.

    Enzyme and pathway databases

    BioCyciEcoCyc:PD01343.
    ECOL316407:JW0989-MONOMER.
    MetaCyc:PD01343.
    BRENDAi1.6.5.2. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A8G6.
    PROiP0A8G6.

    Family and domain databases

    Gene3Di3.40.50.360. 1 hit.
    HAMAPiMF_01017. NQOR.
    InterProiIPR008254. Flavodoxin/NO_synth.
    IPR029039. Flavoprotein-like_dom.
    IPR010089. Flavoprotein_WrbA.
    IPR005025. FMN_Rdtase-like.
    [Graphical view]
    PfamiPF03358. FMN_red. 1 hit.
    [Graphical view]
    SUPFAMiSSF52218. SSF52218. 1 hit.
    TIGRFAMsiTIGR01755. flav_wrbA. 1 hit.
    PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A stationary-phase protein of Escherichia coli that affects the mode of association between the trp repressor protein and operator-bearing DNA."
      Yang W., Ni L., Somerville R.L.
      Proc. Natl. Acad. Sci. U.S.A. 90:5796-5800(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-19.
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins."
      Grandori R., Khalifah P., Boice J.A., Fairman R., Giovanielli K., Carey J.
      J. Biol. Chem. 273:20960-20966(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11, FUNCTION, COFACTOR, SUBUNIT.
      Strain: K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926.
    6. "WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase."
      Patridge E.V., Ferry J.G.
      J. Bacteriol. 188:3498-3506(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-6, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    7. "Role of flavin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA."
      Natalello A., Doglia S.M., Carey J., Grandori R.
      Biochemistry 46:543-553(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: THERMOSTABILITY, DISRUPTION PHENOTYPE, SUBUNIT.
    8. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    9. "Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia coli."
      Andrade S.L., Patridge E.V., Ferry J.G., Einsle O.
      J. Bacteriol. 189:9101-9107(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) IN COMPLEX WITH FMN; NAD; AMP AND SUBSTRATE, SUBUNIT.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH FMN, REACTION MECHANISM, SUBUNIT.

    Entry informationi

    Entry nameiNQOR_ECOLI
    AccessioniPrimary (citable) accession number: P0A8G6
    Secondary accession number(s): P30849, P75890, P77543
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: March 16, 2016
    This is version 99 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    FMN promotes WrbA association into tetramers, which are more thermoresistant than dimers or monomers, suggesting that multimerization underlies the FMN effect on WrbA thermostability.1 Publication

    Caution

    Was originally (PubMed:9694845) thought to enhance the formation and/or stability of non-covalent complexes between the trp repressor protein and operator-bearing DNA. However, WrbA does not specifically influence the affinity or mode of binding of TrpR to its operator.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.