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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)DescriptionActionsGraphical viewLength
    Binding sitei12NAD1 Publication1
    Binding sitei51NAD; via carbonyl oxygen1 Publication1
    Binding sitei98Substrate1 Publication1
    Binding sitei133FMN2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi9 – 14FMN2 Publications6
    Nucleotide bindingi77 – 80FMN2 Publications4
    Nucleotide bindingi112 – 118FMN2 Publications7

    GO - Molecular functioni

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

    GO - Biological processi

    • response to oxidative stress Source: EcoCyc
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11540. wrbA.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    • membrane Source: UniProtKB
    • plasma membrane Source: GO_Central
    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)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved3 Publications
    ChainiPRO_00002007462 – 198NAD(P)H dehydrogenase (quinone)Add BLAST197

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei50N6-acetyllysine1 Publication1

    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

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1198
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 8Combined sources6
    Beta strandi11 – 13Combined sources3
    Helixi14 – 27Combined sources14
    Beta strandi33 – 38Combined sources6
    Helixi45 – 50Combined sources6
    Helixi64 – 68Combined sources5
    Beta strandi70 – 77Combined sources8
    Helixi85 – 91Combined sources7
    Helixi95 – 100Combined sources6
    Turni101 – 105Combined sources5
    Beta strandi107 – 117Combined sources11
    Helixi120 – 133Combined sources14
    Beta strandi137 – 139Combined sources3
    Helixi142 – 145Combined sources4
    Helixi146 – 148Combined sources3
    Beta strandi149 – 152Combined sources4
    Beta strandi159 – 161Combined sources3
    Beta strandi163 – 165Combined sources3
    Helixi176 – 197Combined sources22

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    4YQEX-ray1.33A/B2-198[»]
    5F12X-ray1.50A/B2-198[»]
    ProteinModelPortaliP0A8G6.
    SMRiP0A8G6.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A8G6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini4 – 189Flavodoxin-likeUniRule annotationAdd BLAST186

    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.
    PhylomeDBiP0A8G6.

    Family and domain databases

    Gene3Di3.40.50.360. 1 hit.
    HAMAPiMF_01017. NQOR. 1 hit.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti142G → A in AAA24759 (PubMed:8516330).Curated1

    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
    PDB 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[»]
    4YQEX-ray1.33A/B2-198[»]
    5F12X-ray1.50A/B2-198[»]
    ProteinModelPortaliP0A8G6.
    SMRiP0A8G6.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259550. 7 interactors.
    DIPiDIP-36231N.
    IntActiP0A8G6. 4 interactors.
    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.
    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. 1 hit.
    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...

    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: November 2, 2016
    This is version 103 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.