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Protein

Quinone oxidoreductase 2

Gene

qorB

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

Functioni

Quinone oxidoreductase that may play some additional role beyond quinone reduction. Potential redox sensor protein. Overexpression induces retardation of growth.1 Publication

Catalytic activityi

NAD(P)H + a quinone = NAD(P)+ + a hydroquinone.1 Publication

Kineticsi

  1. KM=65.6 µM for methyl-1,4-benzoquinone (MBQ)1 Publication
  2. KM=18 µM for NADPH1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei33NADP1 Publication1
    Binding sitei171NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi6 – 11NADP1 Publication6
    Nucleotide bindingi73 – 75NADP1 Publication3
    Nucleotide bindingi138 – 143NADP1 Publication6

    GO - Molecular functioni

    Keywordsi

    Molecular functionOxidoreductase
    LigandNADP

    Enzyme and pathway databases

    BioCyciEcoCyc:G7868-MONOMER
    MetaCyc:G7868-MONOMER
    BRENDAi1.6.5.2 2026

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Quinone oxidoreductase 2 (EC:1.6.5.2)
    Gene namesi
    Name:qorB
    Synonyms:qor2, ytfG
    Ordered Locus Names:b4211, JW4169
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12507 qorB

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi139W → A or I: 3-fold increase in the Km for methyl-1,4-benzoquinone. 1 Publication1
    Mutagenesisi139W → F: Almost no change in the Km for methyl-1,4-benzoquinone. 1 Publication1
    Mutagenesisi140Y → A or I: Almost complete loss of catalytic activity. 1 Publication1
    Mutagenesisi140Y → F: No change. 1 Publication1
    Mutagenesisi143N → A or L: 6-fold increase in the Km for methyl-1,4-benzoquinone. No change in affinity for NADPH. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001698251 – 286Quinone oxidoreductase 2Add BLAST286

    Proteomic databases

    PaxDbiP39315
    PRIDEiP39315

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4263443, 14 interactors
    DIPiDIP-12935N
    IntActiP39315, 3 interactors
    STRINGi316385.ECDH10B_4406

    Structurei

    Secondary structure

    1286
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 6Combined sources5
    Helixi10 – 19Combined sources10
    Turni20 – 22Combined sources3
    Helixi25 – 27Combined sources3
    Beta strandi28 – 33Combined sources6
    Turni35 – 37Combined sources3
    Helixi39 – 43Combined sources5
    Beta strandi47 – 50Combined sources4
    Helixi56 – 62Combined sources7
    Turni63 – 65Combined sources3
    Beta strandi67 – 71Combined sources5
    Helixi83 – 94Combined sources12
    Beta strandi98 – 104Combined sources7
    Turni105 – 109Combined sources5
    Helixi115 – 128Combined sources14
    Beta strandi130 – 137Combined sources8
    Helixi141 – 145Combined sources5
    Helixi148 – 154Combined sources7
    Beta strandi156 – 160Combined sources5
    Helixi171 – 183Combined sources13
    Beta strandi184 – 186Combined sources3
    Beta strandi191 – 194Combined sources4
    Helixi202 – 213Combined sources12
    Beta strandi218 – 221Combined sources4
    Helixi224 – 231Combined sources8
    Helixi238 – 252Combined sources15
    Turni253 – 256Combined sources4
    Helixi262 – 267Combined sources6
    Helixi274 – 279Combined sources6
    Helixi280 – 282Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2ZCUX-ray1.80A1-286[»]
    2ZCVX-ray2.30A1-286[»]
    ProteinModelPortaliP39315
    SMRiP39315
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39315

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NmrA-type oxidoreductase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105ECR Bacteria
    COG0702 LUCA
    HOGENOMiHOG000035268
    InParanoidiP39315
    KOiK19267
    OMAiGQAGKVY
    PhylomeDBiP39315

    Family and domain databases

    InterProiView protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf
    IPR008030 NmrA-like
    PfamiView protein in Pfam
    PF05368 NmrA, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P39315-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIAITGATGQ LGHYVIESLM KTVPASQIVA IVRNPAKAQA LAAQGITVRQ
    60 70 80 90 100
    ADYGDEAALT SALQGVEKLL LISSSEVGQR APQHRNVINA AKAAGVKFIA
    110 120 130 140 150
    YTSLLHADTS PLGLADEHIE TEKMLADSGI VYTLLRNGWY SENYLASAPA
    160 170 180 190 200
    ALEHGVFIGA AGDGKIASAT RADYAAAAAR VISEAGHEGK VYELAGDSAW
    210 220 230 240 250
    TLTQLAAELT KQSGKQVTYQ NLSEADFAAA LKSVGLPDGL ADMLADSDVG
    260 270 280
    ASKGGLFDDS KTLSKLIGHP TTTLAESVSH LFNVNN
    Length:286
    Mass (Da):29,734
    Last modified:February 1, 1995 - v1
    Checksum:i643C7A74CEE13CEA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U14003 Genomic DNA Translation: AAA97107.1
    U00096 Genomic DNA Translation: AAC77168.1
    AP009048 Genomic DNA Translation: BAE78212.1
    PIRiS56436
    RefSeqiNP_418632.1, NC_000913.3
    WP_000560561.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC77168; AAC77168; b4211
    BAE78212; BAE78212; BAE78212
    GeneIDi948731
    KEGGiecj:JW4169
    eco:b4211
    PATRICifig|1411691.4.peg.2490

    Similar proteinsi

    Entry informationi

    Entry nameiQOR2_ECOLI
    AccessioniPrimary (citable) accession number: P39315
    Secondary accession number(s): Q2M694
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: March 28, 2018
    This is version 132 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health