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Protein

Quinone oxidoreductase 2

Gene

qorB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:G7868-MONOMER.
    ECOL316407:JW4169-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
    Complete GO annotation...

    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. 13 interactors.
    DIPiDIP-12935N.
    IntActiP39315. 3 interactors.
    MINTiMINT-1227197.
    STRINGi511145.b4211.

    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.
    OMAiCADEGRI.
    PhylomeDBiP39315.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR008030. NmrA-like.
    [Graphical view]
    PfamiPF05368. NmrA. 1 hit.
    [Graphical view]
    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.
    PATRICi32123997. VBIEscCol129921_4343.

    Cross-referencesi

    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.

    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...

    Protein-protein interaction databases

    BioGridi4263443. 13 interactors.
    DIPiDIP-12935N.
    IntActiP39315. 3 interactors.
    MINTiMINT-1227197.
    STRINGi511145.b4211.

    Proteomic databases

    PaxDbiP39315.
    PRIDEiP39315.

    Protocols and materials databases

    DNASUi948731.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC77168; AAC77168; b4211.
    BAE78212; BAE78212; BAE78212.
    GeneIDi948731.
    KEGGiecj:JW4169.
    eco:b4211.
    PATRICi32123997. VBIEscCol129921_4343.

    Organism-specific databases

    EchoBASEiEB2400.
    EcoGeneiEG12507. qorB.

    Phylogenomic databases

    eggNOGiENOG4105ECR. Bacteria.
    COG0702. LUCA.
    HOGENOMiHOG000035268.
    InParanoidiP39315.
    KOiK19267.
    OMAiCADEGRI.
    PhylomeDBiP39315.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7868-MONOMER.
    ECOL316407:JW4169-MONOMER.
    MetaCyc:G7868-MONOMER.
    BRENDAi1.6.5.2. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP39315.
    PROiP39315.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR008030. NmrA-like.
    [Graphical view]
    PfamiPF05368. NmrA. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiQOR2_ECOLI
    AccessioniPrimary (citable) accession number: P39315
    Secondary accession number(s): Q2M694
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: November 2, 2016
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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.