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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331NADP1 Publication
    Binding sitei171 – 1711NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi6 – 116NADP1 Publication
    Nucleotide bindingi73 – 753NADP1 Publication
    Nucleotide bindingi138 – 1436NADP1 Publication

    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.
    RETL1328306-WGS:GSTH-2808-MONOMER.
    RETL1328306-WGS:GSTH-4414-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi139 – 1391W → A or I: 3-fold increase in the Km for methyl-1,4-benzoquinone. 1 Publication
    Mutagenesisi139 – 1391W → F: Almost no change in the Km for methyl-1,4-benzoquinone. 1 Publication
    Mutagenesisi140 – 1401Y → A or I: Almost complete loss of catalytic activity. 1 Publication
    Mutagenesisi140 – 1401Y → F: No change. 1 Publication
    Mutagenesisi143 – 1431N → A or L: 6-fold increase in the Km for methyl-1,4-benzoquinone. No change in affinity for NADPH. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 286286Quinone oxidoreductase 2PRO_0000169825Add
    BLAST

    Proteomic databases

    PaxDbiP39315.
    PRIDEiP39315.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    286
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Helixi10 – 1910Combined sources
    Turni20 – 223Combined sources
    Helixi25 – 273Combined sources
    Beta strandi28 – 336Combined sources
    Turni35 – 373Combined sources
    Helixi39 – 435Combined sources
    Beta strandi47 – 504Combined sources
    Helixi56 – 627Combined sources
    Turni63 – 653Combined sources
    Beta strandi67 – 715Combined sources
    Helixi83 – 9412Combined sources
    Beta strandi98 – 1047Combined sources
    Turni105 – 1095Combined sources
    Helixi115 – 12814Combined sources
    Beta strandi130 – 1378Combined sources
    Helixi141 – 1455Combined sources
    Helixi148 – 1547Combined sources
    Beta strandi156 – 1605Combined sources
    Helixi171 – 18313Combined sources
    Beta strandi184 – 1863Combined sources
    Beta strandi191 – 1944Combined sources
    Helixi202 – 21312Combined sources
    Beta strandi218 – 2214Combined sources
    Helixi224 – 2318Combined sources
    Helixi238 – 25215Combined sources
    Turni253 – 2564Combined sources
    Helixi262 – 2676Combined sources
    Helixi274 – 2796Combined sources
    Helixi280 – 2823Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZCUX-ray1.80A1-286[»]
    2ZCVX-ray2.30A1-286[»]
    ProteinModelPortaliP39315.
    SMRiP39315. Positions 1-283.
    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.
    OrthoDBiEOG6BS8V7.
    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZCUX-ray1.80A1-286[»]
    2ZCVX-ray2.30A1-286[»]
    ProteinModelPortaliP39315.
    SMRiP39315. Positions 1-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263443. 13 interactions.
    DIPiDIP-12935N.
    IntActiP39315. 3 interactions.
    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.
    OrthoDBiEOG6BS8V7.
    PhylomeDBiP39315.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7868-MONOMER.
    ECOL316407:JW4169-MONOMER.
    MetaCyc:G7868-MONOMER.
    RETL1328306-WGS:GSTH-2808-MONOMER.
    RETL1328306-WGS:GSTH-4414-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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Crystal structure of a new type of NADPH-dependent quinone oxidoreductase (QOR2) from Escherichia coli."
      Kim I.K., Yim H.S., Kim M.K., Kim D.W., Kim Y.M., Cha S.S., Kang S.O.
      J. Mol. Biol. 379:372-384(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF TRP-139; TYR-140 AND ASN-143, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION.

    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: January 20, 2016
    This is version 121 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.