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P37339

- LHGO_ECOLI

UniProt

P37339 - LHGO_ECOLI

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Protein
L-2-hydroxyglutarate oxidase LhgO
Gene
lhgO, ygaF, b2660, JW2635
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Oxidizes L-2-hydroxyglutarate, probably to recover alpha-ketoglutarate mistakenly reduced by other enzymes or formed during growth on propionate.1 Publication

Catalytic activityi

(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.1 Publication

Cofactori

FAD.1 Publication

Kineticsi

  1. KM=95 µM for L-2-hydroxyglutarate1 Publication

Vmax=113 nmol/min/mg enzyme

GO - Molecular functioni

  1. L-2-hydroxyglutarate oxidase activity Source: EcoCyc
  2. flavin adenine dinucleotide binding Source: EcoCyc
  3. long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB-EC
  4. medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
  5. very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12387-MONOMER.
    ECOL316407:JW2635-MONOMER.
    MetaCyc:EG12387-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-2-hydroxyglutarate oxidase LhgO (EC:1.1.3.15)
    Gene namesi
    Name:lhgO
    Synonyms:ygaF
    Ordered Locus Names:b2660, JW2635
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12387. lhgO.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 422422L-2-hydroxyglutarate oxidase LhgOUniRule annotation
    PRO_0000169295Add
    BLAST

    Proteomic databases

    PaxDbiP37339.

    Expressioni

    Inductioni

    Expression is induced by RpoS during carbon starvation and at stationary phase. Is also regulated by cAMP-CRP. Repressed by CsiR.1 Publication

    Gene expression databases

    GenevestigatoriP37339.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    groLP0A6F51EBI-555990,EBI-543750

    Protein-protein interaction databases

    DIPiDIP-12096N.
    IntActiP37339. 4 interactions.
    MINTiMINT-1301841.
    STRINGi511145.b2660.

    Structurei

    3D structure databases

    ProteinModelPortaliP37339.
    SMRiP37339. Positions 2-269.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the L2HGDH family.

    Phylogenomic databases

    eggNOGiCOG0579.
    HOGENOMiHOG000245180.
    KOiK15736.
    OMAiNVCNAPS.
    OrthoDBiEOG6X9MHV.
    PhylomeDBiP37339.

    Family and domain databases

    HAMAPiMF_00990. L_hydroxyglutarate_oxidase.
    InterProiIPR006076. FAD-dep_OxRdtase.
    [Graphical view]
    PfamiPF01266. DAO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P37339-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYDFVIIGGG IIGMSTAMQL IDVYPDARIA LLEKESAPAC HQTGHNSGVI    50
    HAGVYYTPGS LKAQFCLAGN RATKAFCDQN GIRYDNCGKM LVATSDLEME 100
    RMRALWERTA ANGIEREWLN ADELREREPN ITGLGGIFVP SSGIVSYRDV 150
    TAAMAKIFQS RGGEIIYNAE VSGLNEHKNG VVIRTRQGGE YEASTLISCS 200
    GLMADRLVKM LGLEPGFIIC PFRGEYFRLA PEHNQIVNHL IYPIPDPAMP 250
    FLGVHLTRMI DGSVTVGPNA VLAFKREGYR KRDFSFSDTL EILGSSGIRR 300
    VLQNHLRSGL GEMKNSLCKS GYLRLVQKYC PRLSLSDLQP WPAGVRAQAV 350
    SPDGKLIDDF LFVTTPRTIH TCNAPSPAAT SAIPIGAHIV SKVQTLLASQ 400
    SNPGRTLRAA RSVDALHAAF NQ 422
    Length:422
    Mass (Da):46,082
    Last modified:December 4, 2007 - v3
    Checksum:i8E13E890B0A7365C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75707.2.
    AP009048 Genomic DNA. Translation: BAA16521.1.
    M88334 Genomic DNA. No translation available.
    PIRiE65045.
    RefSeqiNP_417146.2. NC_000913.3.
    YP_490875.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75707; AAC75707; b2660.
    BAA16521; BAA16521; BAA16521.
    GeneIDi12934112.
    948069.
    KEGGiecj:Y75_p2603.
    eco:b2660.
    PATRICi32120710. VBIEscCol129921_2752.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75707.2 .
    AP009048 Genomic DNA. Translation: BAA16521.1 .
    M88334 Genomic DNA. No translation available.
    PIRi E65045.
    RefSeqi NP_417146.2. NC_000913.3.
    YP_490875.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P37339.
    SMRi P37339. Positions 2-269.
    ModBasei Search...

    Protein-protein interaction databases

    DIPi DIP-12096N.
    IntActi P37339. 4 interactions.
    MINTi MINT-1301841.
    STRINGi 511145.b2660.

    Proteomic databases

    PaxDbi P37339.

    Protocols and materials databases

    DNASUi 948069.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75707 ; AAC75707 ; b2660 .
    BAA16521 ; BAA16521 ; BAA16521 .
    GeneIDi 12934112.
    948069.
    KEGGi ecj:Y75_p2603.
    eco:b2660.
    PATRICi 32120710. VBIEscCol129921_2752.

    Organism-specific databases

    EchoBASEi EB2288.
    EcoGenei EG12387. lhgO.

    Phylogenomic databases

    eggNOGi COG0579.
    HOGENOMi HOG000245180.
    KOi K15736.
    OMAi NVCNAPS.
    OrthoDBi EOG6X9MHV.
    PhylomeDBi P37339.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG12387-MONOMER.
    ECOL316407:JW2635-MONOMER.
    MetaCyc:EG12387-MONOMER.

    Miscellaneous databases

    PROi P37339.

    Gene expression databases

    Genevestigatori P37339.

    Family and domain databases

    HAMAPi MF_00990. L_hydroxyglutarate_oxidase.
    InterProi IPR006076. FAD-dep_OxRdtase.
    [Graphical view ]
    Pfami PF01266. DAO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "Molecular organization of the Escherichia coli gab cluster: nucleotide sequence of the structural genes gabD and gabP and expression of the GABA permease gene."
      Niegemann E., Schulz A., Bartsch K.
      Arch. Microbiol. 160:454-460(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 219-422.
      Strain: K12 / JM103 / ATCC 39403 / DSM 2829 / NCIMB 12044.
    5. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
      Borodovsky M., Rudd K.E., Koonin E.V.
      Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    6. "Multiple stress signal integration in the regulation of the complex sigma S-dependent csiD-ygaF-gabDTP operon in Escherichia coli."
      Metzner M., Germer J., Hengge R.
      Mol. Microbiol. 51:799-811(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    7. "Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase."
      Kalliri E., Mulrooney S.B., Hausinger R.P.
      J. Bacteriol. 190:3793-3798(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiLHGO_ECOLI
    AccessioniPrimary (citable) accession number: P37339
    Secondary accession number(s): P76622, P77020
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: December 4, 2007
    Last modified: June 11, 2014
    This is version 110 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3

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