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Protein

L-2-hydroxyglutarate oxidase LhgO

Gene

lhgO

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.UniRule annotation1 Publication

Catalytic activityi

(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.UniRule annotation1 Publication

Cofactori

FADUniRule annotation1 Publication

Kineticsi

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

Vmax=113 nmol/min/mg enzyme1 Publication

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: EcoCyc
  2. L-2-hydroxyglutarate oxidase activity 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...

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 LhgOUniRule annotation (EC:1.1.3.15UniRule annotation)
Gene namesi
Name:lhgOUniRule annotation
Synonyms:ygaF
Ordered Locus Names:b2660, JW2635
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: 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 LhgOPRO_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 3-269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L2HGDH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0579.
HOGENOMiHOG000245180.
InParanoidiP37339.
KOiK15736.
OMAiHFTRMID.
OrthoDBiEOG6X9MHV.
PhylomeDBiP37339.

Family and domain databases

HAMAPiMF_00990. L_hydroxyglutarate_oxidase.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR030862. L_hydroxyglutarate_Oxase.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37339-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYDFVIIGGG IIGMSTAMQL IDVYPDARIA LLEKESAPAC HQTGHNSGVI
60 70 80 90 100
HAGVYYTPGS LKAQFCLAGN RATKAFCDQN GIRYDNCGKM LVATSDLEME
110 120 130 140 150
RMRALWERTA ANGIEREWLN ADELREREPN ITGLGGIFVP SSGIVSYRDV
160 170 180 190 200
TAAMAKIFQS RGGEIIYNAE VSGLNEHKNG VVIRTRQGGE YEASTLISCS
210 220 230 240 250
GLMADRLVKM LGLEPGFIIC PFRGEYFRLA PEHNQIVNHL IYPIPDPAMP
260 270 280 290 300
FLGVHLTRMI DGSVTVGPNA VLAFKREGYR KRDFSFSDTL EILGSSGIRR
310 320 330 340 350
VLQNHLRSGL GEMKNSLCKS GYLRLVQKYC PRLSLSDLQP WPAGVRAQAV
360 370 380 390 400
SPDGKLIDDF LFVTTPRTIH TCNAPSPAAT SAIPIGAHIV SKVQTLLASQ
410 420
SNPGRTLRAA RSVDALHAAF NQ
Length:422
Mass (Da):46,082
Last modified:December 4, 2007 - v3
Checksum:i8E13E890B0A7365C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP37339.
SMRiP37339. Positions 3-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP37339.

Protocols and materials databases

DNASUi948069.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB2288.
EcoGeneiEG12387. lhgO.

Phylogenomic databases

eggNOGiCOG0579.
HOGENOMiHOG000245180.
InParanoidiP37339.
KOiK15736.
OMAiHFTRMID.
OrthoDBiEOG6X9MHV.
PhylomeDBiP37339.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP37339.

Gene expression databases

GenevestigatoriP37339.

Family and domain databases

HAMAPiMF_00990. L_hydroxyglutarate_oxidase.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR030862. L_hydroxyglutarate_Oxase.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: April 29, 2015
This is version 115 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

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 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.