A0A3Q0L6Y4 · A0A3Q0L6Y4_VIBVU

Function

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Ni2+ (UniProtKB | Rhea| CHEBI:49786 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.

Pathway

Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site59Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site77Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Active site125Proton donor/acceptor
Binding site125Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners

GO annotations

AspectTerm
Molecular Functionlactoylglutathione lyase activity
Molecular Functionmetal ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    lactoylglutathione lyase
  • EC number
  • Alternative names
    • Aldoketomutase
    • Glyoxalase I
    • Ketone-aldehyde mutase
    • Methylglyoxalase
    • S-D-lactoylglutathione methylglyoxal lyase

Gene names

    • Name
      gloA
    • Ordered locus names
      VV1_3100

Organism names

Accessions

  • Primary accession
    A0A3Q0L6Y4

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-129VOC

Sequence similarities

Belongs to the glyoxalase I family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    138
  • Mass (Da)
    15,087
  • Last updated
    2019-02-13 v1
  • Checksum
    B399C1159AC3311B
MSNGRILHTMLRVGNLDKSIQFYTEVMGMQLLRTNENKEYEYTLAFLGYGDESQGAVIELTYNWGKTEYDLGSAFGHIAIGVDDIYVTCDAIKAAGGNVTREPGPVKGGTTHIAFVKDPDGYMIELIQNKQASAGLEG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE016795
EMBL· GenBank· DDBJ
AAO11423.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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