Q5QZL0 · GLO2_IDILO

Function

function

Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site54Zn2+ 1 (UniProtKB | ChEBI)
Binding site56Zn2+ 1 (UniProtKB | ChEBI)
Binding site58Zn2+ 2 (UniProtKB | ChEBI)
Binding site59Zn2+ 2 (UniProtKB | ChEBI)
Binding site110Zn2+ 1 (UniProtKB | ChEBI)
Binding site127Zn2+ 1 (UniProtKB | ChEBI)
Binding site127Zn2+ 2 (UniProtKB | ChEBI)
Binding site165Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionhydroxyacylglutathione hydrolase activity
Molecular Functionmetal ion binding
Biological Processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Hydroxyacylglutathione hydrolase
  • EC number
  • Alternative names
    • Glyoxalase II
      (Glx II
      )

Gene names

    • Name
      gloB
    • Ordered locus names
      IL1697

Organism names

Accessions

  • Primary accession
    Q5QZL0

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000682191-253Hydroxyacylglutathione hydrolase

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    253
  • Mass (Da)
    28,539
  • Last updated
    2005-01-04 v1
  • Checksum
    79CB0E50FF11AD52
MRVHAIEAFDDNYIWAIETNDKDKVIIVDPGEAQPVQQWLEQNSKSIETILVTHHHYDHTGGIAELIEQSPCPVIGPENPEIKTLTKTVTEGDELTVGGIQWQVLTTPGHTLDHISFYTPGFLFCGDTLFSGGCGRMFEGTPEQFTQSLLKLRKLPGETRVFCAHEYTQANVNFALKVEPENAVLQSYAEKVRMLREQEQITLPSTLQLELAINPFLRFDQKSVIAAANKHAESVKNSPEDVFYTIRQWKDNA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE017340
EMBL· GenBank· DDBJ
AAV82530.1
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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