A0A0H3EF67 · A0A0H3EF67_ECO8N

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 site53Zn2+ 1 (UniProtKB | ChEBI)
Binding site55Zn2+ 1 (UniProtKB | ChEBI)
Binding site57Zn2+ 2 (UniProtKB | ChEBI)
Binding site58Zn2+ 2 (UniProtKB | ChEBI)
Binding site110Zn2+ 1 (UniProtKB | ChEBI)
Binding site127Zn2+ 2 (UniProtKB | ChEBI)
Binding site127Zn2+ 1 (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
      NRG857_01055

Organism names

Accessions

  • Primary accession
    A0A0H3EF67

Proteomes

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-165Metallo-beta-lactamase

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    251
  • Mass (Da)
    28,476
  • Last updated
    2015-09-16 v1
  • Checksum
    B519BF5C36928B5A
MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAISANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTPSQMYQSLKKLSALPDDTLVCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETLLQQPEERFAWLRSKKDRF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001855
EMBL· GenBank· DDBJ
ADR25642.1
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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