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A0KXS9 · GLO2_SHESA

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 site55Zn2+ 1 (UniProtKB | ChEBI)
Binding site57Zn2+ 1 (UniProtKB | ChEBI)
Binding site59Zn2+ 2 (UniProtKB | ChEBI)
Binding site60Zn2+ 2 (UniProtKB | ChEBI)
Binding site121Zn2+ 1 (UniProtKB | ChEBI)
Binding site138Zn2+ 1 (UniProtKB | ChEBI)
Binding site138Zn2+ 2 (UniProtKB | ChEBI)
Binding site176Zn2+ 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
      Shewana3_2369

Organism names

Accessions

  • Primary accession
    A0KXS9

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001448121-267Hydroxyacylglutathione 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
    267
  • Mass (Da)
    29,391
  • Last updated
    2006-12-12 v1
  • MD5 Checksum
    83A154CFBB5C423D10AAEAA30970FBD8
MLTITAINAFNDNYIWVLRQDSQQAVYVVDPGDANVVLDYLHAQRLSLAGILITHHHRDHTGGIAALTDHVKQTTGHDLAVYGPQSEDIQGINQPIEPTLSDSLTLPFIDAPVRILSVPGHTAGHIAYLVDDALFCGDTLFSAGCGRLFEGTPSQMWQSLSLLAALPDETRVYCAHEYTLSNLKFAQTVDTDNEALNAYVEEASTLRAQGKATIPSTIGLERAINPFLRPLSPTIVNSIKNQFCDQDLTKADELTCFTLLRQWKDIF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000469
EMBL· GenBank· DDBJ
ABK48598.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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