A0A2K2HA89 · A0A2K2HA89_9BACT

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Sulfur metabolism; glutathione metabolism.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site187L-glutamate (UniProtKB | ChEBI)
Active site462Nucleophile
Binding site480-482L-glutamate (UniProtKB | ChEBI)
Binding site504L-glutamate (UniProtKB | ChEBI)
Binding site533-534L-glutamate (UniProtKB | ChEBI)
Binding site555L-glutamate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionglutathione hydrolase activity
Molecular Functionleukotriene C4 gamma-glutamyl transferase activity
Biological Processglutathione biosynthetic process
Biological Processglutathione catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      ggt
    • ORF names
      C2E25_08495

Organism names

  • Taxonomic identifier
  • Strain
    • HR-1
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfuromonadia > Desulfuromonadales > Geothermobacteraceae > Geothermobacter

Accessions

  • Primary accession
    A0A2K2HA89

Proteomes

PTM/Processing

Post-translational modification

Cleaved by autocatalysis into a large and a small subunit.

Keywords

Interaction

Subunit

This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias56-71Polar residues
Region56-91Disordered

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    646
  • Mass (Da)
    68,613
  • Last updated
    2018-03-28 v1
  • Checksum
    3A7AE37709C4220F
MMPPKRSWPACMPSGGLPGFPTQPRCRTRREVDMCRLCCLLLALGLSIAACHAPQPLQPTSESSSPVQDEPSAAQVIPPGQVPPDERPPVVTPDISLEPLEKISPVAPSAPVFPVAAEEPFGVVAAVHPLAVAAGMRVLSGGGNAVDAAVAAALTLGVVDGYNSGIGGGCLILVRASGGELLAIDGRETAPRLADREMFLHTGEADPDLSRNGPLAVGTPGTLAAYRLLLDKAGTKKLSDLIRPAADLAEQGFLIDGRYADRLRRVAGRLKRDPGSAAIFLDRRGRPWPAGHRLRQPDLAASYRSIAREGIAWFYRGAYARSLDRWMRAHGGVLRFADLADYRPVHRQPIRSGYRGLTIVGFPPPSSGGVLVAEILNILQHFPLARLPAGPRLHLVAEAEKRAFADRAFWLGDADFVPVPRGLLDKGYAAELAAGIDTEMATPVPVAGTPPRAASDLFEHHTTHIAAADRAGNWVAITATLNTSFGAKVVVPGSGIVLNNEMDDFAVAPGVPNSFGLVGAEANSVASGKRPLSSMSPTLVLQGKKPILTLGAAGGPTIISQVVQVLINRFDLGMTLPAAVAAPRIHHQWRPDRLRVERRLSLPVRRVLEKAGHRLQTRGTIGVTQAVGRDREGHLRAVIDPRLQAE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias56-71Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PPFX01000016
EMBL· GenBank· DDBJ
PNU20216.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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