Penicillin G acylase, C-terminal (IPR033813)

Short name: PGA_C

Overlapping homologous superfamilies


Domain relationships



Penicillin G acylase (PGA) is the key enzyme in the industrial production of beta-lactam antibiotics. PGA hydrolyzes the side chain of penicillin G and related beta-lactam antibiotics releasing 6-amino penicillanic acid (6-APA), a building block in the production of semisynthetic penicillins. PGA is widely distributed among microorganisms, including bacteria, yeast and filamentous fungi but its in vivo role remains unclear [PMID: 7816145, PMID: 12950251]. It is synthesized as a precursor which processes itself, comprising a signal sequence, and the A and B chains of the mature enzyme (209 and 557 residues respectively) joined by a spacer peptide of 54 amino acid residues. The AB heterodimer is produced by proteolytic removal of this spacer in the periplasm [PMID: 10993730]. The precursor is considered a peptidase (MEROPS family S45, MEROPS identifier S45.001). The newly-exposed N-terminal serine is the catalytic nucleophile, and PGA is a member of the Ntn hydrolase superfamily [PMID: 7477383, PMID: 10548042].

This entry represents the C-terminal or B domain of the mature protein, following the self-processing which produces the AB heterodimer [PMID: 10993730].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.