id: Pfam:PF01862
pfam_id: PF01862
name: Pyruvoyl-dependent arginine decarboxylase (PvlArgDC)
short_name: PvlArgDC
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01862
counters:
  proteins: 1021
  matches: 1055
  proteomes: 944
  taxa: 1963
  structures: 5
  alphafold_models: 877
  domain_architectures: 8
provenance:
  snapshot_id: interpro-pfam-duf-2026-10-10
  path: data/worklists/interpro-pfam-duf-2026-10-10.json
  sha256: 17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383
  generated_at: '2026-10-10T07:44:21.614711Z'
  source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/
interpro_id: InterPro:IPR002724
description: Methanococcus jannaschii contains homologues of most genes required for spermidine polyamine
  biosynthesis. Yet genomes from neither this organism nor any other euryarchaeon have orthologues of
  the pyridoxal 5'-phosphate- dependent ornithine or arginine decarboxylase genes, required to produce
  putrescine. Instead,these organisms have a new class of arginine decarboxylase (PvlArgDC) formed by
  the self-cleavage of a proenzyme into a 5-kDa subunit and a 12-kDa subunit that contains a reactive
  pyruvoyl group. Although this extremely thermostable enzyme has no significant sequence similarity to
  previously characterised proteins, conserved active site residues are similar to those of the pyruvoyl-dependent
  histidine decarboxylase enzyme, and its subunits form a similar (alpha-beta)(3) complex. Homologues
  of PvlArgDC are found in several bacterial genomes, including those of Chlamydia spp., which have no
  agmatine ureohydrolase enzyme to convert agmatine (decarboxylated arginine) into putrescine. In these
  intracellular pathogens, PvlArgDC may function analogously to pyruvoyl-dependent histidine decarboxylase;
  the cells are proposed to import arginine and export agmatine, increasing the pH and affecting the host
  cell's metabolism. Phylogenetic analysis of Pvl- ArgDC proteins suggests that this gene has been recruited
  from the euryarchaeal polyamine biosynthetic pathway to function as a degradative enzyme in bacteria
  [[cite:PUB00027451]].