id: Pfam:PF01883
pfam_id: PF01883
name: Iron-sulfur cluster assembly protein
short_name: FeS_assembly_P
seed_status: EX_DUF
characterization_status: UNSCORED
curation_status: SEEDED
source_url: https://www.ebi.ac.uk/interpro/api/entry/pfam/PF01883
counters:
  proteins: 37284
  matches: 37296
  proteomes: 17779
  taxa: 28426
  structures: 15
  alphafold_models: 24936
  domain_architectures: 120
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:IPR002744
description: This family has an alpha/beta topology, with 13 conserved hydrophobic residues at its core
  and a putative active site containing a highly conserved cysteine [[cite:PUB00037899]]. Members of this
  family are involved in a range of physiological functions. The family includes PaaJ (PhaH) [swissprot:O84984]
  from Pseudomonas putida. PaaJ forms a complex with PaaG (PhaF) [swissprot:O84982], PaaI (PhaG) [swissprot:O84983]
  and PaaK (PhaI) [swissprot:O84985], which hydroxylates phenylacetic acid to 2-hydroxyphenylacetic acid
  [[cite:PUB00005820]]. It also includes PaaD [swissprot:P76080] from Escherichia coli, a member of a
  multicomponent oxygenase involved in phenylacetyl-CoA hydroxylation [[cite:PUB00010200]]. Furthermore,
  several members of this family are shown to be involved in iron-sulfur (FeS) cluster assembly. Iron-sulfur
  (FeS) clusters are inorganic co-factors that are are able to transfer electrons and act as catalysts
  [[cite:PUB00095787]]. They are involved in diverse cellular processes including cellular respiration,
  DNA replication and repair, antibiotic resistance, and dinitrogen fixation [[cite:PUB00085141]]. The
  biogenesis of such clusters from elemental iron and sulfur is an enzymatic process that requires a set
  of specialised proteins. Proteins containing this domain include the chloroplast protein HCF101 (high
  chlorophyll fluorescence 101), [swissprot:Q6STH5], which has been described as an essential and specific
  factor for assembly of [4Fe-4S]-cluster-containing protein complexes such as the membrane complex Photosystem
  I (PSI) and the heterodimeric FTR (ferredoxin-thioredoxin reductase) complex [[cite:PUB00095787]] and
  is involved in the assembly of [4Fe-4S] clusters and their transfer to apoproteins [[cite:PUB00095787]].
  The mature HCF101 protein contains this domain at the N-terminal as well as eight cysteine residues
  along the sequence. All cysteine residues are conserved among higher plants, but of the two cysteine
  residues located in this domain only Cys128 is highly conserved and is present in the highly conserved
  P-loop domain of the plant HCF101 (CKGGVGKS) [[cite:PUB00095787]]. SufT protein from Staphylococcus
  aureus is composed of this domain solely and is shown to be involved in the maturation of FeS proteins
  [[cite:PUB00085141]]. Given all this data, it is hypothesised that this domain might play a role in
  FeS cluster assembly.