family_id: PANTHER:PTHR10680
family_name: PEPTIDYL-GLYCINE ALPHA-AMIDATING MONOOXYGENASE
preferred_name: Peptide-amidation PHM/PAL proteins
summary: Peptide amidation proceeds through monooxygenase and lyase reactions, carried in separate proteins
  or combined in bifunctional PAM. Copper/ascorbate-dependent monooxygenase chemistry and PAL lyase chemistry
  reside in different structural modules.
functional_coherence: HETEROGENEOUS
coherence_reason: The quail target contains both monooxygenase and PAL-associated architecture. PAL activity
  and ascorbate interaction must be assigned to their respective modules, not inferred from the other
  reaction. The retrieved family includes separate PHM and PAL proteins and therefore neither module-specific
  activity is universal.
subfamilies:
- subfamily_id: PANTHER:PTHR10680:SF14
  label: PEPTIDYL-GLYCINE ALPHA-AMIDATING MONOOXYGENASE
  description: Recorded placement of A0A8C2TBA7. The quail target contains both monooxygenase and PAL-associated
    architecture. PAL activity and ascorbate interaction must be assigned to their respective modules,
    not inferred from the other reaction. The retrieved family includes separate PHM and PAL proteins
    and therefore neither module-specific activity is universal.
  representative_members:
  - id: UniProtKB:A0A8C2TBA7
    gene_symbol: A0A8C2TBA7
    organism: Coturnix japonica
    gene_review: genes/COTJA/A0A8C2TBA7/A0A8C2TBA7-ai-review.yaml
term_assessments:
- assessed_term:
    id: GO:0004598
    label: peptidylamidoglycolate lyase activity
  scope: UNRESOLVED
  scope_reason: PAL structural and mutagenesis data establish the lyase reaction in a zinc-containing
    beta-propeller module. Bifunctional PAM and separate PAL proteins can retain this module, whereas
    PHM-only proteins cannot inherit the lyase activity from their monooxygenase domain. The complete
    set of PAL-bearing functional branches, including shortened products, is not delimited.
  supported_by:
  - reference_id: PMID:19604476
    supporting_text: 'The structures show that PAL

      folds as a six-bladed beta-propeller'
  - reference_id: file:genes/COTJA/A0A8C2TBA7/A0A8C2TBA7-uniprot.txt
    supporting_text: DR   InterPro; IPR000323; Cu2_ascorb_mOase_N.
  - reference_id: file:genes/COTJA/A0A8C2TBA7/A0A8C2TBA7-uniprot.txt
    supporting_text: DR   InterPro; IPR024548; Cu2_monoox_C.
  - reference_id: file:genes/COTJA/A0A8C2TBA7/A0A8C2TBA7-uniprot.txt
    supporting_text: DR   InterPro; IPR000720; PHM/PAL.
  - reference_id: file:genes/COTJA/A0A8C2TBA7/A0A8C2TBA7-uniprot.txt
    supporting_text: FT   SIGNAL          1..21
- assessed_term:
    id: GO:0031418
    label: L-ascorbic acid binding
  scope: UNRESOLVED
  scope_reason: PHM kinetic experiments establish interaction with ascorbate during reduction and activation.
    That evidence belongs to the copper monooxygenase module, not to the PAL lyase module. Bifunctional
    PAM can combine both functions, but the full set of ascorbate-interacting PHM-bearing branches is
    not established by the quail exemplar.
  supported_by:
  - reference_id: PMID:35380039
    supporting_text: ascorbate binds to the enzyme to accomplish reduction
  - reference_id: file:genes/COTJA/A0A8C2TBA7/A0A8C2TBA7-uniprot.txt
    supporting_text: DR   InterPro; IPR000323; Cu2_ascorb_mOase_N.
  - reference_id: file:genes/COTJA/A0A8C2TBA7/A0A8C2TBA7-uniprot.txt
    supporting_text: DR   InterPro; IPR024548; Cu2_monoox_C.
  - reference_id: file:genes/COTJA/A0A8C2TBA7/A0A8C2TBA7-uniprot.txt
    supporting_text: DR   InterPro; IPR000720; PHM/PAL.
  - reference_id: file:genes/COTJA/A0A8C2TBA7/A0A8C2TBA7-uniprot.txt
    supporting_text: FT   SIGNAL          1..21
references:
- id: PMID:19604476
  title: 'Amidation of bioactive peptides: the structure of the lyase domain of the amidating enzyme.'
- id: PMID:35380039
  title: Pre-Steady-State Reactivity of Peptidylglycine Monooxygenase Implicates Ascorbate in Substrate
    Triggering of the Active Conformer.
- id: file:genes/COTJA/A0A8C2TBA7/A0A8C2TBA7-uniprot.txt
- id: file:interpro/panther/PTHR10680/PTHR10680-entries.csv
- id: file:interpro/panther/PTHR10680/PTHR10680-paint.tsv
review_status: COMPLETE
reviewed_by: codex
review_date: '2026-09-10'
notes: 'COTJA/A0A8C2TBA7: requested accession A0A8C2TBA7; current record A0A8C2TBA7; sequence length 846;
  source cohort ARGO50. Family boundaries were assessed using the fetched member set and the cited domain,
  literature and analytical evidence. Gene-review verdicts and ARBA assertions are not independent validation.
  PANTHER subfamily labels and membership are recorded from the frozen UniProt records and panther.obo;
  they do not by themselves prove functional uniformity within a subfamily. PAINT rows were inspected
  as ancestral assertions, but node placement is not adjudicated without the relevant descendant tree/alignment.
  No residue requirement is encoded without a verified sequence-version anchor. A target-level refutation
  is not a family-wide NOT_APPLICABLE judgment. Exact protein-name-only predictions are treated as family-identification
  hypotheses rather than invented GO predictions.'