date: '2026-09-20'
scope: Seven remaining featured TreeGrafter exemplars; all annotation rows including earlier NEW proposals
genes:
- gene: ECOLX/mcr-1
  gene_file: genes/ECOLX/mcr-1/mcr-1-ai-review.yaml
  status: reviewed
  scope: full_gene
  outcome: changed
  annotation_count: 9
  annotations:
  - term_id: GO:0005886
    term_label: plasma membrane
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: Correct and specific cellular location; consistent with the experimental localization (PMID:27655155)
      and the UniProt 'Cell inner membrane' annotation.
  - term_id: GO:0009244
    term_label: lipopolysaccharide core region biosynthetic process
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: MARK_AS_OVER_ANNOTATED
    action: MARK_AS_OVER_ANNOTATED
    outcome: retained
    rationale: 'Mechanistically inaccurate over-propagation: a lipid A phosphoethanolamine transferase
      is binned under ''LPS core region biosynthetic process''. The accurate process is captured by the
      NEW ''response to antibiotic'' annotation below; the molecular event is lipid A modification, not
      core biosynthesis.'
  - term_id: GO:0016020
    term_label: membrane
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: MODIFY
    action: ACCEPT
    outcome: changed
    rationale: Membrane is a valid broad description of the experimentally supported plasma-membrane location.
      A more specific annotation does not make this InterPro annotation incorrect.
  - term_id: GO:0016772
    term_label: transferase activity, transferring phosphorus-containing groups
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: MODIFY
    action: ACCEPT
    outcome: changed
    rationale: This broad transferase activity is chemically entailed by the established lipid A modification
      reaction and is a current GO ancestor of GO:0043838. Retain it alongside the more specific function.
  - term_id: GO:0016776
    term_label: phosphotransferase activity, phosphate group as acceptor
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: MODIFY
    action: MODIFY
    outcome: changed
    rationale: 'Retain MODIFY as a refinement to GO:0043838, not a finding that phosphoethanolamine transfer
      is false. Existing reports disagree: Falcon treats the phosphate-acceptor wording as applicable,
      whereas OpenScientist emphasizes EC 2.7.8.43 and the substituted-phosphate branch. Current QuickGO
      places GO:0043838 under GO:0016780 and GO:0016772, not GO:0016776. The broad text alone does not
      establish a wrong substrate reaction or a wrong graft position.'
  - term_id: GO:0005886
    term_label: plasma membrane
    evidence_type: EXP
    original_reference_id: PMID:27655155
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: Experimental evidence for the bacterial inner (plasma) membrane location; this is the core
      cellular component for the enzyme.
  - term_id: GO:0043838
    term_label: phosphatidylethanolamine:Kdo2-lipid A phosphoethanolamine transferase activity
    evidence_type: IDA
    original_reference_id: PMID:27655155
    previous_action: NEW
    action: NEW
    outcome: retained
    rationale: Replaces the two over-general IEA MF terms with the specific, structurally and biochemically
      supported activity. Directly evidenced by the MCR-1 structure/mechanism papers and EC 2.7.8.43.
  - term_id: GO:0046677
    term_label: response to antibiotic
    evidence_type: IMP
    original_reference_id: PMID:26603172
    previous_action: NEW
    action: NEW
    outcome: retained
    rationale: The biological process in which MCR-1 participates is antibiotic (colistin) resistance
      via target modification; this is the accurate BP, replacing the mis-propagated GO:0009244.
  - term_id: GO:0008270
    term_label: zinc ion binding
    evidence_type: IDA
    original_reference_id: PMID:27655155
    previous_action: NEW
    action: NEW
    outcome: retained
    rationale: Structurally supported zinc binding at the active site; the zinc is mechanistically required
      and is more informative than the keyword-derived 'metal ion binding'.
  changes:
  - term_id: GO:0016020
    previous_action: MODIFY
    action: ACCEPT
  - term_id: GO:0016772
    previous_action: MODIFY
    action: ACCEPT
  evidence:
    existing_adjudications:
    - genes/ECOLX/mcr-1/mcr-1-hypotheses/function-hypothesis-go-0016776/falcon.md
    - genes/ECOLX/mcr-1/mcr-1-hypotheses/function-hypothesis-go-0016776/openscientist.md
    notes_file: genes/ECOLX/mcr-1/mcr-1-notes.md
  adjudication:
    needed: null
    duplicate_runs_launched: false
  validation:
    command: just validate ECOLX mcr-1
    result: passed
  history_record: history/genes/ECOLX/mcr-1/2026-09-21T010056Z-codex-57d196.yaml
  history_validation:
    command: just validate-history history/genes/ECOLX/mcr-1/2026-09-21T010056Z-codex-57d196.yaml
    result: passed
  source_rows_preserved: true
  final_annotation_count: 9
- gene: SACEN/eryAIII
  gene_file: genes/SACEN/eryAIII/eryAIII-ai-review.yaml
  status: reviewed
  scope: full_gene
  outcome: changed
  annotation_count: 8
  annotations:
  - term_id: GO:0004312
    term_label: fatty acid synthase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: MODIFY
    action: MODIFY
    outcome: changed
    rationale: The characterized assembly-line product is 6-deoxyerythronolide B, a macrolide polyketide.
      This supports a polyketide-synthase refinement of the fatty-acid-synthase assignment. Shared acyl-carrier/condensation
      chemistry is real; absence of DH/ER domains from this particular subunit is not, by itself, a universal
      discriminator of all fatty acid synthases.
  - term_id: GO:0004315
    term_label: 3-oxoacyl-[acyl-carrier-protein] synthase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: MODIFY
    action: MODIFY
    outcome: changed
    rationale: The current GO:0004315 definition specifies malonyl-ACP condensation. DEBS modules 5 and
      6 use methylmalonyl-derived units during erythronolide assembly, so retain a substrate-aware refinement
      to polyketide synthase activity. The distinction is the defined reaction, not a rule excluding all
      PKS domains merely because the term is familiar from fatty-acid synthesis.
  - term_id: GO:0006633
    term_label: fatty acid biosynthetic process
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: MODIFY
    action: MODIFY
    outcome: retained
    rationale: Wrong process. Replace with GO:1901115 (erythromycin biosynthetic process).
  - term_id: GO:0016740
    term_label: transferase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: Accurate (general) molecular function.
  - term_id: GO:0016746
    term_label: acyltransferase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: Correct component (AT-domain) molecular function.
  - term_id: GO:0031177
    term_label: phosphopantetheine binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: Correct component (ACP-domain) molecular function.
  - term_id: GO:0033068
    term_label: macrolide biosynthetic process
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: Accurate biological process.
  - term_id: GO:0047879
    term_label: erythronolide synthase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: Correct, specific molecular function for the DEBS subunit.
  changes: []
  evidence:
    existing_adjudications:
    - genes/SACEN/eryAIII/eryAIII-hypotheses/function-hypothesis-go-0004312/falcon.md
    - genes/SACEN/eryAIII/eryAIII-hypotheses/function-hypothesis-go-0004312/openscientist.md
    notes_file: genes/SACEN/eryAIII/eryAIII-notes.md
  adjudication:
    needed: null
    duplicate_runs_launched: false
  validation:
    command: just validate SACEN eryAIII
    result: passed
  history_record: history/genes/SACEN/eryAIII/2026-09-21T010059Z-codex-ecf8a0.yaml
  history_validation:
    command: just validate-history history/genes/SACEN/eryAIII/2026-09-21T010059Z-codex-ecf8a0.yaml
    result: passed
  source_rows_preserved: true
  final_annotation_count: 8
- gene: NICAT/NaPMT3
  gene_file: genes/NICAT/NaPMT3/NaPMT3-ai-review.yaml
  status: reviewed
  scope: full_gene
  outcome: changed
  annotation_count: 7
  annotations:
  - term_id: GO:0003824
    term_label: catalytic activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: MARK_AS_OVER_ANNOTATED
    action: ACCEPT
    outcome: changed
    rationale: Catalytic activity is an entailed broad molecular function of the accepted putrescine N-methyltransferase
      activity. Its generality is not over-annotation.
  - term_id: GO:0004766
    term_label: spermidine synthase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: REMOVE
    action: REMOVE
    outcome: changed
    rationale: PMT proteins evolved from spermidine synthase but now catalyze putrescine N-methylation
      in alkaloid biosynthesis. The target carries the PMT-specific IPR025803/PROSITE assignment and the
      SAM-dependent methylation reaction. The existing reports support a PMT-versus-SPDS functional divergence,
      not loss of catalytic function.
  - term_id: GO:0005829
    term_label: cytosol
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
    outcome: changed
    rationale: The TreeGrafter localization is compatible with the PMT family and there is no target-specific
      evidence of a different compartment. Less detailed study of PMT3 than PMT1 does not make the same
      enzymatic location non-core.
  - term_id: GO:0008295
    term_label: spermidine biosynthetic process
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: REMOVE
    action: REMOVE
    outcome: retained
    rationale: PMT3 channels putrescine into alkaloid biosynthesis rather than spermidine biosynthesis.
  - term_id: GO:0009753
    term_label: response to jasmonic acid
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    previous_action: KEEP_AS_NON_CORE
    action: KEEP_AS_NON_CORE
    outcome: retained
    rationale: The annotation fits nicotine defense-pathway context but is less central than the catalytic
      and pathway assignments.
  - term_id: GO:0030750
    term_label: putrescine N-methyltransferase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: UniProt explicitly assigns the putrescine methyltransferase reaction to this root-expressed
      paralog.
  - term_id: GO:0042179
    term_label: nicotine biosynthetic process
    evidence_type: IEA
    original_reference_id: GO_REF:0000041
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
    outcome: changed
    rationale: UniProt assigns PMT3 to the putrescine-to-N-methylputrescine step of nicotine biosynthesis;
      its PMT-specific InterPro signature and root expression support that inference. Uncertainty about
      relative flux contribution compared with PMT1 paralogs does not make the same pathway activity non-core.
  changes:
  - term_id: GO:0003824
    previous_action: MARK_AS_OVER_ANNOTATED
    action: ACCEPT
  - term_id: GO:0005829
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
  - term_id: GO:0042179
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
  evidence:
    existing_adjudications:
    - genes/NICAT/NaPMT3/NaPMT3-hypotheses/function-hypothesis-go-0004766/falcon.md
    - genes/NICAT/NaPMT3/NaPMT3-hypotheses/function-hypothesis-go-0004766/openscientist.md
    notes_file: genes/NICAT/NaPMT3/NaPMT3-notes.md
  adjudication:
    needed: null
    duplicate_runs_launched: false
  validation:
    command: just validate NICAT NaPMT3
    result: passed
    warnings:
    - General deep-research file not cited; existing focused reports and primary evidence are cited.
  history_record: history/genes/NICAT/NaPMT3/2026-09-21T010103Z-codex-5121e5.yaml
  history_validation:
    command: just validate-history history/genes/NICAT/NaPMT3/2026-09-21T010103Z-codex-5121e5.yaml
    result: passed
  source_rows_preserved: true
  final_annotation_count: 7
- gene: DOROP/ADAR2
  gene_file: genes/DOROP/ADAR2/ADAR2-ai-review.yaml
  status: reviewed
  scope: full_gene
  outcome: changed
  annotation_count: 13
  annotations:
  - term_id: GO:0003723
    term_label: RNA binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
    outcome: changed
    rationale: The broad RNA-binding term is entailed by directly supported dsRNA binding. It is part
      of the core substrate-recognition mechanism, not peripheral simply because a more specific binding
      annotation also exists.
  - term_id: GO:0003725
    term_label: double-stranded RNA binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: dsRNA binding is a core molecular function of sqADAR2, demonstrated directly using recombinant
      protein with quantitative binding assays. The three dsRBD architecture of sqADAR2a is a defining
      and unique feature of this enzyme. This is at the right level of specificity for the binding function.
  - term_id: GO:0003726
    term_label: double-stranded RNA adenosine deaminase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: This is the defining catalytic activity of sqADAR2 and the most important molecular function
      annotation. It has been demonstrated directly using recombinant enzyme on multiple substrates, with
      quantitative activity data. The term is at exactly the right level of specificity.
  - term_id: GO:0004000
    term_label: adenosine deaminase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: MODIFY
    action: MODIFY
    outcome: retained
    rationale: GO:0004000 (adenosine deaminase activity) describes the deamination of free adenosine,
      which is the activity of ADA enzymes, not ADAR enzymes. ADAR2 specifically deaminates adenosine
      residues within double-stranded RNA. The correct term GO:0003726 is already annotated, so this annotation
      should be replaced to avoid confusion between ADA and ADAR activities.
  - term_id: GO:0005634
    term_label: nucleus
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: Nuclear localization is well-supported for ADAR2 enzymes generally, as co-transcriptional
      editing of pre-mRNAs occurs in the nucleus. While sqADAR2 is also found in the cytoplasm, nuclear
      localization remains valid.
  - term_id: GO:0005730
    term_label: nucleolus
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: UNDECIDED
    action: UNDECIDED
    outcome: changed
    rationale: Retain UNDECIDED because the available squid localization evidence resolves nucleus versus
      cytoplasm but not nucleolus. Vertebrate nucleolar localization can support a phylogenetic hypothesis;
      missing target-specific microscopy alone is not a refutation. An explicit comparison of nucleolar-targeting
      determinants would help assess this prediction.
  - term_id: GO:0005737
    term_label: cytoplasm
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: Cytoplasmic localization is directly demonstrated in squid neurons, where sqADAR2 is found
      in the axoplasm and is catalytically active. This represents a significant finding that RNA editing
      occurs outside the nucleus in squid. The term is appropriate.
  - term_id: GO:0006382
    term_label: adenosine to inosine editing
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: A-to-I editing is the defining biological process for sqADAR2. This is supported by extensive
      direct evidence from multiple studies using recombinant protein assays and transcriptome-wide editing
      profiling. The term is at exactly the right level of specificity.
  - term_id: GO:0006396
    term_label: RNA processing
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
    outcome: changed
    rationale: The broad process describes the same direct catalytic work as the accepted A-to-I editing
      annotation. Its generality is not evidence of a non-core role.
  - term_id: GO:0008251
    term_label: tRNA-specific adenosine deaminase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: REMOVE
    action: REMOVE
    outcome: changed
    rationale: tRNA-specific adenosine deaminase activity is the function of ADAT enzymes, not ADAR enzymes.
      sqADAR2 has been tested and shown to be active on dsRNA and mRNA substrates. There is no evidence
      that sqADAR2 edits tRNAs, and the domain architecture (dsRBDs + ADAR-type deaminase domain) is inconsistent
      with tRNA editing activity. This is a phylogenetic transfer error likely due to the shared deaminase
      domain superfamily between ADARs and ADATs. The existing OpenScientist report supports the three-dsRBD
      architecture, while Falcon incorrectly labels C1JAR3 as the two-dsRBD sqADAR2b variant. The cached
      786-aa sequence has three dsRNA-binding domains and is consistent with sqADAR2a. Functional divergence
      is supported, but no exact historical graft error is established from domain architecture alone.
  - term_id: GO:0016556
    term_label: mRNA modification
    evidence_type: NAS
    original_reference_id: PMID:25569156
    previous_action: NEW
    action: NEW
    outcome: retained
    rationale: mRNA modification (GO:0016556) captures the specific substrate class (mRNA) that sqADAR2
      acts on. While GO:0006382 (adenosine to inosine editing) is the most specific process term, mRNA
      modification highlights that the primary biological role of sqADAR2 is to modify mRNAs encoding
      proteins, as opposed to editing structural RNAs or tRNAs.
  - term_id: GO:0008270
    term_label: zinc ion binding
    evidence_type: NAS
    original_reference_id: PMID:37342458
    previous_action: NEW
    action: NEW
    outcome: retained
    rationale: Zinc ion binding is an inherent property of the ADAR catalytic deaminase domain. The UniProt
      entry lists zinc binding as a keyword. While metal ion binding (GO:0046872) is annotated in the
      UniProt GO cross-references, the more specific zinc ion binding term better captures the biochemistry
      of the ADAR active site.
  - term_id: GO:1904115
    term_label: axon cytoplasm
    evidence_type: NAS
    original_reference_id: PMID:32201888
    previous_action: NEW
    action: NEW
    outcome: retained
    rationale: Axon cytoplasm localization is directly demonstrated for sqADAR2 in the squid giant axon
      system. This is a key finding that distinguishes sqADAR2 function from the canonical nuclear-only
      editing paradigm. The term GO:1904115 (axon cytoplasm) is more specific than GO:0005737 (cytoplasm)
      and accurately captures the demonstrated localization.
  changes:
  - term_id: GO:0003723
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
  - term_id: GO:0006396
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
  evidence:
    existing_adjudications:
    - genes/DOROP/ADAR2/ADAR2-hypotheses/function-hypothesis-go-0008251/falcon.md
    - genes/DOROP/ADAR2/ADAR2-hypotheses/function-hypothesis-go-0008251/openscientist.md
    notes_file: genes/DOROP/ADAR2/ADAR2-notes.md
  adjudication:
    needed: Nucleolar localization remains UNDECIDED; functional ADAR-vs-ADAT hypothesis already has two
      reports.
    duplicate_runs_launched: false
  validation:
    command: just validate DOROP ADAR2
    result: passed
    warnings:
    - General deep-research file not cited; existing focused reports and primary evidence are cited.
  history_record: history/genes/DOROP/ADAR2/2026-09-21T010105Z-codex-a21475.yaml
  history_validation:
    command: just validate-history history/genes/DOROP/ADAR2/2026-09-21T010105Z-codex-a21475.yaml
    result: passed
  source_rows_preserved: true
  final_annotation_count: 13
- gene: NICAT/NaUGT1_candidate_UGT85A2_0
  gene_file: genes/NICAT/NaUGT1_candidate_UGT85A2_0/NaUGT1_candidate_UGT85A2_0-ai-review.yaml
  status: reviewed
  scope: full_gene
  outcome: Gene-level nicotine function established from primary supplementary sequences and assays; report
    categorical refutation rejected with reproducible evidence. Alternative substrate activities remain
    unresolved.
  annotation_count: 6
  annotations:
  - term_id: GO:0008194
    term_label: UDP-glycosyltransferase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: MODIFY
    action: ACCEPT
    outcome: changed
    rationale: UDP-glycosyltransferase activity is a valid broad parent of the accepted UDP-glucosyltransferase
      function. The more specific donor assignment does not invalidate this broad InterPro inference.
  - term_id: GO:0035251
    term_label: UDP-glucosyltransferase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    previous_action: ACCEPT
    action: MODIFY
    outcome: retained
    rationale: GO:0050139 already exists for this exact reaction. The Cell 2026 NaUGT1 assay/perturbation
      primers map to the g26396 locus, and its primer-compatible extended ORF contains the complete A0A2H4GSI3
      sequence. Independent tobacco UGT1 supplements explicitly map the assayed N-glucosyltransferase
      to a close homolog (466 identities across 485 alignment columns). This establishes gene-level function;
      the retrieved assays do not directly test the isolated 485-aa database form. Narrow the generic
      MF using the existing term rather than proposing a duplicate ontology term.
  - term_id: GO:0080043
    term_label: quercetin 3-O-glucosyltransferase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: REMOVE
    action: UNDECIDED
    outcome: changed
    rationale: Primary 2026 data support nicotinate N-glucosylation at the mapped g26396 locus, with a
      documented construct-boundary caveat. They do not assay every alternative acceptor. Neither the
      positive nicotine function nor sequence-family distance establishes that quercetin or 7-deoxyloganetic
      acid cannot also be glucosylated. The earlier reports wrongly used missing assays and automated
      homolog names as negative biochemical evidence. Retain the source assertion for substrate-panel
      adjudication rather than asserting a negative function.
  - term_id: GO:0080044
    term_label: quercetin 7-O-glucosyltransferase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: REMOVE
    action: UNDECIDED
    outcome: changed
    rationale: Primary 2026 data support nicotinate N-glucosylation at the mapped g26396 locus, with a
      documented construct-boundary caveat. They do not assay every alternative acceptor. Neither the
      positive nicotine function nor sequence-family distance establishes that quercetin or 7-deoxyloganetic
      acid cannot also be glucosylated. The earlier reports wrongly used missing assays and automated
      homolog names as negative biochemical evidence. Retain the source assertion for substrate-panel
      adjudication rather than asserting a negative function.
  - term_id: GO:0102970
    term_label: 7-deoxyloganetic acid glucosyltransferase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000003
    previous_action: MARK_AS_OVER_ANNOTATED
    action: UNDECIDED
    outcome: changed
    rationale: Primary 2026 data support nicotinate N-glucosylation at the mapped g26396 locus, with a
      documented construct-boundary caveat. They do not assay every alternative acceptor. Neither the
      positive nicotine function nor sequence-family distance establishes that quercetin or 7-deoxyloganetic
      acid cannot also be glucosylated. The earlier reports wrongly used missing assays and automated
      homolog names as negative biochemical evidence. Retain the source assertion for substrate-panel
      adjudication rather than asserting a negative function.
  - term_id: GO:0042179
    term_label: nicotine biosynthetic process
    evidence_type: IDA
    original_reference_id: PMID:41928514
    previous_action: NEW
    action: NEW
    outcome: reinstated_author_proposal_with_primary_evidence
    rationale: Reinstate the prior author proposal with primary biochemical evidence and verified gene-level
      identity rather than the earlier notes-only TAS. NaUGT1 itself catalyzes an on-pathway reaction,
      established by recombinant assay and pathway reconstruction, independently of knockout necessity
      evidence. Supplemental primers map to g26396; the inferred N-terminal extension relative to the
      cached protein is documented, and no unverified isoform identifier is invented. QuickGO confirms
      the process definition/parents and analogous annotations on PMT1, PMT3, QPT2 and A622. No redundant
      process ancestor/descendant or GO-CAM assignment exists on this target.
  changes:
  - term_id: GO:0008194
    previous_action: MODIFY
    action: ACCEPT
  - term_id: GO:0080043
    previous_action: REMOVE
    action: UNDECIDED
  - term_id: GO:0080044
    previous_action: REMOVE
    action: UNDECIDED
  - term_id: GO:0102970
    previous_action: MARK_AS_OVER_ANNOTATED
    action: UNDECIDED
  - term_id: GO:0042179
    previous_action: NEW
    action: WITHDRAWN
    reason: Exact-target nicotine function remains unresolved; retain hypothesis/evidence in notes and
      suggested_questions pending focused mapping adjudication.
  evidence:
    existing_adjudications:
    - genes/NICAT/NaUGT1_candidate_UGT85A2_0/NaUGT1_candidate_UGT85A2_0-hypotheses/function-hypothesis-go-0080043/falcon.md
    - genes/NICAT/NaUGT1_candidate_UGT85A2_0/NaUGT1_candidate_UGT85A2_0-hypotheses/function-hypothesis-go-0080043/openscientist.md
    - genes/NICAT/NaUGT1_candidate_UGT85A2_0/NaUGT1_candidate_UGT85A2_0-hypotheses/naugt1-candidate-identity-and-nicotinate-glucosylation/openscientist.md
    notes_file: genes/NICAT/NaUGT1_candidate_UGT85A2_0/NaUGT1_candidate_UGT85A2_0-notes.md
    primary_references:
    - PMID:42151135
    - PMID:41928514
    - PMID:31611893
    bioinformatics: genes/NICAT/NaUGT1_candidate_UGT85A2_0/NaUGT1_candidate_UGT85A2_0-bioinformatics/RESULTS.md
  adjudication:
    status: incorporated
    job_id: a85d6e42-5653-4e27-a7f7-7c4db18ffd6a
    verdict_assessment: DISPUTED; pathway-exclusion finding OVERTURNED by primary 2026 reconstitution.
    findings_incorporated:
    - Exact tobacco UGT1 mapping A0A1S3YWH6/Nitab4.5_0006222g0020 from original supplemental tables; assayed 479-aa
      sequence globally 96.08% identical to target across all 485 columns.
    - Cell NaUGT1 primers map to the same g26396 genomic locus; inferred 530-aa construct contains complete 485-aa
      target unchanged after 45-aa extension.
    - Report O-versus-N family exclusion and storage-only pathway model contradicted by two 2026 primaries;
      plant nicotinate N-GTs already characterized in PMID:31611893.
    - Artifact average linkage mislabeled neighbor joining; identity traceback terminal overhang issue;
      independently recomputed published construct instead.
    - The positive nicotinate reaction does not exclude promiscuous alternative substrates; three source-specific
      MF claims remain UNDECIDED.
    duplicate_runs_launched: false
    remaining_expert_questions:
    - Native initiation site and activity of isolated 485-aa form.
    - Quantified quercetin/iridoid substrate panel.
  validation:
    command: just validate NICAT NaUGT1_candidate_UGT85A2_0
    result: passed
    warnings:
    - 'Uncited Falcon annotation support: primary 2026 evidence supersedes its unresolved mapping; report
      retained with DISPUTED assessment.'
  final_annotation_count: 6
  history_record: history/genes/NICAT/NaUGT1_candidate_UGT85A2_0/2026-09-21T010107Z-codex-0fd609.yaml
  history_validation:
    command: just validate-history history/genes/NICAT/NaUGT1_candidate_UGT85A2_0/2026-09-21T010107Z-codex-0fd609.yaml
    result: passed
  source_rows_preserved: true
  followup_changes:
  - term_id: GO:0035251
    from_action: ACCEPT
    action: MODIFY
    replacement: GO:0050139
    reason: Exact existing MF verified; primary assays mapped to g26396.
  - term_id: GO:0042179
    from_action: WITHDRAWN
    action: NEW
    reason: Reinstated using primary IDA and independently verified locus identity, preserving 485-aa construct
      caveat.
  - section: proposed_new_terms
    change: Removed duplicate nicotinate N-glucosyltransferase proposal; GO:0050139 already exists.
  followup_history_record: history/genes/NICAT/NaUGT1_candidate_UGT85A2_0/2026-09-21T025359Z-codex-4b25d4.yaml
  followup_history_validation: passed
- gene: PSEPK/aceK
  gene_file: genes/PSEPK/aceK/aceK-ai-review.yaml
  status: reviewed
  scope: full_gene
  outcome: changed
  annotation_count: 10
  annotations:
  - term_id: GO:0004721
    term_label: phosphoprotein phosphatase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: MODIFY
    action: ACCEPT
    outcome: changed
    rationale: Both existing adjudications support phosphoprotein phosphatase activity in substance. A
      more specific substrate term is useful in the core summary, but its availability does not make the
      TreeGrafter parent assertion biologically incorrect.
  - term_id: GO:0005524
    term_label: ATP binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: MARK_AS_OVER_ANNOTATED
    action: ACCEPT
    outcome: changed
    rationale: The UniProt record explicitly annotates ATP-binding residues, and the characterized AceK
      structure contains ATP. This functional ligand interaction is real and core; coexistence with kinase
      activity is not over-annotation.
  - term_id: GO:0005737
    term_label: cytoplasm
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: UniProt annotates the cytoplasmic location and this is consistent with the function of
      a soluble metabolic regulatory enzyme.
  - term_id: GO:0006006
    term_label: glucose metabolic process
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: MARK_AS_OVER_ANNOTATED
    action: MARK_AS_OVER_ANNOTATED
    outcome: changed
    rationale: Glucose-versus-acetate growth changes the AceK/IDH regulatory state. That observation supports
      metabolic regulation but does not itself establish a glucose-specific metabolic pathway role, since
      TCA and glyoxylate partitioning also concerns other carbon sources. Retain the over-annotation judgment
      with this scope distinction, without claiming that AceK is inactive whenever cells grow on glucose.
  - term_id: GO:0006097
    term_label: glyoxylate cycle
    evidence_type: IEA
    original_reference_id: GO_REF:0000104
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: AceK enables flux through the glyoxylate shunt by inactivating IDH, partitioning isocitrate
      toward isocitrate lyase and malate synthase. This is a defining biological role of the enzyme.
  - term_id: GO:0006099
    term_label: tricarboxylic acid cycle
    evidence_type: IEA
    original_reference_id: GO_REF:0000104
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: By reactivating IDH (dephosphorylation), AceK restores TCA-cycle flux; by inactivating
      IDH (phosphorylation) it diverts flux to the glyoxylate bypass. This regulatory role makes the TCA
      cycle association appropriate.
  - term_id: GO:0008772
    term_label: '[isocitrate dehydrogenase (NADP+)] kinase activity'
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: ACCEPT
    action: ACCEPT
    outcome: retained
    rationale: Matches the UniProt-annotated catalytic activity (EC 2.7.11.5) and the kinase half of the
      bifunctional enzyme. This is a central, specific core function.
  - term_id: GO:0016208
    term_label: AMP binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
    outcome: changed
    rationale: The E. coli AceK structure shows AMP at an interdomain allosteric site controlling the
      opposing catalytic activities. This provides positive family-level support for the TreeGrafter inference
      to the conserved P. putida AceK. An unmeasured target-specific binding constant is not sufficient
      reason to mark the inherited mechanism non-core.
  - term_id: GO:0016788
    term_label: hydrolase activity, acting on ester bonds
    evidence_type: IEA
    original_reference_id: GO_REF:0000104
    previous_action: MARK_AS_OVER_ANNOTATED
    action: ACCEPT
    outcome: changed
    rationale: Hydrolase activity acting on ester bonds is a valid broad function of the enzyme. Redundancy
      with substrate-specific phosphatase activity is not a biological error.
  - term_id: GO:0016791
    term_label: phosphatase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: MODIFY
    action: ACCEPT
    outcome: changed
    rationale: Phosphatase activity is entailed by the accepted specific phosphoprotein dephosphorylation
      reaction. Retain the correct InterPro parent term.
  changes:
  - term_id: GO:0004721
    previous_action: MODIFY
    action: ACCEPT
  - term_id: GO:0005524
    previous_action: MARK_AS_OVER_ANNOTATED
    action: ACCEPT
  - term_id: GO:0016208
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
  - term_id: GO:0016788
    previous_action: MARK_AS_OVER_ANNOTATED
    action: ACCEPT
  - term_id: GO:0016791
    previous_action: MODIFY
    action: ACCEPT
  evidence:
    existing_adjudications:
    - genes/PSEPK/aceK/aceK-hypotheses/function-hypothesis-go-0004721/falcon.md
    - genes/PSEPK/aceK/aceK-hypotheses/function-hypothesis-go-0004721/openscientist.md
    notes_file: genes/PSEPK/aceK/aceK-notes.md
  adjudication:
    needed: null
    duplicate_runs_launched: false
  validation:
    command: just validate PSEPK aceK
    result: passed
    warnings:
    - The specific phosphatase core term is not separately in existing_annotations; broad correct source
      annotations are retained. No redundant NEW was added.
  history_record: history/genes/PSEPK/aceK/2026-09-21T010110Z-codex-3e6fb9.yaml
  history_validation:
    command: just validate-history history/genes/PSEPK/aceK/2026-09-21T010110Z-codex-3e6fb9.yaml
    result: passed
  source_rows_preserved: true
  final_annotation_count: 10
- gene: PSEPK/ahpC
  gene_file: genes/PSEPK/ahpC/ahpC-ai-review.yaml
  status: reviewed
  scope: full_gene
  outcome: changed
  annotation_count: 13
  annotations:
  - term_id: GO:0004601
    term_label: peroxidase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: MODIFY
    action: ACCEPT
    outcome: changed
    rationale: Peroxiredoxin activity is peroxidase activity. The broad parent does not become wrong because
      the catalytic subfamily is known.
  - term_id: GO:0005737
    term_label: cytoplasm
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: ACCEPT
    action: ACCEPT
    outcome: changed
    rationale: The available evidence supports AhpC as a soluble cytoplasmic protein.
  - term_id: GO:0005829
    term_label: cytosol
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: MODIFY
    action: ACCEPT
    outcome: changed
    rationale: The current cytosol definition excludes organelles but includes soluble proteins and protein
      complexes. It applies to bacteria; the existing cytoplasm annotation does not justify replacing
      this correct, more specific localization.
  - term_id: GO:0006979
    term_label: response to oxidative stress
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
    outcome: changed
    rationale: Direct peroxide reduction performs work in the oxidative-stress response. The more specific
      detoxification annotation is complementary and does not make this core protective role peripheral.
  - term_id: GO:0008379
    term_label: thioredoxin peroxidase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: MODIFY
    action: MODIFY
    outcome: changed
    rationale: QuickGO checked on 2026-09-20 marks GO:0008379 obsolete; preserve the source GOA identifier
      and refine its review to the active peroxiredoxin term. Independently, the existing reports support
      a typical AhpC/AhpF system and distinguish its immediate protein reductant from free thioredoxin.
      Their donor discussion does not undermine peroxide reduction, antioxidant activity or H2O2 catabolism.
  - term_id: GO:0016209
    term_label: antioxidant activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
    outcome: changed
    rationale: The broad antioxidant activity follows from the accepted peroxiredoxin reaction; it is
      the same core function at broader granularity.
  - term_id: GO:0016491
    term_label: oxidoreductase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    previous_action: MODIFY
    action: ACCEPT
    outcome: changed
    rationale: This broad parent is chemically entailed by peroxiredoxin activity. It is acceptable alongside
      the specific function.
  - term_id: GO:0033554
    term_label: cellular response to stress
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
    outcome: changed
    rationale: The general stress-response annotation is supported by the direct antioxidant mechanism
      and OxyR-associated response. Broadness alone does not turn that response into a non-core function.
  - term_id: GO:0042744
    term_label: hydrogen peroxide catabolic process
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: MODIFY
    action: ACCEPT
    outcome: changed
    rationale: Hydrogen peroxide is among the substrates explicitly listed in the UniProt reaction/function
      annotation. Activity toward additional organic hydroperoxides does not invalidate the specific H2O2
      catabolic process or require generalizing it.
  - term_id: GO:0045454
    term_label: cell redox homeostasis
    evidence_type: IEA
    original_reference_id: GO_REF:0000118
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
    outcome: changed
    rationale: Peroxide reduction directly limits oxidative burden as part of the antioxidant system.
      This is a supported broad process, not merely an unrelated phenotype.
  - term_id: GO:0051920
    term_label: peroxiredoxin activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: ACCEPT
    action: ACCEPT
    outcome: changed
    rationale: This term captures the core catalytic identity of the protein without overcommitting to
      donor-specific chemistry at the single-gene-product level.
  - term_id: GO:0098869
    term_label: cellular oxidant detoxification
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: ACCEPT
    action: ACCEPT
    outcome: changed
    rationale: The process term aligns with both the known chemistry of the enzyme and the regulatory/physiological
      evidence from P. putida.
  - term_id: GO:0102039
    term_label: NADH-dependent peroxiredoxin activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    previous_action: MODIFY
    action: MODIFY
    outcome: changed
    rationale: The coupled AhpCF system is NADH-dependent, as recognized by both existing reports. AhpC
      directly reduces peroxide while AhpF supplies electrons from NADH. Retain the donor-independent
      single-subunit refinement to peroxiredoxin activity; this is a gene-product scope distinction, not
      a claim that NADH-dependent AhpCF physiology is absent. Whether GO:0102039 is conventionally assigned
      to the catalytic AhpC subunit itself remains a useful curation second opinion.
  changes:
  - term_id: GO:0004601
    previous_action: MODIFY
    action: ACCEPT
  - term_id: GO:0005829
    previous_action: MODIFY
    action: ACCEPT
  - term_id: GO:0006979
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
  - term_id: GO:0016209
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
  - term_id: GO:0016491
    previous_action: MODIFY
    action: ACCEPT
  - term_id: GO:0033554
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
  - term_id: GO:0042744
    previous_action: MODIFY
    action: ACCEPT
  - term_id: GO:0045454
    previous_action: KEEP_AS_NON_CORE
    action: ACCEPT
  evidence:
    existing_adjudications:
    - genes/PSEPK/ahpC/ahpC-hypotheses/function-hypothesis-go-0008379/falcon.md
    - genes/PSEPK/ahpC/ahpC-hypotheses/function-hypothesis-go-0008379/openscientist.md
    notes_file: genes/PSEPK/ahpC/ahpC-notes.md
  adjudication:
    needed: 'Optional curation scope check: GO:0102039 on AhpC catalytic subunit versus full AhpCF system;
      existing reports already discuss donor mechanism.'
    duplicate_runs_launched: false
  validation:
    command: just validate PSEPK ahpC
    result: passed
  history_record: history/genes/PSEPK/ahpC/2026-09-21T010113Z-codex-6e4a4a.yaml
  history_validation:
    command: just validate-history history/genes/PSEPK/ahpC/2026-09-21T010113Z-codex-6e4a4a.yaml
    result: passed
  source_rows_preserved: true
  final_annotation_count: 13
validation:
  all_source_fields: Compared all original non-NEW annotation metadata against HEAD; unchanged.
  original_rows_reviewed: 66
  final_annotation_rows: 65
  withdrawn_author_proposals: 1
  history_records: All seven scaffolded by just new-history with actor-name codex and passed just validate-history.
  gene_reviews: All seven pass just validate; advisory warnings documented per gene.
