id: P49264
gene_symbol: CYP71B1
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:13288
  label: Thlaspi arvense
description: Cytochrome P450 71B1 is a heme-thiolate cytochrome P450 monooxygenase of
  field pennycress, a member of the CYP71 clan that dominates plant specialized
  (defense) metabolism. It was identified as a full-length cDNA cloned from Thlaspi
  arvense in 1994, but its substrate, catalyzed reaction, metabolic pathway, expression
  pattern, and subcellular localization have not been experimentally determined. Based
  on conserved P450 architecture it is predicted to catalyze NADPH- and O2-dependent
  oxidation of an organic substrate using a heme cofactor, with the heme iron coordinated
  by a conserved axial cysteine; like most plant P450s it is expected, but not shown, to
  be anchored to the endoplasmic reticulum membrane.
alternative_records:
- id: A0AAU9RUE5
  relationship: REFERENCE_PROTEOME_EQUIVALENT
  reference_proteome: UP000836841
  reviewed_on: '2026-10-19'
  reason: Retain P49264 as the primary Swiss-Prot accession. The reference sequence is exactly identical
    across all 496 residues. Other P450 hits are substantially less similar. This supports equivalent
    protein representation without relying on the broad automatic cytochrome-P450 name to establish substrate
    specificity.
  evidence:
  - type: PROTEOME_SEARCH
    description: MMseqs2 searched 26,379 sequences across UP000836841 at E <= 1e-5 and sensitivity 7.5,
      returning 214 hits. Every returned sequence was globally aligned using BLOSUM62 with gap-open -10
      and extension -0.5. Scores and sequences for all 214 returned candidates are retained, with 10 detailed
      alignment files. The heuristic search does not establish genomic absence or unique locus identity.
    supported_by:
    - reference_id: file:THLAR/CYP71B1/CYP71B1-record-evidence.yaml
      supporting_text: 'target_sequence_count: 26379'
    - reference_id: file:THLAR/CYP71B1/CYP71B1-record-evidence.yaml
      supporting_text: 'candidate_count: 214'
  - type: SEQUENCE_COMPARISON
    description: 'A0AAU9RUE5: 496 identities across 496 global-alignment columns (100.0% identity including
      gaps), 0 substitutions and 0 gap columns. Query coverage is 100.0%; target coverage is 100.0%. Sequence
      similarity is interpreted in the manual rationale. Identity over paired residues is 100.0000% (496/496);
      gap columns are excluded from this denominator.'
    supported_by:
    - reference_id: file:THLAR/CYP71B1/CYP71B1-record-evidence.yaml
      supporting_text: |-
        query_length: 496
          target_length: 496
          alignment_columns: 496
          identities: 496
          mismatches: 0
          gap_columns: 0
          identity_percent: 100.0
          query_coverage_percent: 100.0
          target_coverage_percent: 100.0
  - type: PROTEOME_MEMBERSHIP
    description: The primary accession is outside every searched exact-taxon reference proteome. Current
      UniProt records place A0AAU9RUE5 in UP000836841 and give it the same taxon as the primary.
    supported_by:
    - reference_id: file:THLAR/CYP71B1/CYP71B1-record-evidence.yaml
      supporting_text: 'primary_in_any_reference_proteome: false'
    - reference_id: file:THLAR/CYP71B1/CYP71B1-record-evidence.yaml
      supporting_text: 'alternative_in_reference_proteome: true'
    - reference_id: file:THLAR/CYP71B1/CYP71B1-record-evidence.yaml
      supporting_text: 'same_taxon: true'
  - type: RECORD_HISTORY
    description: 'Sampled UniSave observations: 26-NOV-2014, entry version 68.: no Proteomes cross-reference;
      07-OCT-2020, entry version 77.: no Proteomes cross-reference; 27-NOV-2024, entry version 86.: no
      Proteomes cross-reference. These dated observations do not establish uninterrupted membership/absence,
      the exact change date, or UniProt''s motivation.'
    supported_by:
    - reference_id: file:THLAR/CYP71B1/CYP71B1-record-evidence.yaml
      supporting_text: |-
        entry_date: 26-NOV-2014, entry version 68.
          proteomes: []
    - reference_id: file:THLAR/CYP71B1/CYP71B1-record-evidence.yaml
      supporting_text: |-
        entry_date: 07-OCT-2020, entry version 77.
          proteomes: []
    - reference_id: file:THLAR/CYP71B1/CYP71B1-record-evidence.yaml
      supporting_text: |-
        entry_date: 27-NOV-2024, entry version 86.
          proteomes: []
existing_annotations:
  - term:
      id: GO:0004497
      label: monooxygenase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    qualifier: enables
    review:
      summary: Well-supported family-level inference. The protein has canonical
        cytochrome P450 domain architecture (Pfam PF00067), and plant P450s are
        heme-thiolate monooxygenases. The specific substrate and reaction are unknown,
        but monooxygenase activity is a sound conservative annotation.
      action: ACCEPT
      supported_by:
        - reference_id: file:THLAR/CYP71B1/CYP71B1-deep-research-falcon.md
          supporting_text: Plant cytochrome P450s are heme-thiolate monooxygenases that
            catalyze oxygenation reactions
  - term:
      id: GO:0005506
      label: iron ion binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    qualifier: enables
    review:
      summary: Correct. The P450 catalytic center binds an iron-containing heme; UniProt
        annotates an axial heme iron-binding residue at position 436. Iron ion binding
        is appropriate, captured more specifically by the heme binding annotation.
      action: ACCEPT
      supported_by:
        - reference_id: file:THLAR/CYP71B1/CYP71B1-deep-research-falcon.md
          supporting_text: a conserved cysteine coordinates the heme iron in the P450
            catalytic center
  - term:
      id: GO:0016705
      label: oxidoreductase activity, acting on paired donors, with incorporation or
        reduction of molecular oxygen
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    qualifier: enables
    review:
      summary: Correct and standard for a cytochrome P450 monooxygenase, which uses
        molecular oxygen with NADPH as the paired electron donor. Conservative
        family-level inference.
      action: ACCEPT
      supported_by:
        - reference_id: file:THLAR/CYP71B1/CYP71B1-deep-research-falcon.md
          supporting_text: RH + O2 + NADPH + H+ -> ROH + H2O + NADP+
  - term:
      id: GO:0020037
      label: heme binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    qualifier: enables
    review:
      summary: Correct. Cytochrome P450s are heme-thiolate proteins; UniProt annotates
        the axial heme iron-binding residue (position 436). This is the most specific
        cofactor annotation and underpins the monooxygenase activity.
      action: ACCEPT
      supported_by:
        - reference_id: file:THLAR/CYP71B1/CYP71B1-deep-research-falcon.md
          supporting_text: P450s share a conserved catalytic center in which a conserved
            cysteine coordinates the heme iron
core_functions:
  - description: CYP71B1 is a heme-thiolate cytochrome P450 monooxygenase predicted to
      catalyze NADPH/O2-dependent oxidation of an organic substrate. The physiological
      substrate, reaction, and pathway are unknown; CYP71-clan membership suggests a
      role in specialized (defense) metabolism, but this is not established for the
      pennycress protein.
    molecular_function:
      id: GO:0004497
      label: monooxygenase activity
    supported_by:
      - reference_id: PMID:8066138
        supporting_text: Cloning and sequencing of a full-length cDNA from Thlaspi
          arvense L. that encodes a cytochrome P-450
      - reference_id: file:THLAR/CYP71B1/CYP71B1-deep-research-falcon.md
        supporting_text: heme-thiolate monooxygenase; CYP71 clan enriched in plant
          specialized metabolism; substrate of pennycress CYP71B1 not determined
references:
  - id: file:THLAR/CYP71B1/CYP71B1-record-evidence.yaml
    title: Compact archived record and sequence evidence for P49264
  - id: GO_REF:0000002
    title: Gene Ontology annotation through association of InterPro records with GO
      terms
    findings: []
  - id: PMID:8066138
    title: Cloning and sequencing of a full-length cDNA from Thlaspi arvense L. that
      encodes a cytochrome P-450.
    findings:
      - statement: Reports the full-length cDNA of Thlaspi arvense CYP71B1 (a cytochrome
          P450); a sequence report with no functional characterization.
        reference_section_type: ABSTRACT
    reference_review:
      relevance: MEDIUM
      correctness: VERIFIED
      review_notes: PubMed-verified. The sole primary reference for this gene; it
        establishes existence/sequence only, not function. Abstract-only in cache.
  - id: file:THLAR/CYP71B1/CYP71B1-deep-research-falcon.md
    title: Falcon/Edison deep research report for CYP71B1, Thlaspi arvense
    findings:
      - statement: Concludes pennycress CYP71B1 is functionally uncharacterized; only a
          heme-thiolate plant P450 monooxygenase classification can be inferred, with
          CYP71-clan members commonly acting in specialized/defense metabolism (e.g.
          Arabidopsis camalexin pathway). Flags symbol ambiguity with Arabidopsis
          CYP71B1 (At1g13080).
        reference_section_type: OTHER
suggested_questions:
  - question: What substrate(s) and reaction does Thlaspi arvense CYP71B1 catalyze, and
      in which pathway (e.g. glucosinolate, indole/camalexin-type, or other specialized
      metabolism) does it act?
  - question: Is CYP71B1 anchored to the endoplasmic reticulum membrane, as is typical
      for CYP71-clan plant P450s?
suggested_experiments:
  - description: Heterologously express CYP71B1 (e.g. in yeast or N. benthamiana
      microsomes with a plant cytochrome P450 reductase) and screen candidate substrates
      from Brassicaceae specialized metabolism (indole/tryptophan-derived intermediates,
      glucosinolate precursors) by LC-MS to identify the catalyzed reaction.
  - description: Determine subcellular localization with a fluorescent-protein fusion and
      test for an N-terminal ER membrane anchor.
