id: Q0WW53
gene_symbol: AT4G38370
taxon:
  id: NCBITaxon:3702
  label: Arabidopsis thaliana
status: COMPLETE
description: The histidine-phosphatase fold and retained catalytic motif make enzymatic activity plausible,
  but no target biochemistry or securely resolved substrate-specific functional transfer establishes it.
source_documents:
- genes/ARATH/AT4G38370/AT4G38370-protnlm-source.json
- genes/ARATH/AT4G38370/AT4G38370-notes.md
references:
- id: PMID:19015259
  title: Structural and biochemical studies of TIGAR (TP53-induced glycolysis and apoptosis regulator).
  findings:
  - statement: Direct TIGAR biochemistry establishes donor activity and substrate discrimination, not
      the substrate of the Arabidopsis protein.
    supporting_text: 'The

      recombinant human and zebra fish enzymes hydrolyze fructose-2,6-bisphosphate as

      well as fructose-1,6-bisphosphate but not fructose 6-phosphate in vitro.'
  full_text_unavailable: true
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Primary report checked against the cached abstract/full text; the evidence scope is
      stated in the finding.
- id: file:ARATH/AT4G38370/AT4G38370-bioinformatics/RESULTS.md
  title: Exploratory exact-input alignment to the experimentally characterized TIGAR donor
- id: file:ARATH/AT4G38370/AT4G38370-prediction-donor.json
  title: UniProt identification of the structure-matched TIGAR donor
- id: file:ARATH/AT4G38370/AT4G38370-protnlm-source.json
  title: Frozen exact-input ProtNLM output and UniProt sequence for Q0WW53
predictions:
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-10
  source_reference_id: file:ARATH/AT4G38370/AT4G38370-protnlm-source.json
  predicted_term:
    id: GO:0003824
    label: catalytic activity
  predicted_term_type: GO_MF
  review:
    assessment: UNC
    confidence_score: 1
    summary: The intact histidine-phosphatase-like sequence and retained catalytic histidine support plausible
      enzymatic activity. However, the structurally similar TIGAR donor is a different substrate-specific
      branch, and the low-identity alignment cannot establish a complete functional active site or exclude
      a noncatalytic member. No assay or sufficiently specific evolutionary evidence resolves catalysis
      of the target. The prediction does not itself claim TIGAR or phosphoglycerate-mutase chemistry.
    supported_by:
    - reference_id: file:ARATH/AT4G38370/AT4G38370-bioinformatics/RESULTS.md
      supporting_text: '| Active site: Tele-phosphohistidine intermediate | 11–11 | 1 / 1 | 1 |'
    - reference_id: PMID:19015259
      supporting_text: 'The

        recombinant human and zebra fish enzymes hydrolyze fructose-2,6-bisphosphate as

        well as fructose-1,6-bisphosphate but not fructose 6-phosphate in vitro.'
    - reference_id: file:ARATH/AT4G38370/AT4G38370-prediction-donor.json
      supporting_text: '"value": "Fructose-2,6-bisphosphatase TIGAR B"'