ProtNLM2 External predictions
View prediction review YAML · AT4G38370-protnlm-predictions-review.yaml · Review status: COMPLETE
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
Review score: 2 = concordant with evidence; 1 = uncertain; 0 = discordant with evidence. This is an assessment score, not a model probability.
UNC — Uncertain Review score: 1/2
Prediction method: ProtNLM2 · Version: UniProt API snapshot 2026-09-10 · file:ARATH/AT4G38370/AT4G38370-protnlm-source.json
Review rationale: 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.
Supporting Evidence:
- file:ARATH/AT4G38370/AT4G38370-bioinformatics/RESULTS.md: "| Active site: Tele-phosphohistidine intermediate | 11–11 | 1 / 1 | 1 |"
- PMID:19015259: "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."
- file:ARATH/AT4G38370/AT4G38370-prediction-donor.json: ""value": "Fructose-2,6-bisphosphatase TIGAR B""