The fold-level name is reasonable. The only emitted GO term is generic catalytic activity; the TIGAR structural donor does not establish a particular phosphatase substrate or glycolytic role for AT4G38370.
Q0WW53 maps to AT4G38370 and PTHR47821:SF2. Its 225-residue sequence contains an N-terminal RHG motif. The emitted donor Q7ZVE3 is zebrafish TIGAR B. Exploratory global alignment preserves the donor catalytic histidine and proton-donor/acceptor residues, but is highly gapped and has low overall identity; the apparent mismatch at a transition-state contact is not reliable evidence of catalytic loss. No TIGAR-specific substrate assignment follows from this alignment.
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.
The complete emitted record is preserved in AT4G38370-protnlm-source.json. Assessments below address the selected protein product; evidence on longer products is identified explicitly.
Phosphoglycerate mutase-like protein
CNN (CS 2). “Phosphoglycerate mutase-like protein” is a qualified fold-level description consistent with the histidine-phosphatase domain assignment. The “-like” wording does not assert phosphoglycerate turnover or a glycolytic pathway role.
All 1 emitted GO claims are individually assessed in AT4G38370-protnlm-predictions-review.yaml.
PTHR47821:SF2 places the target among phosphoglycerate-mutase-family proteins. The histidine-phosphatase fold encompasses different phosphosugar reactions, so a common RHG catalytic motif cannot identify a substrate. It also does not establish the specialized secreted phytase architecture of another histidine-phosphatase branch.
No target-specific biochemical study was located under AT4G38370 or Q0WW53. The TIGAR primary report is abstract-only and explicitly establishes donor enzymology. The genuine Falcon synthesis supplies family hypotheses but does not establish a target reaction. The sequence comparison is exploratory: sparse global alignments are not used to call residue loss or to identify an evolved pseudoenzyme.
Exact sequence mapping: AT4G38370-bioinformatics/RESULTS.md. Global alignments can place nonhomologous alternative tails opposite gaps or distant residues; only conserved segments and explicitly retained feature intervals support functional transfer.