# AT4G38370 re-review: entry identity and catalytic-residue mapping

Generated by `catalytic_residues_rereview.py` (run with `uv run --script`). Sequences and curated features fetched live from UniProt REST.

## Entry identity (same locus At4g38370)

- F4JTN4: length 225; differences vs Q0WW53: none (identical)
- Q8LCU4: length 225; differences vs Q0WW53: ['K90E']

## Motif scan on Q0WW53

- RHG (branch-1 nucleophile motif): [(16, 'RHG')]
- E proton donor context (xRERxxG): [(107, 'LRERYFG')]
- C-terminal HG: [(172, 'SHGD')]

## Mapping of curated sites from Swiss-Prot branch-1 enzymes (local BLOSUM62 alignment)

### P18669 human PGAM1 (2,3-bisphosphoglycerate-dependent phosphoglycerate mutase)
Aligned pairs 149, identical 53 (35.6%).

| Feature | Ligand | Ref residue | Q0WW53 residue |
|---|---|---|---|
| Active site: Tele-phosphohistidine intermediate |  | H11 | H17 |
| Active site: Proton donor/acceptor |  | E89 | E109 |
| Binding site:  | substrate | R62 | H83 |
| Binding site:  | substrate | K100 | unaligned |
| Site: Transition state stabilizer |  | H186 | H173 |

### P62707 E. coli GpmA (2,3-bisphosphoglycerate-dependent phosphoglycerate mutase)
Aligned pairs 152, identical 47 (30.9%).

| Feature | Ligand | Ref residue | Q0WW53 residue |
|---|---|---|---|
| Active site: Tele-phosphohistidine intermediate |  | H11 | H17 |
| Active site: Proton donor/acceptor |  | E89 | E109 |
| Binding site:  | substrate | R62 | R86 |
| Binding site:  | substrate | K100 | unaligned |
| Site: Transition state stabilizer |  | H184 | H173 |

### Q9NQ88 human TIGAR (fructose-2,6-bisphosphatase)
Aligned pairs 156, identical 54 (34.6%).

| Feature | Ligand | Ref residue | Q0WW53 residue |
|---|---|---|---|
| Active site: Tele-phosphohistidine intermediate |  | H11 | H17 |
| Active site: Proton donor/acceptor |  | E89 | E109 |
| Site: Transition state stabilizer |  | H198 | unaligned |

Fold-level comparators only: none of these references is in PANTHER PTHR47821, so the mapping tests retention of the shared histidine-phosphatase catalytic apparatus, not substrate identity.