Function
Oxidizes a glycolytic intermediate to the first committed phosphorylated-serine precursor.
A reusable three-reaction pathway that converts the glycolytic intermediate 3-phospho-D-glycerate to L-serine through 3-phosphooxypyruvate and O-phospho-L-serine. The module represents the conserved SerA, SerC, and SerB reaction roles independently of their genomic arrangement. Additional activities of individual enzymes, including 2-hydroxyglutarate oxidation by some SerA proteins and vitamin B6 precursor transamination by some SerC proteins, are outside this pathway boundary.
All recommended fields populated.
✓ present
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
3 complete review(s) · 1 with deep research · 3 missing review · 2 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| Escherichia coli SerB P0AGB0 | ✗ | — | — |
| Escherichia coli SerC P23721 | ✗ | — | — |
| Haemophilus influenzae SerA P43885 | ✗ | — | — |
| serA Q88CM5 | ✓ | ✓ | ✗ |
| serB Q88DB8 | ✓ | ✓ | ✗ |
| serC Q88M07 | ✓ | ✓ | ✓ |
Exact UniProt exemplars delimit the three reaction roles without restricting the module taxonomically. No cellular location or molecular function is repeated at module level. SerC can also catalyze phosphohydroxythreonine transamination in DXP-dependent vitamin B6 biosynthesis, but that separate reaction is not a fourth part of this module. Some bacterial SerA proteins use an ACT domain for L-serine feedback, but effector sensitivity is a lineage- and sequence-dependent regulatory property rather than an additional pathway part. No ancestral PTN node is asserted without verified PAINT IBD evidence.
Oxidizes a glycolytic intermediate to the first committed phosphorylated-serine precursor.
Transfers an amino group from glutamate to 3-phosphooxypyruvate.
Hydrolyzes O-phospho-L-serine to free L-serine.