PLI (score 0): the paragraph assigns dolichyl-phosphate mannose synthesis to an ALG5-family protein.
ProtNLM A0A5F5PM72, frozen API snapshot 2026-09-08.
Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex
| Claim | Assessment | Evidence |
|---|---|---|
| Transfers mannose from GDP-mannose to dolichol phosphate | PLI | Human ALG5 is the UDP-glucose-dependent dolichyl-phosphate glucosyltransferase; exact horse sequence belongs to this family. |
| Catalytic subunit of DPM synthase | PLI | This assigns a different dolichol-sugar synthase identity; no DPM-complex membership or GDP-mannose chemistry is supported for ALG5. |
| Product supplies N-glycosylation, GPI anchoring and O-mannosylation | Mixed | N-glycosylation is relevant to ALG5 through Dol-P-Glc, but the predicted Dol-P-Man product and downstream GPI/O-mannosylation routes do not follow. |
Human PMID:10359825(https://pubmed.ncbi.nlm.nih.gov/10359825/), DOI 10.1073/pnas.96.12.6982, functionally complements the yeast alg5 defect with human ALG5. The curated human UniProt Q9Y673 reaction uses UDP-glucose and its experimentally grounded description states “glucose donor substrate used sequentially by ALG6, ALG8 and ALG10”. Those observations establish the relevant substrate/pathway distinction.
The horse alignment preserves the membrane anchor and 94.6% identity across 294 paired residues, but reveals an internal 30 aa deletion (human 95–124). Therefore, an active horse glucosyltransferase is not asserted as experimentally established, and the main horse activity annotation remains uncertain. This uncertainty does not supply positive evidence for conversion to GDP-mannose specificity or DPM-complex membership. The exact training donor is unknown; PARALOG_OVERANNOTATION describes the inappropriate transfer between distinct dolichol-sugar synthase functions, not a recovered model provenance chain.