ERG8

UniProt ID: A0A1D8PLH0
Organism: Candida albicans SC5314
Review Status: COMPLETE
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Gene Description

Candida albicans ERG8 encodes a GHMP-family phosphomevalonate kinase that phosphorylates 5-phosphomevalonate with ATP to produce 5-diphosphomevalonate in the cytoplasmic mevalonate pathway. The reaction supplies isopentenyl diphosphate for farnesyl diphosphate production and downstream ergosterol biosynthesis, using the fungal/plant ERG8-type PMK fold rather than the unrelated animal PMVK fold.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004631 phosphomevalonate kinase activity
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from the fungal/plant GHMP phosphomevalonate kinase node PTN001274235. The node is sound for fungal PTHR31814 members, and C. albicans ERG8 belongs to PTHR31814:SF2 and catalyzes the ATP-dependent conversion of 5-phosphomevalonate to 5-diphosphomevalonate.
Supporting Evidence:
PMID:11243736
Phosphomevalonate kinase (PMK; EC 2.7.4.2) catalyzes the phosphorylation of 5-phosphomevalonate into 5-diphosphomevalonate
file:CANAL/ERG8/ERG8-uniprot.txt
PANTHER; PTHR31814:SF2; PHOSPHOMEVALONATE KINASE; 1
GO:0004631 phosphomevalonate kinase activity
IEA
GO_REF:0000120
ACCEPT
Summary: Combined UniProt IEA from the yeast ERG8 ortholog, InterPro ERG8 family, RHEA:16341, and EC:2.7.4.2. These all point to the same accepted phosphomevalonate kinase reaction.
Supporting Evidence:
file:CANAL/ERG8/ERG8-uniprot.txt
Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate +
file:CANAL/ERG8/ERG8-uniprot.txt
InterPro; IPR016005; Erg8.
GO:0004631 phosphomevalonate kinase activity
ISS
GO_REF:0000024
ACCEPT
Summary: Manual similarity transfer from S. cerevisiae ERG8 (P24521). The transfer is correct because Candida ERG8 is in the same fungal GHMP PMK subfamily and retains the curated phosphomevalonate kinase reaction.
Supporting Evidence:
file:CANAL/ERG8/ERG8-uniprot.txt
Belongs to the GHMP kinase family. Mevalonate kinase subfamily.
file:CANAL/ERG8/ERG8-uniprot.txt
Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate +
GO:0005524 ATP binding
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: InterPro2GO transfer from the GHMP kinase N-terminal ATP-binding domain. ATP is the phosphoryl donor of the accepted PMK reaction, so nucleotide binding is correct but secondary to phosphomevalonate kinase activity.
Reason: ATP binding is a substrate-binding component of the core kinase reaction.
Supporting Evidence:
file:CANAL/ERG8/ERG8-uniprot.txt
Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate +
GO:0005575 cellular_component
ND
GO_REF:0000015
ACCEPT
Summary: CGD ND root cellular-component placeholder; it records absence of direct C. albicans component evidence rather than a biological localization.
Reason: ACCEPT under the ND acceptance rule (projects/NO_DATA.md). The evidence this review cites for the cellular component is inferred (from orthologs, family membership or sequence features) or comes from other species; none of it is literature on this gene product in this species. This was judged from the review's own content during the NO_DATA re-action pass, not from a new literature search. Earlier action: REMOVE. Re-checked 2026-10-31: the paper cited in core_functions (PMID:11243736) is a comparative study of phosphomevalonate kinases, not a C. albicans localization. The gene's notes record a literature search that found no direct C. albicans ERG8 paper, so no study localizes this protein.
Supporting Evidence:
file:CANAL/ERG8/ERG8-notes.md
Newer-paper searches for direct C. albicans ERG8 literature did not find a
GO:0005737 cytoplasm
IEA
GO_REF:0000120
MODIFY
Summary: UniProt SubCell transfer to cytoplasm. This coarse location is consistent with the soluble cytosolic fungal mevalonate-pathway enzyme, and GO:0005829 is the better specific descendant.
Reason: Cytoplasm is directionally correct but general for a soluble ERG8-type phosphomevalonate kinase; cytosol is the supported descendant, matching the sibling yeast and S. pombe ERG8 reviews and the absence of any secretory or organelle targeting signal in the Candida protein.
Proposed replacements: cytosol
Supporting Evidence:
file:CANAL/ERG8/ERG8-uniprot.txt
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
GO:0005777 peroxisome
IBA
GO_REF:0000033
REMOVE
Summary: IBA to peroxisome derives from Eukaryota-level PAINT node PTN000781523, seeded only by Arabidopsis PMK. The family review judged this placement in need of pruning for fungal ERG8 members.
Reason: PTN000781523 places a single Arabidopsis-seeded peroxisomal PMK assertion above the plant-fungal split. Candida ERG8 ends in IGL rather than a canonical PTS1 motif and is expected to execute its mevalonate pathway step in the cytosol.
Propagation Review
Root cause: PROPAGATION BAD
Failure modes: COMPARTMENT OR COMPLEX MISMATCH LINEAGE OR TAXON MISMATCH
Sources checked:
PANTHER:PTN000781523 Β· PTN000781523 SUPPORTS SOURCE BUT NOT TARGET
PTN000781523 is a Eukaryota-level node seeded only by Arabidopsis AT1G31910 and over-propagates a plant peroxisomal PMK localization to fungal cytosolic ERG8 proteins.
Supporting Evidence:
file:interpro/panther/PTHR31814/PTHR31814-review.yaml
Peroxisome is removed by both the S. cerevisiae ERG8 and S. pombe erg8 reviews: the fungal mevalonate pathway enzymes are cytosolic.
file:interpro/panther/PTHR31814/PTHR31814-paint.tsv
PTHR31814 PTN000781523 GO:0005777 C IBD false
file:CANAL/ERG8/ERG8-uniprot.txt
VLEEKPEDYI GL
GO:0006696 ergosterol biosynthetic process
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from fungal PAINT node PTN001274236, seeded by yeast ERG8. The annotation is correct: C. albicans ERG8 catalyzes an early mevalonate-pathway step that supplies isopentenyl diphosphate for farnesyl diphosphate and ergosterol biosynthesis.
Supporting Evidence:
file:interpro/panther/PTHR31814/PTHR31814-paint.tsv
PTHR31814 PTN001274236 GO:0006696 P IBD false
file:CANAL/ERG8/ERG8-uniprot.txt
Phosphomevalonate kinase; part of the second module of ergosterol biosynthesis pathway
GO:0006696 ergosterol biosynthetic process
IEA
GO_REF:0000107
ACCEPT
Summary: EnsemblFungi IEA transfer from the experimentally annotated S. cerevisiae ERG8 ortholog. The process is correct because phosphomevalonate kinase feeds the isopentenyl diphosphate and farnesyl diphosphate pools used for ergosterol production.
Supporting Evidence:
file:CANAL/ERG8/ERG8-uniprot.txt
Phosphomevalonate kinase; part of the second module of ergosterol biosynthesis pathway
GO:0019287 isopentenyl diphosphate biosynthetic process, mevalonate pathway
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from PTN001274235, the fungal/plant GHMP phosphomevalonate kinase node. ERG8 carries out step 2 of the three-step conversion from mevalonate to isopentenyl diphosphate.
Supporting Evidence:
file:interpro/panther/PTHR31814/PTHR31814-paint.tsv
PTHR31814 PTN001274235 GO:0019287 P IBD false
file:CANAL/ERG8/ERG8-uniprot.txt
via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
GO:0019287 isopentenyl diphosphate biosynthetic process, mevalonate pathway
IEA
GO_REF:0000120
ACCEPT
Summary: UniPathway/orthology IEA to IPP biosynthesis via the mevalonate pathway. The assignment is the direct pathway context of the accepted phosphomevalonate kinase reaction.
Supporting Evidence:
file:CANAL/ERG8/ERG8-uniprot.txt
via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:

Core Functions

Phosphomevalonate kinase: ATP-dependent phosphorylation of 5-phosphomevalonate to 5-diphosphomevalonate in the cytoplasmic mevalonate pathway, feeding isopentenyl diphosphate and ergosterol biosynthesis.

Supporting Evidence:
  • PMID:11243736
    Phosphomevalonate kinase (PMK; EC 2.7.4.2) catalyzes the phosphorylation of 5-phosphomevalonate into 5-diphosphomevalonate
  • file:CANAL/ERG8/ERG8-uniprot.txt
    Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate +
  • file:CANAL/ERG8/ERG8-uniprot.txt
    via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
  • file:CANAL/ERG8/ERG8-uniprot.txt
    SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.

References

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πŸ“š Additional Documentation

Notes

(ERG8-notes.md)

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