gcv3 (SPBP19A11.01; UniProt Q9HDV9) encodes the mitochondrial H protein of the glycine cleavage system. It carries a covalently attached lipoyl cofactor that accepts the methylamine group from glycine decarboxylation by the P protein (gcv2), delivers it to the T protein (gcv1) for transfer to tetrahydrofolate, and is reoxidised by dihydrolipoyl dehydrogenase (dld1). In S. cerevisiae the orthologous GCV3 is also needed to lipoylate the E2 subunits of pyruvate and 2-oxoglutarate dehydrogenases; whether S. pombe gcv3 has that second role is untested. Mitochondrial localisation comes from a genome-wide screen; function is assigned by orthology.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005739 mitochondrion | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: ORFeome YFP screen placed gcv3 in mitochondria. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein. file:SCHPO/gcv3/gcv3-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}. |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inference; agrees with the HDA. Supporting Evidence: file:SCHPO/gcv3/gcv3-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}. |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping, based on the ORFeome screen. Supporting Evidence: file:SCHPO/gcv3/gcv3-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}. |
| GO:0005759 mitochondrial matrix | IC GO_REF:0000036 | ACCEPT | Summary: Curator inference from the glycine cleavage process (mitochondrial matrix). Supporting Evidence: file:SCHPO/gcv3/gcv3-uniprot.txt FUNCTION: The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine. |
| GO:0005960 glycine cleavage complex | IBA GO_REF:0000033 | ACCEPT | Summary: The lipoylated H protein is the central carrier subunit of the glycine cleavage system. Supporting Evidence: file:SCHPO/gcv3/gcv3-uniprot.txt SUBUNIT: Component of the glycine decarboxylase complex (GDC), which is composed of four proteins: P, T, L and H. |
| GO:0005960 glycine cleavage complex | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro GcvH mapping; agrees with the IBA. Supporting Evidence: file:SCHPO/gcv3/gcv3-uniprot.txt SUBUNIT: Component of the glycine decarboxylase complex (GDC), which is composed of four proteins: P, T, L and H. |
| GO:0019464 glycine decarboxylation via glycine cleavage system | IBA GO_REF:0000033 | ACCEPT | Summary: Core process: the H protein carries the aminomethyl intermediate between the P and T proteins and is reoxidised by L protein. Supporting Evidence: file:SCHPO/gcv3/gcv3-uniprot.txt The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity). |
| GO:0019464 glycine decarboxylation via glycine cleavage system | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro mapping; agrees with the IBA. Supporting Evidence: file:SCHPO/gcv3/gcv3-uniprot.txt The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity). |
| GO:0140104 molecular carrier activity | NAS GO_REF:0000051 | ACCEPT | Summary: The H protein is a non-catalytic carrier: its covalently bound lipoyl arm carries the methylamine intermediate between the P and T proteins and is then reoxidised by the L protein. Molecular carrier activity is the appropriate MF. In S. cerevisiae, GCV3 also supplies lipoyl groups for lipoylation of other 2-oxoacid dehydrogenase E2 subunits; that role is not tested in S. pombe. Supporting Evidence: file:SCHPO/gcv3/gcv3-uniprot.txt The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity). file:SCHPO/gcv3/gcv3-uniprot.txt Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250}; |
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Download this section (compressed HTML)Q: Is S. pombe gcv3 required for lipoylation of the pyruvate and 2-oxoglutarate dehydrogenase E2 subunits, as S. cerevisiae GCV3 is?
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