mct1 (SPAC11G7.05c; UniProt O13698) encodes mitochondrial malonyl-CoA:ACP transacylase (EC 2.3.1.39), which loads malonyl groups onto mitochondrial ACP, the committed step of mitochondrial type II fatty acid synthesis (mtFAS). Function is assigned by orthology to S. cerevisiae MCT1; it is mitochondrial in a genome-wide screen.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004314 [acyl-carrier-protein] S-malonyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Malonyl-CoA:ACP transacylase activity (PAINT/EC). Reason: No S. pombe biochemistry. Support is the UniProt catalytic-activity statement (EC 2.3.1.39) and FabD-family membership (Pfam Acyl_transf_1 acyltransferase domain), the family of malonyl-CoA:ACP transacylases; the PAINT donors include E. coli FabD and S. cerevisiae MCT1. Function is therefore by orthology. Supporting Evidence: file:SCHPO/mct1/mct1-uniprot.txt Reaction=holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA; file:SCHPO/mct1/mct1-uniprot.txt SIMILARITY: Belongs to the FabD family. file:SCHPO/mct1/mct1-uniprot.txt PF00698; Acyl_transf_1 |
| GO:0004314 [acyl-carrier-protein] S-malonyltransferase activity | IEA GO_REF:0000003 | ACCEPT | Summary: Malonyl-CoA:ACP transacylase activity (PAINT/EC). Reason: No S. pombe biochemistry. Support is the UniProt catalytic-activity statement (EC 2.3.1.39) and FabD-family membership (Pfam Acyl_transf_1 acyltransferase domain), the family of malonyl-CoA:ACP transacylases; the PAINT donors include E. coli FabD and S. cerevisiae MCT1. Function is therefore by orthology. Supporting Evidence: file:SCHPO/mct1/mct1-uniprot.txt Reaction=holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA; file:SCHPO/mct1/mct1-uniprot.txt SIMILARITY: Belongs to the FabD family. file:SCHPO/mct1/mct1-uniprot.txt PF00698; Acyl_transf_1 |
| GO:0005739 mitochondrion | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: ORFeome YFP screen: mitochondrion. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of mitochondrial location. Reason: Mitochondrial location is experimental for this protein: UniProt cites the S. pombe ORFeome localisation screen (PubMed:16823372, also the source of the separate HDA row), and the record has a predicted mitochondrial transit peptide (FT TRANSIT, ECO:0000255). The organelle term is kept as informative. Supporting Evidence: file:SCHPO/mct1/mct1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372} file:SCHPO/mct1/mct1-uniprot.txt FUNCTION: Involved in biosynthesis of fatty acids in mitochondria. |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt/ARBA location mapping; consistent. Reason: Mitochondrial location is experimental for this protein: UniProt cites the S. pombe ORFeome localisation screen (PubMed:16823372, also the source of the separate HDA row), and the record has a predicted mitochondrial transit peptide (FT TRANSIT, ECO:0000255). The organelle term is kept as informative. Supporting Evidence: file:SCHPO/mct1/mct1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372} file:SCHPO/mct1/mct1-uniprot.txt FUNCTION: Involved in biosynthesis of fatty acids in mitochondria. |
| GO:0006633 fatty acid biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: Mitochondrial type II fatty acid synthesis. Reason: The UniProt function is by similarity (ECO:0000250) to characterised mitochondrial malonyl transacylases (S. cerevisiae MCT1, human MCAT); FabD-family membership supports loading malonyl groups onto ACP for type II fatty acid synthesis. Evidence is by orthology, not from S. pombe experiments. Supporting Evidence: file:SCHPO/mct1/mct1-uniprot.txt FUNCTION: Involved in biosynthesis of fatty acids in mitochondria. file:SCHPO/mct1/mct1-uniprot.txt PATHWAY: Lipid metabolism; fatty acid biosynthesis. file:SCHPO/mct1/mct1-uniprot.txt SIMILARITY: Belongs to the FabD family. |
| GO:0006633 fatty acid biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: Mitochondrial type II fatty acid synthesis. Reason: The UniProt function is by similarity (ECO:0000250) to characterised mitochondrial malonyl transacylases (S. cerevisiae MCT1, human MCAT); FabD-family membership supports loading malonyl groups onto ACP for type II fatty acid synthesis. Evidence is by orthology, not from S. pombe experiments. Supporting Evidence: file:SCHPO/mct1/mct1-uniprot.txt FUNCTION: Involved in biosynthesis of fatty acids in mitochondria. file:SCHPO/mct1/mct1-uniprot.txt PATHWAY: Lipid metabolism; fatty acid biosynthesis. file:SCHPO/mct1/mct1-uniprot.txt SIMILARITY: Belongs to the FabD family. |
| GO:0016740 transferase activity | IEA GO_REF:0000002 | MODIFY | Summary: Generic InterPro-derived parent of the specific activity, which is already annotated. Reason: Too general. By family membership (FabD family; Pfam Acyl_transf_1; PANTHER mitochondrial malonyl-CoA-ACP transacylase subfamily) and the curated EC 2.3.1.39 reaction, the transfer mct1 performs is malonyl from CoA to holo-ACP, i.e. [acyl-carrier-protein] S-malonyltransferase activity, which the gene already carries. No S. pombe enzyme assay is cached. Proposed replacements: [acyl-carrier-protein] S-malonyltransferase activity Supporting Evidence: file:SCHPO/mct1/mct1-uniprot.txt Reaction=holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA; file:SCHPO/mct1/mct1-uniprot.txt SIMILARITY: Belongs to the FabD family. file:SCHPO/mct1/mct1-uniprot.txt PTHR42681:SF1; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL |
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