ACC1 (FAS3/MTR7, YNR016C) encodes the cytosolic acetyl-CoA carboxylase of S. cerevisiae, a ~250 kDa biotin-dependent enzyme that carries biotin carboxylase, biotin carboxyl carrier and carboxyltransferase domains on a single polypeptide and functions as a homodimer. It catalyses the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA (EC 6.4.1.2), the committed and rate-limiting step of cytosolic de novo fatty acid synthesis by the FAS1/FAS2 fatty acid synthase, and also supplies malonyl-CoA for ER-bound very-long-chain fatty acid elongation. Acc1 is essential even with fatty acid supplementation, reflecting its requirement for very-long-chain fatty acids needed for nuclear envelope integrity. It is soluble in the cytosol and peripherally associated with the cytosolic face of the (nuclear) ER membrane. ACC1 expression is co-regulated with phospholipid synthesis by Ino2/Ino4/Opi1, and the enzyme is inhibited by phosphorylation and by soraphen A. Its paralog HFA1 encodes the mitochondrial isoform. Because Acc1 consumes the nucleocytosolic acetyl-CoA pool, its activity limits global histone acetylation and so links fatty acid synthesis to chromatin regulation. Acc1 activity is also needed for the acylation and vacuolar membrane association of Vac8, and thus for normal vacuole morphology. ACC1 translation is controlled by an upstream ORF that raises Acc1 levels late in the cell cycle and adjusts them to nutrients.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003989 acetyl-CoA carboxylase activity | EXP PMID:12663926 Crystal structure of the carboxyltransferase domain of acety... | ACCEPT | Summary: EXP (Zhang et al. 2003): crystal structure and kinetics of the yeast Acc1 carboxyltransferase domain with CoA; UniProt cites this paper for the EC 6.4.1.2 reaction. Core MF of Acc1. Supporting Evidence: PMID:12663926 The active site is at the interface of a dimer file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + |
| GO:0003989 acetyl-CoA carboxylase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from the eukaryotic multidomain ACC node (PTN000429606; plant, mouse Acaca/Acacb and other ACCs). Acc1 is the canonical cytosolic member of this clade; core MF. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + PMID:8098706 Overexpression of the ACC1 gene from a high copy number plasmid resulted in overexpression of a 250-kDa biotin-enzyme and enzymatic activity of acetyl-CoA carboxylase |
| GO:0003989 acetyl-CoA carboxylase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA (GO_REF:0000120) via RHEA:11308 / EC 6.4.1.2 and ACC central-domain InterPro signatures. Correct for Acc1. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + |
| GO:0003989 acetyl-CoA carboxylase activity | IMP PMID:8098706 Acetyl-CoA carboxylase from yeast is an essential enzyme and... | ACCEPT | Summary: IMP (Hasslacher et al. 1993): ACC1 disruption halves ACC activity in heterozygous diploids and overexpression raises it, identifying ACC1 as the structural gene for yeast ACC. Core MF. Supporting Evidence: PMID:8098706 Overexpression of the ACC1 gene from a high copy number plasmid resulted in overexpression of a 250-kDa biotin-enzyme and enzymatic activity of acetyl-CoA carboxylase |
| GO:0003989 acetyl-CoA carboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-10 (fatty acid biosynthesis, initial steps) assigning Acc1 to acetyl-CoA + ATP + HCO3- -> malonyl-CoA (EC 6.4.1.2), the committed step of cytosolic de novo fatty acid synthesis. Correct. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + PMID:6103540 The mutant is deficient in de novo biosynthesis of long-chain fatty acids and specifically requires a saturated fatty acid of chain length 14-16 C atoms for growth |
| GO:0003989 acetyl-CoA carboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-5962 (superpathway of fatty acid biosynthesis, saturated and unsaturated) assigning Acc1 to acetyl-CoA + ATP + HCO3- -> malonyl-CoA (EC 6.4.1.2), the committed step of cytosolic de novo fatty acid synthesis. Correct. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + PMID:6103540 The mutant is deficient in de novo biosynthesis of long-chain fatty acids and specifically requires a saturated fatty acid of chain length 14-16 C atoms for growth |
| GO:0003989 acetyl-CoA carboxylase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-6336 (superpathway of fatty acid biosynthesis, saturated) assigning Acc1 to acetyl-CoA + ATP + HCO3- -> malonyl-CoA (EC 6.4.1.2), the committed step of cytosolic de novo fatty acid synthesis. Correct. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + PMID:6103540 The mutant is deficient in de novo biosynthesis of long-chain fatty acids and specifically requires a saturated fatty acid of chain length 14-16 C atoms for growth |
| GO:0004075 biotin carboxylase activity | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: IEA via RHEA:13501 / EC 6.3.4.14 (biotin carboxylase half-reaction). The BC domain of Acc1 carries out this partial reaction on its own BCCP domain; correct but a component of the overall ACC activity. Reason: Partial (domain) activity subsumed by acetyl-CoA carboxylase activity. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt Reaction=N(6)-biotinyl-L-lysyl-[protein] + hydrogencarbonate + ATP = PMID:6103540 the biotin carboxylase component enzyme exhibited less than 10% of wild-type specific activity |
| GO:0004075 biotin carboxylase activity | IMP PMID:6108218 Yeast mutants defective in acetyl-coenzyme A carboxylase and... | KEEP AS NON CORE | Summary: IMP (Mishina et al. 1980): acc1 mutant enzymes are deficient in the biotin carboxylase component activity, showing that Acc1 harbours this partial activity on the same polypeptide. Correct domain-level activity, subsumed by the overall ACC reaction. Reason: Partial (domain) activity subsumed by acetyl-CoA carboxylase activity. Supporting Evidence: PMID:6108218 These results suggest that acc1 is a cluster gene coding for a multifunctional protein harboring both acetyl-CoA carboxylase component enzyme activities on the same polypeptide chain PMID:6108218 both component enzymes, biotin carboxylase and transcarboxylase, were simultaneously affected in most mutants |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: IEA from ATP-grasp / CPS ATP-binding InterPro domains of the BC domain. ATP is a substrate of the carboxylation; correct but implied by the catalytic activity. Reason: Substrate-binding term implied by the catalytic activity. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: IEA from UniProt subcellular location (Cytoplasm). Correct; cytosol is the more precise location. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane; PMID:14761959 Whereas ACC1 is involved in cytoplasmic fatty acid synthesis |
| GO:0005739 mitochondrion | HDA PMID:14576278 The proteome of Saccharomyces cerevisiae mitochondria. | MARK AS OVER ANNOTATED | Summary: HDA from a mitochondrial proteomics survey (PMID:14576278). Acc1 lacks the mitochondrial targeting sequence that its paralog Hfa1 carries, and the mitochondrial ACC role is assigned to Hfa1; detection of this very abundant cytosolic/ER-associated enzyme in mitochondrial preparations most likely reflects contamination. Reason: High-throughput mitochondrial detection not supported by targeting or function; mitochondrial ACC is Hfa1. Supporting Evidence: PMID:14761959 Other than Acc1p, the N-terminal sequence of Hfa1p comprises a canonical mitochondrial targeting signal together with a matrix protease cleavage site PMID:14576278 The proteome of Saccharomyces cerevisiae mitochondria. |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | MARK AS OVER ANNOTATED | Summary: HDA from a mitochondrial proteomics survey (PMID:16823961). Acc1 lacks the mitochondrial targeting sequence that its paralog Hfa1 carries, and the mitochondrial ACC role is assigned to Hfa1; detection of this very abundant cytosolic/ER-associated enzyme in mitochondrial preparations most likely reflects contamination. Reason: High-throughput mitochondrial detection not supported by targeting or function; mitochondrial ACC is Hfa1. Supporting Evidence: PMID:14761959 Other than Acc1p, the N-terminal sequence of Hfa1p comprises a canonical mitochondrial targeting signal together with a matrix protease cleavage site PMID:16823961 A total of 851 different proteins (PROMITO dataset) were identified |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | REMOVE | Summary: IBA (is_active_in) from node PTN000429607 whose experimental sources are mitochondrial ACCs (Hfa1 SGD:S000004820, human ACACB, mouse/rat Acacb). Acc1 diverged as the cytosolic isoform: it lacks the N-terminal mitochondrial targeting sequence present in Hfa1, does not complement hfa1, and its function is in cytoplasmic fatty acid synthesis. The inherited location does not apply to Acc1. Propagation Review Root cause: PROPAGATION BAD Failure modes: COMPARTMENT OR COMPLEX MISMATCH Sources checked: PANTHER:PTN000429607 · PTN000429607 SUPPORTS SOURCE BUT NOT TARGET Node grounded in mitochondrial ACCs (Hfa1, ACACB); Acc1 is the cytosolic paralog lacking an MTS. Supporting Evidence: PMID:14761959 Other than Acc1p, the N-terminal sequence of Hfa1p comprises a canonical mitochondrial targeting signal together with a matrix protease cleavage site PMID:14761959 Whereas ACC1 is involved in cytoplasmic fatty acid synthesis |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:9438137 Yeast acetyl-CoA carboxylase is associated with the cytoplas... | ACCEPT | Summary: IDA (Ivessa et al. 1997): fractionation and immunofluorescence show Acc1 loosely (peripherally) associated with the cytosolic face of the nuclear ER membrane, proposed to channel malonyl-CoA to the ER elongase. Correct peripheral location. Supporting Evidence: PMID:9438137 it is loosely associated with the cytosolic surface of the nuclear ER membrane |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: IEA from UniProt subcellular location (Endoplasmic reticulum membrane; peripheral, cytoplasmic side), based on Ivessa et al. 1997. Correct. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane; PMID:9438137 it is loosely associated with the cytosolic surface of the nuclear ER membrane |
| GO:0005829 cytosol | HDA PMID:26928762 One library to make them all: streamlining the creation of y... | ACCEPT | Summary: HDA (SWAp-Tag GFP library, Yofe et al. 2016) detects Acc1 in the cytosol. Consistent with its role in cytoplasmic fatty acid synthesis. Supporting Evidence: PMID:26928762 One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. PMID:14761959 Whereas ACC1 is involved in cytoplasmic fatty acid synthesis |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: RCA (is_active_in) from YeastPathways PWY3O-10 (fatty acid biosynthesis, initial steps) placing the ACC step in the cytosol. Correct for Acc1. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane; PMID:14761959 Whereas ACC1 is involved in cytoplasmic fatty acid synthesis |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: RCA (is_active_in) from YeastPathways PWY3O-5962 (superpathway of fatty acid biosynthesis, saturated and unsaturated) placing the ACC step in the cytosol. Correct for Acc1. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane; PMID:14761959 Whereas ACC1 is involved in cytoplasmic fatty acid synthesis |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: RCA (is_active_in) from YeastPathways PWY3O-6336 (superpathway of fatty acid biosynthesis, saturated) placing the ACC step in the cytosol. Correct for Acc1. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane; PMID:14761959 Whereas ACC1 is involved in cytoplasmic fatty acid synthesis |
| GO:0006085 acetyl-CoA biosynthetic process | IMP PMID:15341732 Crystal structure of the carboxyltransferase domain of acety... | MODIFY | Summary: IMP from the CT-domain inhibitor study (Zhang et al. 2004). Acc1 consumes acetyl-CoA; it does not synthesise it. The product of the reaction is malonyl-CoA, so the correct process is malonyl-CoA biosynthetic process. Proposed replacements: malonyl-CoA biosynthetic process Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + file:yeast/ACC1/ACC1-uniprot.txt PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from PMID:15341732 The inhibitor is bound in the active site at the interface of a dimer of the CT domain |
| GO:0006606 protein import into nucleus | IMP PMID:12730220 Nuclear accumulation of the small GTPase Gsp1p depends on nu... | MARK AS OVER ANNOTATED | Summary: IMP (Gao et al. 2003): the mtr7-1 (acc1) allele impairs nuclear accumulation of GFP-Gsp1p at restrictive temperature. Acc1 is a metabolic enzyme; the effect is an indirect consequence of defective lipid (VLCFA) synthesis and nuclear envelope integrity rather than participation in nuclear import. Reason: Indirect phenotype of a lipid biosynthetic enzyme; Acc1 does not perform any step of nuclear import. Supporting Evidence: PMID:12730220 the enzyme acetyl-CoA carboxylase (MTR7) control the distribution and cellular concentration of Gsp1p PMID:26458104 ScACC is crucial for the production of very-long-chain fatty acids and the maintenance of the nuclear envelope |
| GO:0006633 fatty acid biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from eukaryotic ACC node (PTN000429606 etc.). Acc1 catalyses the committed step of cytosolic fatty acid synthesis; correct. Supporting Evidence: PMID:6103540 The mutant is deficient in de novo biosynthesis of long-chain fatty acids and specifically requires a saturated fatty acid of chain length 14-16 C atoms for growth file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + |
| GO:0006633 fatty acid biosynthetic process | IEA GO_REF:0000002 | ACCEPT | Summary: IEA from InterPro IPR013537 (ACC central domain). Correct for Acc1. Supporting Evidence: PMID:6103540 The mutant is deficient in de novo biosynthesis of long-chain fatty acids and specifically requires a saturated fatty acid of chain length 14-16 C atoms for growth |
| GO:0006633 fatty acid biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-10 (fatty acid biosynthesis, initial steps). Acc1 supplies malonyl-CoA for cytosolic FAS; correct. Supporting Evidence: PMID:6103540 The mutant is deficient in de novo biosynthesis of long-chain fatty acids and specifically requires a saturated fatty acid of chain length 14-16 C atoms for growth file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + |
| GO:0006633 fatty acid biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-5962 (superpathway of fatty acid biosynthesis, saturated and unsaturated). Acc1 supplies malonyl-CoA for cytosolic FAS; correct. Supporting Evidence: PMID:6103540 The mutant is deficient in de novo biosynthesis of long-chain fatty acids and specifically requires a saturated fatty acid of chain length 14-16 C atoms for growth file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + |
| GO:0009317 acetyl-CoA carboxylase complex | IMP PMID:15341732 Crystal structure of the carboxyltransferase domain of acety... | KEEP AS NON CORE | Summary: IMP (Zhang et al. 2004, CT-domain structure). Yeast ACC is a single multidomain polypeptide acting as a homodimer; the GO complex term (exemplified by the heteromeric E. coli ACC) can be applied to the Acc1 homodimer. Acceptable but non-core. Reason: Homodimeric holoenzyme; complex term adds little beyond the MF. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt SUBUNIT: Homodimer. PMID:26458104 function as homodimers and higher oligomers |
| GO:0016743 carboxyl- or carbamoyltransferase activity | IMP PMID:15341732 Crystal structure of the carboxyltransferase domain of acety... | KEEP AS NON CORE | Summary: IMP (Zhang et al. 2004): carboxyltransferase partial activity of the CT domain (transfer of the carboxyl group from carboxybiotin to acetyl-CoA), assayed with the inhibitor CP-640186. Correct as a domain activity, subsumed by acetyl-CoA carboxylase activity. Reason: Partial (domain) activity subsumed by acetyl-CoA carboxylase activity. Supporting Evidence: PMID:15341732 CP-640186 has tight interactions with the putative biotin binding site in the CT domain PMID:6108218 These results suggest that acc1 is a cluster gene coding for a multifunctional protein harboring both acetyl-CoA carboxylase component enzyme activities on the same polypeptide chain |
| GO:0016874 ligase activity | IEA GO_REF:0000002 | TOO GENERAL | Summary: IEA from InterPro IPR011763 (CoA carboxyltransferase C-terminal). ACC is EC 6.4.1.2, a ligase, so correct but uninformative compared with acetyl-CoA carboxylase activity. Reason: Uninformative parent of the core MF. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + |
| GO:0019367 fatty acid elongation, saturated fatty acid | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: RCA from YeastPathways PWY3O-6336 (superpathway of fatty acid biosynthesis, saturated). Acc1 provides malonyl-CoA that is also the two-carbon donor of ER elongases, and acc1 mutants are defective in very-long-chain fatty acid synthesis, so involvement in elongation is genuine but secondary to its committed-step role. Reason: Malonyl-CoA supply for elongation is a real but secondary role. Supporting Evidence: PMID:26458104 ScACC is crucial for the production of very-long-chain fatty acids and the maintenance of the nuclear envelope PMID:9438137 it is loosely associated with the cytosolic surface of the nuclear ER membrane |
| GO:0042759 long-chain fatty acid biosynthetic process | IEA GO_REF:0000117 | ACCEPT | Summary: IEA from ARBA00034980 rule. Consistent with the IMP evidence that Acc1 is required for long-chain fatty acid synthesis. Supporting Evidence: PMID:6103540 The mutant is deficient in de novo biosynthesis of long-chain fatty acids and specifically requires a saturated fatty acid of chain length 14-16 C atoms for growth |
| GO:0042759 long-chain fatty acid biosynthetic process | IMP PMID:6103540 Fatty acid-requiring mutant of Saccharomyces cerevisiae defe... | ACCEPT | Summary: IMP (Roggenkamp et al. 1980): acc1-167 is deficient in de novo long-chain fatty acid synthesis and needs C14-C16 saturated fatty acids. Correct. Supporting Evidence: PMID:6103540 The mutant is deficient in de novo biosynthesis of long-chain fatty acids and specifically requires a saturated fatty acid of chain length 14-16 C atoms for growth |
| GO:0042802 identical protein binding | IPI PMID:26458104 Crystal structure of the 500-kDa yeast acetyl-CoA carboxylas... | KEEP AS NON CORE | Summary: IPI (Wei & Tong 2015): crystal structure of the 500-kDa Acc1 holoenzyme dimer. Homodimerisation is required because the CT active site lies at the dimer interface; correct but non-core. Reason: Self-association required for activity; captured by the catalytic MF. Supporting Evidence: PMID:26458104 function as homodimers and higher oligomers PMID:12663926 The active site is at the interface of a dimer |
| GO:0042802 identical protein binding | IPI PMID:31454312 The role of structural pleiotropy and regulatory evolution i... | KEEP AS NON CORE | Summary: IPI from a paralog/homomer DHFR-PCA study (Marchant et al. 2019) detecting Acc1-Acc1 self-interaction. Consistent with the known homodimer. Reason: Self-association required for activity; captured by the catalytic MF. Supporting Evidence: PMID:31454312 The role of structural pleiotropy and regulatory evolution in the retention of heteromers of paralogs. file:yeast/ACC1/ACC1-uniprot.txt SUBUNIT: Homodimer. |
| GO:0042803 protein homodimerization activity | IMP PMID:15341732 Crystal structure of the carboxyltransferase domain of acety... | KEEP AS NON CORE | Summary: IMP (Zhang et al. 2004): the CT domain dimerises and the active site is formed at the dimer interface. Correct but non-core. Reason: Structural requirement for the catalytic activity. Supporting Evidence: PMID:15341732 The inhibitor is bound in the active site at the interface of a dimer of the CT domain file:yeast/ACC1/ACC1-uniprot.txt SUBUNIT: Homodimer. |
| GO:0046872 metal ion binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: IEA from ATP-grasp InterPro domain (IPR011761). The BC domain binds Mn2+/Mg2+ for ATP-dependent carboxylation; correct but uninformative. Reason: Cofactor binding implied by the catalytic activity. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt Note=Binds 2 manganese ions per subunit. |
| GO:1905502 acetyl-CoA binding | IMP PMID:15341732 Crystal structure of the carboxyltransferase domain of acety... | KEEP AS NON CORE | Summary: IMP (Zhang et al. 2004): the CT domain binds the acyl-CoA substrate at the dimer interface. Substrate binding is part of the catalytic activity; non-core. Reason: Substrate binding implied by the catalytic activity. Supporting Evidence: PMID:15341732 The inhibitor is bound in the active site at the interface of a dimer of the CT domain |
| GO:2001295 malonyl-CoA biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: IEA from UniPathway UPA00655 (malonyl-CoA biosynthesis from acetyl-CoA, step 1/1). This is exactly the process Acc1 carries out; core BP. Supporting Evidence: file:yeast/ACC1/ACC1-uniprot.txt PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from file:yeast/ACC1/ACC1-uniprot.txt Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + |
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Download this section (compressed HTML)Q: Is the essential, fatty-acid-irremediable requirement for Acc1 fully explained by malonyl-CoA supply to the ER elongases (VLCFA for sphingolipids), or does Acc1 have an additional non-catalytic role at the nuclear envelope?
Q: Does Acc1 contribute any malonyl-CoA to mitochondria, or is the mitochondrial pool supplied exclusively by Hfa1?
Experiment: Rescue of acc1 null lethality by targeted expression of a malonyl-CoA synthetase or by VLCFA/sphingolipid supplementation, to separate VLCFA supply from any non-catalytic role.
Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availability of acetyl-CoA; rate-limiting step for de novo biosynthesis of long-chain fatty acids; translational regulation in response to nutrients and cell cycle stage depends on its upstream ORF; ACC1 has a paralog, HFA1, that arose from the whole genome duplication
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