ACACA encodes acetyl-CoA carboxylase 1 (ACC1, also ACC-alpha; EC 6.4.1.2), a large cytosolic, biotin-dependent multi-domain enzyme that catalyzes the first, committed and rate-limiting step of de novo fatty acid biosynthesis: the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA (acetyl-CoA + HCO3- + ATP = malonyl-CoA + ADP + phosphate). Catalysis proceeds in two half-reactions carried out by distinct domains: an N-terminal biotin carboxylase (BC) domain uses ATP to carboxylate a biotin cofactor covalently attached to a central biotinyl-binding (biotin carboxyl carrier, BCC) domain, and a C-terminal carboxyltransferase (CT) domain then transfers the carboxyl group from carboxybiotin to acetyl-CoA, producing malonyl-CoA. Two magnesium or manganese ions per subunit are required. ACC1 is one of two mammalian ACC isozymes; it is the cytosolic enzyme supplying malonyl-CoA for chain elongation by fatty acid synthase, whereas the paralogous ACC2/ACACB is anchored to the outer mitochondrial membrane and regulates fatty acid oxidation. The malonyl-CoA product of ACC1 both feeds fatty acid synthesis and serves as a signaling metabolite. ACC1 activity is tightly and multiply regulated: inhibited by AMPK-dependent phosphorylation (notably Ser-80), allosterically activated by citrate which promotes polymerization into catalytically active filaments, further activated by the MID1IP1 (MIG12/S14R) protein that lowers the citrate threshold for polymerization, and inhibited by long-chain acyl-CoA. Its phosphorylated inactive form is bound by the BRCT domains of BRCA1, which blocks dephosphorylation and represses lipogenesis. Loss-of-function variants cause the autosomal recessive acetyl-CoA carboxylase deficiency (ACACAD), an inborn error of de novo fatty acid synthesis, and the enzyme is a drug target in metabolic disease (e.g. hepatic steatosis).
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006633 fatty acid biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic (IBA) annotation to fatty acid biosynthetic process. ACC1 catalyzes the committed, rate-limiting step of de novo fatty acid biosynthesis, so this is a correct core biological process for this gene. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt the first and rate-limiting step of de novo fatty PMID:29899443 a rate-limiting step in fatty acid biosynthesis |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Phylogenetic (IBA) annotation placing ACC1 as active in the mitochondrion. This is a paralog/compartment mis-propagation: the mitochondrion-anchored acetyl-CoA carboxylase isozyme is ACC2/ACACB, whereas Q13085 is the cytosolic ACC1. UniProt localizes ACC1 to the cytoplasm/cytosol, and the HPA IDA confirms cytosol. The mitochondrial term reflects the ACC-family phylogenetic node (which includes ACC2 orthologs), not ACC1. Reason: ORGANELLES check (2026-10-24): the PAINT IBD for GO:0005739 sits on PTHR45728 node PTN000429607 and its descendant evidence is MGI:2140940 and RGD:620500 (mouse and rat Acacb), UniProtKB:O00763 (human ACACB) and SGD:S000004820 (yeast HFA1, the mitochondrial acetyl-CoA carboxylase). Every seed is the mitochondrial-isozyme lineage; none is an ACC1 ortholog. ACC1 is placed under the node by descent, but its own curated location is cytosol, and it lacks the ACC2 N-terminal mitochondrial-anchoring extension. The organelle claim is not supported for this gene, so the row stays MARK_AS_OVER_ANNOTATED (the only GO:0005739 row) and no sub-compartment row is added. Propagation Review Root cause: PROPAGATION BAD Failure modes: COMPARTMENT OR COMPLEX MISMATCH Supporting Evidence: PMID:29899443 the metabolic, cytosolic ACC1, and ACC2, which is file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0003989 acetyl-CoA carboxylase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic (IBA) annotation to the defining catalytic activity of this enzyme. This is the core molecular function of ACC1 and is directly supported by experimental data. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt catalyzes the carboxylation of acetyl- |
| GO:0003989 acetyl-CoA carboxylase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic annotation (ARBA/UniRule, RHEA:11308, EC:6.4.1.2) to acetyl-CoA carboxylase activity. This is the gene's own correct core molecular function; the electronic support (EC 6.4.1.2 / RHEA mapping) is consistent with the curated catalytic activity. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt malonyl-CoA + ADP + |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO electronic annotation to ATP binding. ACC1 has an ATP-grasp subdomain within the biotin carboxylase domain and uses ATP to carboxylate biotin; UniProt records a defined ATP binding site (residues 315-320). This molecular function is correct and directly supports catalysis. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt ligand="ATP" |
| GO:0005829 cytosol | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic annotation to cytosol, consistent with the curated subcellular location and with the experimental (HPA IDA) cytosol annotation. Correct core localization for ACC1. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0006633 fatty acid biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic annotation to fatty acid biosynthetic process, a correct core BP for ACC1 (it catalyzes the committed step). Redundant with the IBA/ISS/IC annotations to the same term. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt the first and rate-limiting step of de novo fatty |
| GO:0006637 acyl-CoA metabolic process | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: ARBA electronic annotation to the broad term acyl-CoA metabolic process. While malonyl-CoA is technically an acyl-CoA, this general term is less informative than the specific and already-annotated malonyl-CoA biosynthetic process (GO:2001295) and fatty acid biosynthetic process (GO:0006633). Over-annotation via a generic term. |
| GO:0016874 ligase activity | IEA GO_REF:0000002 | MODIFY | Summary: InterPro2GO electronic annotation to the broad term ligase activity. ACC1 is a biotin-dependent carboxylase/ligase, but this generic term is subsumed by the specific and experimentally supported acetyl-CoA carboxylase activity (GO:0003989). Replace with the specific molecular function. Proposed replacements: acetyl-CoA carboxylase activity Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt catalyzes the carboxylation of acetyl- |
| GO:0046872 metal ion binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: InterPro2GO electronic annotation to metal ion binding. ACC1 binds two magnesium or manganese ions per subunit in the biotin carboxylase/ATP-grasp domain, so this generic MF is accurate. It is supporting rather than the core function; retained as non-core. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt Binds 2 magnesium or manganese ions per subunit |
| GO:0005515 protein binding | IPI PMID:16326698 BRCA1 affects lipid synthesis through its interaction with a... | MARK AS OVER ANNOTATED | Summary: IPI annotation capturing the physical interaction with BRCA1 (P38398). BRCA1 binds the phosphorylated, inactive form of ACC1 and prevents its dephosphorylation, repressing lipogenesis. The interaction is real and biologically meaningful, but the bare "protein binding" term is uninformative as a molecular function. Supporting Evidence: PMID:16326698 BRCA1 interacts solely with the phosphorylated and inactive |
| GO:0005515 protein binding | IPI PMID:18056116 Aldo-keto reductase family 1 B10 affects fatty acid synthesi... | MARK AS OVER ANNOTATED | Summary: IPI annotation for the interaction with AKR1B10 (O60218), which associates with and stabilizes ACCA (protecting it from ubiquitin-proteasome degradation). Real interaction but the generic "protein binding" MF is uninformative. Supporting Evidence: PMID:18056116 AKR1B10 associates with acetyl-CoA carboxylase-alpha (ACCA) |
| GO:0005515 protein binding | IPI PMID:19343720 Identification and characterization of proteins interacting ... | MARK AS OVER ANNOTATED | Summary: IPI annotation for the interaction with SIRT1 (Q96EB6), curated by IntAct from a sirtuin interactome study. The interaction is recorded, but the bare "protein binding" term is uninformative as a molecular function. |
| GO:0005515 protein binding | IPI PMID:20457939 Induced polymerization of mammalian acetyl-CoA carboxylase b... | MARK AS OVER ANNOTATED | Summary: IPI annotation for the interaction with MID1IP1 (MIG12; mouse Q9CQ20), which binds ACC and induces its polymerization and activation. Functionally important regulatory interaction, but the generic "protein binding" MF is uninformative. Supporting Evidence: PMID:20457939 MIG12, a 22 kDa cytosolic protein of |
| GO:0005515 protein binding | IPI PMID:38892011 Pin1 Exacerbates Non-Alcoholic Fatty Liver Disease by Enhanc... | MARK AS OVER ANNOTATED | Summary: IPI annotation for the interaction with PIN1 (Q13526). Pin1 binds ACC1 via its WW domain, blocks ACC1 phosphorylation and thereby activates it, promoting fatty acid synthesis. Real, mechanistically characterized interaction; the bare "protein binding" term remains uninformative as a molecular function. Supporting Evidence: PMID:38892011 Pin1 interacts directly with ACC1 and inhibits ACC1 phosphorylation |
| GO:0042802 identical protein binding | IPI PMID:20457939 Induced polymerization of mammalian acetyl-CoA carboxylase b... | KEEP AS NON CORE | Summary: IPI annotation to identical protein binding, reflecting ACC1 self-association. ACC1 forms homodimers, homotetramers and higher-order filamentous polymers (the citrate/MIG12 activated state). The self-interaction is well established; retained as non-core since it underlies the regulatory oligomerization rather than the catalytic function itself. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt Monomer, homodimer, and homotetramer |
| GO:0006084 acetyl-CoA metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl-projected annotation to acetyl-CoA metabolic process. ACC1 consumes acetyl-CoA as its substrate (converting it to malonyl-CoA), so participation in acetyl-CoA metabolism is accurate. Retained as a correct, supporting (non-core) process. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt catalyzes the carboxylation of acetyl- |
| GO:0051289 protein homotetramerization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl-projected annotation to protein homotetramerization. ACC1 is a monomer, homodimer and homotetramer, and self-assembly into oligomers/filaments is central to its allosteric regulation. Correct but regulatory; retained as non-core. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt Monomer, homodimer, and homotetramer |
| GO:0046949 fatty-acyl-CoA biosynthetic process | TAS Reactome:R-HSA-75105 | KEEP AS NON CORE | Summary: Reactome TAS annotation placing ACC1 in fatty-acyl-CoA biosynthesis. ACC1 supplies the malonyl-CoA that fuels the fatty acid synthase pathway; this reflects pathway context rather than ACC1's direct product. Retained as a correct non-core process (the specific malonyl-CoA/fatty-acid biosynthesis terms are the core BP). |
| GO:0046949 fatty-acyl-CoA biosynthetic process | TAS Reactome:R-HSA-75851 | KEEP AS NON CORE | Summary: Reactome TAS annotation (duplicate of the fatty-acyl-CoA biosynthetic process annotation) from the ACC carboxylation reaction module. Pathway-context process retained as non-core. |
| GO:2001295 malonyl-CoA biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: UniPathway-derived annotation to malonyl-CoA biosynthetic process. This is precisely the direct product-forming process of ACC1 (malonyl-CoA from acetyl-CoA, step 1/1) and is a core biological process for this gene. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt malonyl-CoA biosynthesis; malonyl-CoA from |
| GO:0003989 acetyl-CoA carboxylase activity | TAS Reactome:R-HSA-200555 | ACCEPT | Summary: Reactome TAS annotation to the enzyme's core catalytic activity (malonyl-CoA formation in liver). Correct core molecular function. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt catalyzes the carboxylation of acetyl- |
| GO:0003989 acetyl-CoA carboxylase activity | TAS Reactome:R-HSA-75851 | ACCEPT | Summary: Reactome TAS annotation to acetyl-CoA carboxylase activity (biotinylated ACACA polymer carboxylating acetyl-CoA to malonyl-CoA). Correct core molecular function; redundant with the experimental IDA annotations. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt catalyzes the carboxylation of acetyl- |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Experimental (IDA, HPA immunofluorescence) annotation to cytosol. This is the authoritative, directly demonstrated subcellular location of ACC1 and matches the curated UniProt localization. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0003989 acetyl-CoA carboxylase activity | IDA PMID:26976583 Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic ... | ACCEPT | Summary: Experimental (IDA) annotation to acetyl-CoA carboxylase activity. This study characterizes ACC enzymatic activity and its allosteric inhibition by ND-630 (which blocks dimerization of both ACC isozymes and inhibits enzymatic activity), directly assaying the carboxylase function. Core molecular function. Supporting Evidence: PMID:26976583 prevent dimerization and inhibit the enzymatic activity of both ACC isozymes |
| GO:0003989 acetyl-CoA carboxylase activity | IDA PMID:29899443 Structural basis for regulation of human acetyl-CoA carboxyl... | ACCEPT | Summary: Experimental (IDA) annotation to acetyl-CoA carboxylase activity from the cryo-EM structural/functional study of human ACC1, which directly establishes the ATP-dependent carboxylation of acetyl-CoA and its regulation. Core molecular function. Supporting Evidence: PMID:29899443 Acetyl-CoA carboxylase catalyses the ATP-dependent carboxylation of acetyl-CoA |
| GO:0005515 protein binding | IPI PMID:29899443 Structural basis for regulation of human acetyl-CoA carboxyl... | MARK AS OVER ANNOTATED | Summary: IPI annotation for the interaction with BRCA1 (P38398), here supported by the cryo-EM structure of the inhibited ACC1 filament bound by the BRCA1 BRCT domains. Real and structurally characterized, but the bare "protein binding" MF is uninformative. Supporting Evidence: PMID:29899443 binding of the BRCT domains of the breast cancer type 1 susceptibility protein |
| GO:0006633 fatty acid biosynthetic process | IC GO_REF:0000111 | ACCEPT | Summary: Curator-inferred (IC) annotation to fatty acid biosynthetic process, based on the acetyl-CoA carboxylase activity annotation (GO:0003989). This is a correct core BP for ACC1, whose product malonyl-CoA is the committed precursor for fatty acid synthesis. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt the first and rate-limiting step of de novo fatty |
| GO:0003989 acetyl-CoA carboxylase activity | IDA PMID:20457939 Induced polymerization of mammalian acetyl-CoA carboxylase b... | ACCEPT | Summary: Experimental (IDA) annotation to acetyl-CoA carboxylase activity. This study assays ACC enzymatic activity and its enhancement (>50-fold) upon MIG12-induced polymerization, directly measuring the carboxylase function. Core molecular function. Supporting Evidence: PMID:20457939 increased ACC activity by > 50-fold in the presence of |
| GO:0005829 cytosol | TAS Reactome:R-HSA-200555 | ACCEPT | Summary: Reactome TAS annotation to cytosol, consistent with the experimental (IDA) and curated localization of ACC1. Correct core localization. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2993814 | ACCEPT | Summary: Reactome TAS annotation to cytosol (from the HLCS-biotinylates-ACACA module). Correct core localization, redundant with the experimental IDA annotation. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3065958 | ACCEPT | Summary: Reactome TAS annotation to cytosol (from an ACACA degradation module). Correct core localization, redundant with the experimental IDA annotation. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0005829 cytosol | TAS Reactome:R-HSA-75851 | ACCEPT | Summary: Reactome TAS annotation to cytosol (from the ACC carboxylation reaction module). Correct core localization, redundant with the experimental IDA annotation. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0005829 cytosol | TAS Reactome:R-HSA-163743 | ACCEPT | Summary: Reactome TAS annotation to cytosol (from an ACACA transcriptional-activation module). Correct core localization, redundant with the experimental IDA annotation. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1655845 | ACCEPT | Summary: Reactome TAS annotation to cytosol (from an ACACA expression module). Correct core localization, redundant with the experimental IDA annotation. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3323184 | ACCEPT | Summary: Reactome TAS annotation to cytosol (from a defective-HLCS biotinylation module). Correct core localization, redundant with the experimental IDA annotation. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0003989 acetyl-CoA carboxylase activity | ISS PMID:20952656 Crystal structure of Spot 14, a modulator of fatty acid synt... | ACCEPT | Summary: Sequence-similarity (ISS) annotation to acetyl-CoA carboxylase activity, transferred from mouse ortholog Q5SWU9. This is the correct core molecular function, corroborated by multiple experimental IDA annotations in human. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt catalyzes the carboxylation of acetyl- |
| GO:0005515 protein binding | IPI PMID:20952656 Crystal structure of Spot 14, a modulator of fatty acid synt... | MARK AS OVER ANNOTATED | Summary: IPI annotation for the interaction with MID1IP1 (MIG12; mouse Q9CQ20). The Spot 14 (S14)/MIG12 study shows MIG12 induces ACC polymerization and activity; the S14-MIG12 heterodimer attenuates this. Real regulatory interaction, but bare "protein binding" is uninformative as a molecular function. Supporting Evidence: PMID:20952656 MIG12 modulates fatty acid synthesis by inducing the polymerization and activity of acetyl-CoA carboxylase |
| GO:0005829 cytosol | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity (ISS) annotation to cytosol, transferred from mouse ortholog Q5SWU9. Consistent with the experimental (IDA) and curated localization of ACC1. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm, cytosol |
| GO:0006084 acetyl-CoA metabolic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Sequence-similarity (ISS) annotation to acetyl-CoA metabolic process, transferred from mouse ortholog Q5SWU9. ACC1 consumes acetyl-CoA as substrate; accurate but supporting, retained as non-core. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt catalyzes the carboxylation of acetyl- |
| GO:0006633 fatty acid biosynthetic process | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity (ISS) annotation to fatty acid biosynthetic process, transferred from mouse ortholog Q5SWU9. Correct core BP for ACC1; redundant with the IBA/IEA/IC annotations to the same term. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt the first and rate-limiting step of de novo fatty |
| GO:0051289 protein homotetramerization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Sequence-similarity (ISS) annotation to protein homotetramerization, transferred from mouse ortholog Q5SWU9. ACC1 forms homotetramers (and higher-order polymers) as part of its allosteric regulation. Correct but regulatory; retained as non-core. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt Monomer, homodimer, and homotetramer |
| GO:0051289 protein homotetramerization | ISS PMID:20952656 Crystal structure of Spot 14, a modulator of fatty acid synt... | KEEP AS NON CORE | Summary: Sequence-similarity (ISS) annotation to protein homotetramerization (from the MIG12/S14 polymerization study, transferred from mouse Q5SWU9). Correct but regulatory oligomer assembly; retained as non-core. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt Monomer, homodimer, and homotetramer |
| GO:0005515 protein binding | IPI PMID:16794074 TRB3 links the E3 ubiquitin ligase COP1 to lipid metabolism. | MARK AS OVER ANNOTATED | Summary: IPI annotation (BHF-UCL) for the interaction with the TRB3/COP1 ubiquitination system (with/from Q8K4K2, mouse Trib3). ACC is the substrate whose degradation is triggered by the TRB3-COP1 axis during fasting. Real interaction, but the bare "protein binding" MF is uninformative. Supporting Evidence: PMID:16794074 stimulates lipolysis by triggering the degradation of ACC in adipose tissue |
| GO:0003989 acetyl-CoA carboxylase activity | TAS PMID:7905825 Cloning of human acetyl-CoA carboxylase cDNA. | ACCEPT | Summary: TAS annotation to acetyl-CoA carboxylase activity from the original human ACC cDNA cloning paper, which characterizes ACC as the rate-limiting enzyme in long-chain fatty acid biogenesis. Correct core molecular function. Supporting Evidence: PMID:7905825 Acetyl-CoA carboxylase is the rate-limiting enzyme in the biogenesis of |
| GO:0004075 biotin carboxylase activity | IDA PMID:29899443 Structural basis for regulation of human acetyl-CoA carboxyl... | NEW | Summary: Proposed new annotation. The N-terminal biotin carboxylase (BC) / ATP-grasp domain of ACC1 catalyzes the first half-reaction: ATP-dependent carboxylation of the biotin cofactor carried by the biotinyl-binding domain. This sub-activity of the overall acetyl-CoA carboxylase reaction is a defined domain function not separately captured in GOA and is supported by the domain architecture and structural work. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt the ATP-dependent transient carboxylation of the PMID:29899443 Acetyl-CoA carboxylase catalyses the ATP-dependent carboxylation of acetyl-CoA |
| GO:0009374 biotin binding | IDA PMID:29899443 Structural basis for regulation of human acetyl-CoA carboxyl... | NEW | Summary: Proposed new annotation. ACC1 carries a biotin cofactor covalently attached to the central biotinyl-binding (biotin carboxyl carrier) domain that is required for catalytic activity; the biotin shuttles the activated carboxyl group between the biotin carboxylase and carboxyltransferase active sites. Not separately captured in GOA. Supporting Evidence: file:human/ACACA/ACACA-uniprot.txt The biotin cofactor is covalently attached to the central |
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