ACACA_MOUSE
ID ACACA_MOUSE Reviewed; 2345 AA.
AC Q5SWU9; A2A6H4; Q5SWU6; Q5SWU7; Q5SWU8; Q6JIZ1; Q6PHL9; Q705X8; Q705X9;
AC Q91VC8; Q925C4; Q925C5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Acetyl-CoA carboxylase 1 {ECO:0000305};
DE Short=ACC1;
DE EC=6.4.1.2 {ECO:0000269|PubMed:20952656};
DE AltName: Full=ACC-alpha;
DE AltName: Full=Acetyl-CoA carboxylase 265;
GN Name=Acaca {ECO:0000312|MGI:MGI:108451};
GN Synonyms=Acac {ECO:0000312|EMBL:AAS13685.1}, Gm738;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAS13685.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAS13685.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAS13685.1};
RA Mao J., Wakil S.J.;
RT "Characterization of the mouse acetyl-CoA carboxylase 1 (ACC1) gene and
RT identification of an intronless pseudogene.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-119 (ISOFORM 2).
RC STRAIN=SWR/J; TISSUE=Brain;
RX PubMed=15607423; DOI=10.1016/j.ygeno.2004.10.001;
RA Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C., Joulin V.;
RT "Asymmetric expression of transcripts derived from the shared promoter
RT between the divergently oriented ACACA and TADA2L genes.";
RL Genomics 85:71-84(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAK57392.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-38; 1221-1348 AND 1681-1891.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK57392.1};
RX PubMed=12668174; DOI=10.1016/s1388-1981(03)00041-6;
RA Salles J., Sargueil F., Knoll-Gellida A., Witters L.A., Cassagne C.,
RA Garbay B.;
RT "Acetyl-CoA carboxylase and SREBP expression during peripheral nervous
RT system myelination.";
RL Biochim. Biophys. Acta 1631:229-238(2003).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAH56500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1501-2345.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH56500.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH56500.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6] {ECO:0000305}
RP PROTEIN SEQUENCE OF 298-306 AND 2267-2275, INTERACTION WITH BRCA1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12360400; DOI=10.1038/sj.onc.1205915;
RA Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M.,
RA Venezia N.D.;
RT "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT
RT domains.";
RL Oncogene 21:6729-6739(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-29, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-79, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29; SER-47;
RP THR-57; SER-79; THR-609; SER-1215; SER-1217; THR-1226; SER-1258 AND
RP SER-1262, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP INTERACTION WITH MID1IP1.
RX PubMed=20457939; DOI=10.1073/pnas.1001292107;
RA Kim C.W., Moon Y.A., Park S.W., Cheng D., Kwon H.J., Horton J.D.;
RT "Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12
RT provides a tertiary level of regulation of fatty acid synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:9626-9631(2010).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, SUBUNIT,
RP INTERACTION WITH MID1IP1, PHOSPHORYLATION AT SER-79, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20952656; DOI=10.1073/pnas.1012736107;
RA Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M., McKean W.B.,
RA Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.;
RT "Crystal structure of Spot 14, a modulator of fatty acid synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010).
RN [14]
RP INDUCTION BY ENDOCANNABINOID ANANDAMIDE.
RX PubMed=21987372; DOI=10.1002/hep.24733;
RA Jourdan T., Demizieux L., Gresti J., Djaouti L., Gaba L., Verges B.,
RA Degrace P.;
RT "Antagonism of peripheral hepatic cannabinoid receptor-1 improves liver
RT lipid metabolism in mice: evidence from cultured explants.";
RL Hepatology 55:790-799(2012).
CC -!- FUNCTION: Cytosolic enzyme that catalyzes the carboxylation of acetyl-
CC CoA to malonyl-CoA, the first and rate-limiting step of de novo fatty
CC acid biosynthesis (PubMed:20952656). This is a 2 steps reaction
CC starting with the ATP-dependent carboxylation of the biotin carried by
CC the biotin carboxyl carrier (BCC) domain followed by the transfer of
CC the carboxyl group from carboxylated biotin to acetyl-CoA
CC (PubMed:20952656). {ECO:0000269|PubMed:20952656}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC Evidence={ECO:0000269|PubMed:20952656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11309;
CC Evidence={ECO:0000305|PubMed:20952656};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-
CC ProRule:PRU00969};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000250|UniProtKB:Q13085,
CC ECO:0000255|PROSITE-ProRule:PRU01066};
CC -!- ACTIVITY REGULATION: Inhibited by phosphorylation (By similarity).
CC Citrate promotes oligomerization of the protein into filaments that
CC correspond to the most active form of the carboxylase
CC (PubMed:20952656). {ECO:0000250|UniProtKB:Q13085,
CC ECO:0000269|PubMed:20952656}.
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000269|PubMed:20952656}.
CC -!- SUBUNIT: Monomer, homodimer, and homotetramer (PubMed:20952656). Can
CC form filamentous polymers (PubMed:20952656). Interacts in its inactive
CC phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA
CC dephosphorylation and inhibits lipid synthesis (PubMed:12360400).
CC Interacts with MID1IP1; interaction with MID1IP1 promotes
CC oligomerization and increases its activity (PubMed:20952656,
CC PubMed:20457939). {ECO:0000269|PubMed:12360400,
CC ECO:0000269|PubMed:20457939, ECO:0000269|PubMed:20952656}.
CC -!- INTERACTION:
CC Q5SWU9; Q9CQ20: Mid1ip1; NbExp=2; IntAct=EBI-773043, EBI-473024;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12360400,
CC ECO:0000269|PubMed:20952656}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SWU9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SWU9-2; Sequence=VSP_026101;
CC -!- INDUCTION: Up-regulated by endocannabinoid anandamide/AEA.
CC {ECO:0000269|PubMed:21987372}.
CC -!- DOMAIN: Consists of an N-terminal biotin carboxylation/carboxylase (BC)
CC domain that catalyzes the ATP-dependent transient carboxylation of the
CC biotin covalently attached to the central biotinyl-binding/biotin
CC carboxyl carrier (BCC) domain. The C-terminal carboxyl transferase (CT)
CC domain catalyzes the transfer of the carboxyl group from carboxylated
CC biotin to acetyl-CoA to produce malonyl-CoA.
CC {ECO:0000250|UniProtKB:Q13085}.
CC -!- PTM: Phosphorylation on Ser-1262 is required for interaction with
CC BRCA1. {ECO:0000250|UniProtKB:Q13085}.
CC -!- PTM: Phosphorylation at Ser-79 by AMPK inactivates enzyme activity.
CC {ECO:0000250|UniProtKB:P11497}.
CC -!- PTM: The biotin cofactor is covalently attached to the central
CC biotinyl-binding domain and is required for the catalytic activity.
CC {ECO:0000250|UniProtKB:Q13085}.
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DR EMBL; AY451393; AAS13685.1; -; mRNA.
DR EMBL; AL596252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ619664; CAF02251.1; -; mRNA.
DR EMBL; AJ619665; CAF02252.1; -; Genomic_DNA.
DR EMBL; AF374167; AAK57389.1; -; mRNA.
DR EMBL; AF374168; AAK57390.1; -; mRNA.
DR EMBL; AF374169; AAK57391.1; -; mRNA.
DR EMBL; AF374170; AAK57392.1; -; mRNA.
DR EMBL; BC056500; AAH56500.1; -; mRNA.
DR CCDS; CCDS25185.1; -. [Q5SWU9-1]
DR RefSeq; NP_579938.2; NM_133360.2. [Q5SWU9-1]
DR RefSeq; XP_006532016.1; XM_006531953.1. [Q5SWU9-2]
DR RefSeq; XP_006532017.1; XM_006531954.2. [Q5SWU9-1]
DR RefSeq; XP_006532018.1; XM_006531955.1. [Q5SWU9-1]
DR RefSeq; XP_006532019.1; XM_006531956.2. [Q5SWU9-1]
DR RefSeq; XP_006532020.1; XM_006531957.3. [Q5SWU9-1]
DR RefSeq; XP_011246969.1; XM_011248667.1. [Q5SWU9-1]
DR AlphaFoldDB; Q5SWU9; -.
DR SMR; Q5SWU9; -.
DR BioGRID; 223322; 9.
DR DIP; DIP-32276N; -.
DR IntAct; Q5SWU9; 10.
DR MINT; Q5SWU9; -.
DR STRING; 10090.ENSMUSP00000099490; -.
DR BindingDB; Q5SWU9; -.
DR ChEMBL; CHEMBL3086; -.
DR iPTMnet; Q5SWU9; -.
DR PhosphoSitePlus; Q5SWU9; -.
DR SwissPalm; Q5SWU9; -.
DR EPD; Q5SWU9; -.
DR jPOST; Q5SWU9; -.
DR MaxQB; Q5SWU9; -.
DR PaxDb; Q5SWU9; -.
DR PeptideAtlas; Q5SWU9; -.
DR PRIDE; Q5SWU9; -.
DR ProteomicsDB; 286026; -. [Q5SWU9-1]
DR ProteomicsDB; 286027; -. [Q5SWU9-2]
DR Antibodypedia; 73364; 653 antibodies from 39 providers.
DR DNASU; 107476; -.
DR Ensembl; ENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532. [Q5SWU9-1]
DR Ensembl; ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532. [Q5SWU9-1]
DR GeneID; 107476; -.
DR KEGG; mmu:107476; -.
DR UCSC; uc007kql.1; mouse. [Q5SWU9-1]
DR CTD; 31; -.
DR MGI; MGI:108451; Acaca.
DR VEuPathDB; HostDB:ENSMUSG00000020532; -.
DR eggNOG; KOG0368; Eukaryota.
DR GeneTree; ENSGT00940000156706; -.
DR HOGENOM; CLU_000395_5_0_1; -.
DR InParanoid; Q5SWU9; -.
DR OMA; LIQCAMP; -.
DR OrthoDB; 156081at2759; -.
DR PhylomeDB; Q5SWU9; -.
DR TreeFam; TF300061; -.
DR BRENDA; 6.4.1.2; 3474.
DR Reactome; R-MMU-163765; ChREBP activates metabolic gene expression.
DR Reactome; R-MMU-196780; Biotin transport and metabolism.
DR Reactome; R-MMU-200425; Carnitine metabolism.
DR Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis.
DR UniPathway; UPA00655; UER00711.
DR BioGRID-ORCS; 107476; 19 hits in 77 CRISPR screens.
DR ChiTaRS; Acaca; mouse.
DR PRO; PR:Q5SWU9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SWU9; protein.
DR Bgee; ENSMUSG00000020532; Expressed in epididymal fat pad and 252 other tissues.
DR ExpressionAtlas; Q5SWU9; baseline and differential.
DR Genevisible; Q5SWU9; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009374; F:biotin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0019538; P:protein metabolic process; IMP:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; Alternative promoter usage; ATP-binding;
KW Biotin; Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..2345
FT /note="Acetyl-CoA carboxylase 1"
FT /id="PRO_0000258040"
FT DOMAIN 116..617
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT DOMAIN 274..465
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 744..818
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 1575..1913
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 1917..2233
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1575..2233
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT ACT_SITE 440
FT /evidence="ECO:0000255"
FT BINDING 300..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 423
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 436
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 436
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 436
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 1822
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q00955"
FT BINDING 2126
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q00955"
FT BINDING 2128
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q00955"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11497"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11497"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11497"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20952656,
FT ECO:0007744|PubMed:17208939, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 79
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000305|PubMed:20952656,
FT ECO:0007744|PubMed:17208939, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 785
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11497,
FT ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11497"
FT MOD_RES 1215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1226
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 1333
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT MOD_RES 2152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13085"
FT VAR_SEQ 1
FT /note="M -> MMWWSTLMSLLRASSFWRRISAETIRIIRALRAYFERIM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15607423"
FT /id="VSP_026101"
FT CONFLICT 623
FT /note="E -> G (in Ref. 1; AAS13685)"
FT /evidence="ECO:0000305"
FT CONFLICT 906
FT /note="S -> P (in Ref. 1; AAS13685)"
FT /evidence="ECO:0000305"
FT CONFLICT 933
FT /note="C -> Y (in Ref. 1; AAS13685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1456
FT /note="L -> S (in Ref. 1; AAS13685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1995
FT /note="S -> G (in Ref. 1; AAS13685)"
FT /evidence="ECO:0000305"
FT CONFLICT 2077
FT /note="V -> I (in Ref. 1; AAS13685)"
FT /evidence="ECO:0000305"
FT CONFLICT 2169
FT /note="E -> K (in Ref. 1; AAS13685)"
FT /evidence="ECO:0000305"
FT CONFLICT 2251
FT /note="F -> S (in Ref. 1; AAS13685)"
FT /evidence="ECO:0000305"
FT CONFLICT 2257
FT /note="T -> A (in Ref. 1; AAS13685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2345 AA; 265257 MW; 6995C534B054FE02 CRC64;
MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD
LGISGLQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV
LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG
PNNNNYANVE LILDIAKRIP VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG
DKIASSIVAQ TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA
EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL AKQSRHLEVQ
ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF EHMEQCAVKL AKMVGYVSAG
TVEYLYSQDG SFYFLELNPR LQVEHPCTEM VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG
VSPWGDAPID FENSAHVPCP RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF
SVAAAGGLHE FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE
SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VSLRNSISNF LHSLERGQVL
PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS
SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE
IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS
TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSRVKDW VERLMKTLRD PSLPLLELQD
IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF
FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM
NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA
RQVLIASHLP SYELRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS
NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE IMGCFCDSPP
QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED DRLAAMFREF TQQNKATLVE
HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE FPKFFTFRAR DKFEEDRIYR HLEPALAFQL
ELNRMRNFDL TAIPCANHKM HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY
LQNEGERLLL EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS
RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS RTAQIMFQAY
GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI PEMFRQSLIK LWESMSTQAF
LPSPPLPSDI LTYTELVLDD QGQLVHMNRL PGGNEIGMVA WKMSLKSPEY PDGRDIIVIG
NDITYRIGSF GPQEDLLFLR ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDP
EDPYKGYKYL YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG
MIAGESSLAY DEVITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA GALNKVLGRE
VYTSNNQLGG IQIMHNNGVT HSTVCDDFEG VFTVLHWLSY MPKSVHSSVP LLNSKDPIDR
IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL SGFFDYGSFS EIMQPWAQTV VVGRARLGGI
PVGVVAVETR TVELSIPADP ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM
VFANWRGFSG GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN
PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL GTPELSPTER
KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV INDILDWKTS RTFFYWRLRR
LLLEDLVKKK IHNANPELTD GQIQAMLRRW FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE
DGVRSVIEEN IKYISRDYVL KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM
DSPST
