ID   ACAC_CHICK              Reviewed;        2324 AA.
AC   P11029;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   04-NOV-2026, entry version 168.
DE   RecName: Full=Acetyl-CoA carboxylase;
DE            Short=ACC;
DE            EC=6.4.1.2;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
GN   Name=ACAC;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND BIOTINYLATION AT
RP   LYS-786.
RC   TISSUE=Liver;
RX   PubMed=2893793; DOI=10.1016/s0021-9258(18)69116-1;
RA   Takai T., Yokoyama C., Wada K., Tanabe T.;
RT   "Primary structure of chicken liver acetyl-CoA carboxylase deduced from
RT   cDNA sequence.";
RL   J. Biol. Chem. 263:2651-2657(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 493-820.
RC   TISSUE=Liver;
RX   PubMed=2879745; DOI=10.1016/0014-5793(87)81564-8;
RA   Takai T., Wada K., Tanabe T.;
RT   "Primary structure of the biotin-binding site of chicken liver acetyl-CoA
RT   carboxylase.";
RL   FEBS Lett. 212:98-102(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-18; 99-111; 121-132; 153-163; 278-288; 300-311;
RP   336-350; 589-607; 742-755; 826-845; 1083-1096; 1147-1155; 1157-1169;
RP   1233-1239; 1275-1286; 1319-1326; 1349-1362; 1365-1377; 1387-1397;
RP   1653-1678; 1701-1708; 1727-1737; 1759-1775; 1801-1810; 1815-1833;
RP   1882-1891; 1899-1906; 1955-1986; 2040-2049; 2067-2080; 2092-2104;
RP   2177-2186; 2190-2195; 2199-2206 AND 2209-2226, ACETYLATION AT MET-1, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V., Black E.J., Gillespie D.A.;
RL   Submitted (JAN-2007) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis of
CC       long-chain fatty acids. Carries out three functions: biotin carboxyl
CC       carrier protein, biotin carboxylase and carboxyltransferase.
CC       {ECO:0000250|UniProtKB:Q13085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP +
CC         phosphate + H(+); 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:0000250|UniProtKB:Q5SWU9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-biotinyl-L-lysyl-[protein] + hydrogencarbonate + ATP =
CC         N(6)-carboxybiotinyl-L-lysyl-[protein] + ADP + phosphate + H(+);
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000250|UniProtKB:Q5SWU9};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000250|UniProtKB:O00763};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: By phosphorylation.
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR   EMBL; J03541; AAA48701.1; -; mRNA.
DR   EMBL; X05019; CAA28675.1; -; mRNA.
DR   PIR; A29924; A29924.
DR   RefSeq; NP_990836.2; NM_205505.2.
DR   AlphaFoldDB; P11029; -.
DR   SMR; P11029; -.
DR   BioGRID; 676751; 1.
DR   FunCoup; P11029; 1592.
DR   STRING; 9031.ENSGALP00000043760; -.
DR   PaxDb; 9031-ENSGALP00000043760; -.
DR   GeneID; 396504; -.
DR   KEGG; gga:396504; -.
DR   CTD; 31; -.
DR   VEuPathDB; HostDB:geneid_396504; -.
DR   eggNOG; KOG0368; Eukaryota.
DR   InParanoid; P11029; -.
DR   OrthoDB; 14612at2759; -.
DR   PhylomeDB; P11029; -.
DR   SABIO-RK; P11029; -.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:P11029; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; TAS:AgBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:AgBase.
DR   GO; GO:0005524; F:ATP binding; IDA:AgBase.
DR   GO; GO:0009374; F:biotin binding; IDA:AgBase.
DR   GO; GO:0004075; F:biotin carboxylase activity; IDA:AgBase.
DR   GO; GO:0050692; F:DNA binding domain binding; IDA:AgBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0046966; F:nuclear thyroid hormone receptor binding; TAS:AgBase.
DR   GO; GO:0005102; F:signaling receptor binding; TAS:AgBase.
DR   GO; GO:0032810; F:sterol response element binding; TAS:AgBase.
DR   GO; GO:0040029; P:epigenetic regulation of gene expression; IDA:AgBase.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IDA:AgBase.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IDA:AgBase.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR   GO; GO:0009743; P:response to carbohydrate; IDA:AgBase.
DR   GO; GO:0070542; P:response to fatty acid; TAS:AgBase.
DR   GO; GO:0097066; P:response to thyroid hormone; IDA:AgBase.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   FunFam; 2.40.460.10:FF:000001; Acetyl-CoA carboxylase 1; 1.
DR   FunFam; 2.40.50.100:FF:000005; Acetyl-CoA carboxylase 1; 1.
DR   FunFam; 3.30.470.20:FF:000005; Acetyl-CoA carboxylase 1; 1.
DR   FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR   FunFam; 3.40.50.20:FF:000005; acetyl-CoA carboxylase isoform X2; 1.
DR   FunFam; 3.90.226.10:FF:000010; acetyl-CoA carboxylase isoform X2; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR   Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR   InterPro; IPR049076; ACCA.
DR   InterPro; IPR049074; ACCA_BT.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR005479; CPAse_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR45728:SF5; ACETYL-COA CARBOXYLASE 1; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF21385; ACCA_BT; 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; SSF52096; ClpP/crotonase; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 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; ATP-binding; Biotin; Cytoplasm; Direct protein sequencing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Ligase; Lipid biosynthesis;
KW   Lipid metabolism; Manganese; Metal-binding; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..2324
FT                   /note="Acetyl-CoA carboxylase"
FT                   /id="PRO_0000146768"
FT   DOMAIN          117..618
FT                   /note="Biotin carboxylation"
FT   DOMAIN          275..466
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          745..819
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          1553..1891
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          1895..2211
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1553..2211
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000250"
FT   BINDING         315..320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         424
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         439
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1800
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2104
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2106
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         786
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT                   ECO:0000269|PubMed:2893793"
FT   MOD_RES         1193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   2324 AA;  262720 MW;  3F1C541F01BBBEF6 CRC64;
     MEESSQPAKP LEMNPHSRFI IGSVSEDNSE DETSSLVKLD LLEEKERSLS PVSVCSDSLS
     DLGLPSAQDG LANHMRPSMS GLHLVKQGRD RKKVDVQRDF TVASPAEFVT RFGGNRVIEK
     VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG
     GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLHKNGIAFM GPPSQAMWAL
     GDKIASSIVA QTAGIPTLPW NGSGLRVDWQ ENDLQKRILN VPQELYEKGY VKDADDGLRA
     AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV
     QILADQYGNA ISLFGRDCSV QRRHQKIIEE APASIATSVV FEHMEQCAVK LAKMVGYVSA
     GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL HRIKDIRVMY
     GVSPWGDGSI DFENSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY
     FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
     ESFQQNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSFRNSVSN FLHSLERGQV
     LPAHTLLNTV DVELIYEGRK YVLKVTRQSP NSYVVIMNSS CVEVDVHRLS DGGLLLSYDG
     SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSILRSPSAG KLIQYVVEDG GHVFAGQCFA
     EIEVMKMVMT LTAGESGCIH YVKRPGAVLD PGCVIAKLQL DDPSRVQQAE LHTGTLPQIQ
     STALRGEKLH RIFHYVLDNL VNVMNGYCLP EPYFSSKVKG WVERLMKTLR DPSLPLLELQ
     DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV
     FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLKVETQ FQHGHYDKCV FALREENKSD
     MNAVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELI NILTELTQLS KTTNAKVALR
     ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH
     SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RMSFSSNLNH
     YGMVHVASVS DVLLDNSFTP PCQRMGGMVS FRTFEDFVRI FDEVMSCFCD SPPQSPTFPE
     AGHASLYDED KAAREEPIHI LNVAIKTDGD VDDDGLAAMF REFTQSKKSV LIEHGIRRLT
     FLVAQKREFP KFFTFRARDK FEEDRIYRHL EPALAFQLEL NRMRNFDLTA IPCANHKMHL
     YLGAAKVEVG TEVTDYRFFV RAIIRHSDLV TKEASFEYLQ NEGERLLLEA MDELEVAFNN
     TNVRTDCNHI FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEL KINIRLTPTG
     KAIPIRLFLT NESGYYLDIS LYKEVTDSRT GQIMFQAYGD KQGPLHGMLI NTPYVTKDLL
     QSKRFQAQSL GTSYVYDIPE MFRQSLIKLW DSMNEHAFLP TPPLPSDILT YTELVLDDQG
     QLVHMNRLPG GNEIGMVAWK MTLKTPEYPE GRDIIVIGND ITYRIGSFGP QEDVLFLRAS
     ELARTHGIPR IYVAANSGAR IGLAEEIRHM FHVAWEDPDD PYKGYKYLYL TPQDYKKVSA
     LNSVHCEHVE DNGESRYKIT DIIGKEDGLG IENLRGSGMI AGESSLAYES IITINLVTCR
     AIGIGAYLVR LGQRTIQVEN SHIILTGCGA LNKVLGREVY TSNNQLGGIQ IMHNNGVTHG
     TVCDDFEGVY TILLWLSYMP KSVYSPVPIL KVKDPIDRTI DFVPTKTPYD PRWMLAGRPN
     PSQKGQWQSG FFDNGSFLEI MQPWAQTVVV GRARLGGIPV GVVAVETRTV ELSIPADPAN
     LDSEAKIIQQ AGQVWFPDSA FKTAQAINDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF
     GAYIVDGLRE YRQPVLIYIP PQAELRGGSW AVIDPTINPR HMEMYADRES RGGILEPEGT
     VEIKFRRKDL VKTMRRVDPV YMRLAERLGT PELSAADRKD LESKLKEREE FLIPIYHQVA
     MQFADLHDTP GRMQEKGAIT DILDWKTSRT FFYWRLRRLL LEDVVKKKIH DANPELTDGQ
     IQAMLRRWFV EVEGTVKAYL WDSNKDLVEW LEKQLMEEEG VRSVVDENIK YISRDYILKQ
     IRSLVQANPE VAMDSIVHMT QHISPTQRAE IVRILSTMDS PSST
//