ACAC_CHICK
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 03-AUG-2022, entry version 155.
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=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:0000250|UniProtKB:Q5SWU9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
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_990836.1; NM_205505.1.
DR AlphaFoldDB; P11029; -.
DR SMR; P11029; -.
DR BioGRID; 676751; 1.
DR STRING; 9031.ENSGALP00000034072; -.
DR PRIDE; P11029; -.
DR GeneID; 396504; -.
DR KEGG; gga:396504; -.
DR CTD; 31; -.
DR VEuPathDB; HostDB:geneid_396504; -.
DR eggNOG; KOG0368; Eukaryota.
DR InParanoid; P11029; -.
DR PhylomeDB; P11029; -.
DR SABIO-RK; P11029; -.
DR UniPathway; UPA00655; UER00711.
DR PRO; PR:P11029; -.
DR Proteomes; UP000000539; Unplaced.
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:UniProtKB-KW.
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:0006633; P:fatty acid biosynthetic process; IDA:AgBase.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IDA:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:AgBase.
DR GO; GO:0065008; P:regulation of biological quality; IDA:AgBase.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; 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 GO; GO:0006810; P:transport; TAS:AgBase.
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; 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
