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Acetyl-CoA carboxylase (ACC) (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 ACAC_CHICK              Reviewed;        2324 AA.
P11029;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
10-MAY-2017, entry version 139.
RecName: Full=Acetyl-CoA carboxylase;
Short=ACC;
EC=6.4.1.2;
Includes:
RecName: Full=Biotin carboxylase;
EC=6.3.4.14;
Name=ACAC;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
BIOTINYLATION AT LYS-786.
TISSUE=Liver;
PubMed=2893793;
Takai T., Yokoyama C., Wada K., Tanabe T.;
"Primary structure of chicken liver acetyl-CoA carboxylase deduced
from cDNA sequence.";
J. Biol. Chem. 263:2651-2657(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 493-820.
TISSUE=Liver;
PubMed=2879745; DOI=10.1016/0014-5793(87)81564-8;
Takai T., Wada K., Tanabe T.;
"Primary structure of the biotin-binding site of chicken liver acetyl-
CoA carboxylase.";
FEBS Lett. 212:98-102(1987).
[3]
PROTEIN SEQUENCE OF 1-18; 99-111; 121-132; 153-163; 278-288; 300-311;
336-350; 589-607; 742-755; 826-845; 1083-1096; 1147-1155; 1157-1169;
1233-1239; 1275-1286; 1319-1326; 1349-1362; 1365-1377; 1387-1397;
1653-1678; 1701-1708; 1727-1737; 1759-1775; 1801-1810; 1815-1833;
1882-1891; 1899-1906; 1955-1986; 2040-2049; 2067-2080; 2092-2104;
2177-2186; 2190-2195; 2199-2206 AND 2209-2226, ACETYLATION AT MET-1,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V., Black E.J., Gillespie D.A.;
Submitted (JAN-2007) to UniProtKB.
-!- FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis
of long-chain fatty acids. Carries out three functions: biotin
carboxyl carrier protein, biotin carboxylase and
carboxyltransferase. {ECO:0000250|UniProtKB:Q13085}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000250|UniProtKB:Q5SWU9}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000250|UniProtKB:Q5SWU9}.
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586;
Evidence={ECO:0000250|UniProtKB:O00763};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: By phosphorylation.
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBCELLULAR LOCATION: Cytoplasm.
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EMBL; J03541; AAA48701.1; -; mRNA.
EMBL; X05019; CAA28675.1; -; mRNA.
PIR; A29924; A29924.
RefSeq; NP_990836.1; NM_205505.1.
UniGene; Gga.1480; -.
UniGene; Gga.6380; -.
ProteinModelPortal; P11029; -.
SMR; P11029; -.
BioGrid; 676751; 1.
PRIDE; P11029; -.
GeneID; 396504; -.
KEGG; gga:396504; -.
CTD; 31; -.
HOVERGEN; HBG005371; -.
InParanoid; P11029; -.
KO; K11262; -.
PhylomeDB; P11029; -.
SABIO-RK; P11029; -.
UniPathway; UPA00655; UER00711.
PRO; PR:P11029; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0005737; C:cytoplasm; TAS:AgBase.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:AgBase.
GO; GO:0005524; F:ATP binding; IDA:AgBase.
GO; GO:0009374; F:biotin binding; IDA:AgBase.
GO; GO:0004075; F:biotin carboxylase activity; IDA:AgBase.
GO; GO:0050692; F:DBD domain binding; IDA:AgBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005102; F:receptor binding; TAS:AgBase.
GO; GO:0032810; F:sterol response element binding; TAS:AgBase.
GO; GO:0046966; F:thyroid hormone receptor binding; TAS:AgBase.
GO; GO:0006633; P:fatty acid biosynthetic process; IDA:AgBase.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IDA:AgBase.
GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:AgBase.
GO; GO:0065008; P:regulation of biological quality; IDA:AgBase.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IDA:AgBase.
GO; GO:0009743; P:response to carbohydrate; IDA:AgBase.
GO; GO:0070542; P:response to fatty acid; TAS:AgBase.
GO; GO:0097066; P:response to thyroid hormone; IDA:AgBase.
GO; GO:0006810; P:transport; TAS:AgBase.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR013537; AcCoA_COase_cen.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR001882; Biotin_BS.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR029045; ClpP/crotonase-like_dom.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom.
InterPro; IPR011054; Rudment_hybrid_motif.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF08326; ACC_central; 1.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF01039; Carboxyl_trans; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52096; SSF52096; 2.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00188; BIOTIN; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS50989; COA_CT_CTER; 1.
PROSITE; PS50980; COA_CT_NTER; 1.
PROSITE; PS00866; CPSASE_1; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Biotin; Complete proteome; Cytoplasm;
Direct protein sequencing; Fatty acid biosynthesis;
Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 2324 Acetyl-CoA carboxylase.
/FTId=PRO_0000146768.
DOMAIN 117 618 Biotin carboxylation.
DOMAIN 275 466 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 745 819 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1553 1891 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 1895 2211 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 315 320 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1553 2211 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
ACT_SITE 441 441 {ECO:0000250}.
METAL 424 424 Manganese 1. {ECO:0000250}.
METAL 437 437 Manganese 1. {ECO:0000250}.
METAL 437 437 Manganese 2. {ECO:0000250}.
METAL 439 439 Manganese 2. {ECO:0000250}.
BINDING 1800 1800 Coenzyme A. {ECO:0000250}.
BINDING 2104 2104 Coenzyme A. {ECO:0000250}.
BINDING 2106 2106 Coenzyme A. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine. {ECO:0000269|Ref.3}.
MOD_RES 78 78 Phosphoserine. {ECO:0000250}.
MOD_RES 80 80 Phosphoserine. {ECO:0000250}.
MOD_RES 786 786 N6-biotinyllysine. {ECO:0000255|PROSITE-
ProRule:PRU01066,
ECO:0000269|PubMed:2893793}.
MOD_RES 1193 1193 Phosphoserine. {ECO:0000250}.
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


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