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Database: UniProt
Entry: P11029
LinkDB: P11029
Original site: P11029 
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   10-APR-2019, entry version 145.
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;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP   BIOTINYLATION AT LYS-786.
RC   TISSUE=Liver;
RX   PubMed=2893793;
RA   Takai T., Yokoyama C., Wada K., Tanabe T.;
RT   "Primary structure of chicken liver acetyl-CoA carboxylase deduced
RT   from 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-
RT   CoA 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,
RP   AND 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
CC       of long-chain fatty acids. Carries out three functions: biotin
CC       carboxyl carrier protein, biotin carboxylase and
CC       carboxyltransferase. {ECO:0000250|UniProtKB:Q13085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         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] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, 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
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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   UniGene; Gga.1480; -.
DR   UniGene; Gga.6380; -.
DR   ProteinModelPortal; 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   HOVERGEN; HBG005371; -.
DR   InParanoid; P11029; -.
DR   KO; K11262; -.
DR   PhylomeDB; P11029; -.
DR   SABIO-RK; P11029; -.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:P11029; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005623; C:cell; IDA:AgBase.
DR   GO; GO:0005737; C:cytoplasm; TAS:AgBase.
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:DBD domain binding; IDA:AgBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; TAS:AgBase.
DR   GO; GO:0032810; F:sterol response element binding; TAS:AgBase.
DR   GO; GO:0046966; F:thyroid hormone receptor 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; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1   2324       Acetyl-CoA carboxylase.
FT                                /FTId=PRO_0000146768.
FT   DOMAIN      117    618       Biotin carboxylation.
FT   DOMAIN      275    466       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      745    819       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN     1553   1891       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01136}.
FT   DOMAIN     1895   2211       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01137}.
FT   NP_BIND     315    320       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION     1553   2211       Carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01138}.
FT   ACT_SITE    441    441       {ECO:0000250}.
FT   METAL       424    424       Manganese 1. {ECO:0000250}.
FT   METAL       437    437       Manganese 1. {ECO:0000250}.
FT   METAL       437    437       Manganese 2. {ECO:0000250}.
FT   METAL       439    439       Manganese 2. {ECO:0000250}.
FT   BINDING    1800   1800       Coenzyme A. {ECO:0000250}.
FT   BINDING    2104   2104       Coenzyme A. {ECO:0000250}.
FT   BINDING    2106   2106       Coenzyme A. {ECO:0000250}.
FT   MOD_RES       1      1       N-acetylmethionine. {ECO:0000269|Ref.3}.
FT   MOD_RES      78     78       Phosphoserine. {ECO:0000250}.
FT   MOD_RES      80     80       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     786    786       N6-biotinyllysine. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066,
FT                                ECO:0000269|PubMed:2893793}.
FT   MOD_RES    1193   1193       Phosphoserine. {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
//
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