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P11029 (ACAC_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA carboxylase

Short name=ACC
EC=6.4.1.2

Including the following 1 domains:

  1. Biotin carboxylase
    EC=6.3.4.14
Gene names
Name:ACAC
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length2324 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

Cofactor

Biotin By similarity.

Binds 2 manganese ions per subunit By similarity.

Enzyme regulation

By phosphorylation.

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.

Subcellular location

Cytoplasm.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23242324Acetyl-CoA carboxylase
PRO_0000146768

Regions

Domain117 – 618502Biotin carboxylation
Domain275 – 466192ATP-grasp
Domain752 – 81867Biotinyl-binding
Domain1675 – 2171497Carboxyltransferase
Nucleotide binding315 – 3206ATP Potential

Sites

Active site4411 By similarity
Metal binding4241Manganese 1 By similarity
Metal binding4371Manganese 1 By similarity
Metal binding4371Manganese 2 By similarity
Metal binding4391Manganese 2 By similarity
Binding site18001Coenzyme A By similarity
Binding site21041Coenzyme A By similarity
Binding site21061Coenzyme A By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.3
Modified residue781Phosphoserine By similarity
Modified residue801Phosphoserine By similarity
Modified residue7861N6-biotinyllysine
Modified residue11931Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P11029 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 3F1C541F01BBBEF6

FASTA2,324262,720
        10         20         30         40         50         60 
MEESSQPAKP LEMNPHSRFI IGSVSEDNSE DETSSLVKLD LLEEKERSLS PVSVCSDSLS 

        70         80         90        100        110        120 
DLGLPSAQDG LANHMRPSMS GLHLVKQGRD RKKVDVQRDF TVASPAEFVT RFGGNRVIEK 

       130        140        150        160        170        180 
VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG 

       190        200        210        220        230        240 
GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLHKNGIAFM GPPSQAMWAL 

       250        260        270        280        290        300 
GDKIASSIVA QTAGIPTLPW NGSGLRVDWQ ENDLQKRILN VPQELYEKGY VKDADDGLRA 

       310        320        330        340        350        360 
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV 

       370        380        390        400        410        420 
QILADQYGNA ISLFGRDCSV QRRHQKIIEE APASIATSVV FEHMEQCAVK LAKMVGYVSA 

       430        440        450        460        470        480 
GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL HRIKDIRVMY 

       490        500        510        520        530        540 
GVSPWGDGSI DFENSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY 

       550        560        570        580        590        600 
FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET 

       610        620        630        640        650        660 
ESFQQNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSFRNSVSN FLHSLERGQV 

       670        680        690        700        710        720 
LPAHTLLNTV DVELIYEGRK YVLKVTRQSP NSYVVIMNSS CVEVDVHRLS DGGLLLSYDG 

       730        740        750        760        770        780 
SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSILRSPSAG KLIQYVVEDG GHVFAGQCFA 

       790        800        810        820        830        840 
EIEVMKMVMT LTAGESGCIH YVKRPGAVLD PGCVIAKLQL DDPSRVQQAE LHTGTLPQIQ 

       850        860        870        880        890        900 
STALRGEKLH RIFHYVLDNL VNVMNGYCLP EPYFSSKVKG WVERLMKTLR DPSLPLLELQ 

       910        920        930        940        950        960 
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV 

       970        980        990       1000       1010       1020 
FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLKVETQ FQHGHYDKCV FALREENKSD 

      1030       1040       1050       1060       1070       1080 
MNAVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELI NILTELTQLS KTTNAKVALR 

      1090       1100       1110       1120       1130       1140 
ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH 

      1150       1160       1170       1180       1190       1200 
SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RMSFSSNLNH 

      1210       1220       1230       1240       1250       1260 
YGMVHVASVS DVLLDNSFTP PCQRMGGMVS FRTFEDFVRI FDEVMSCFCD SPPQSPTFPE 

      1270       1280       1290       1300       1310       1320 
AGHASLYDED KAAREEPIHI LNVAIKTDGD VDDDGLAAMF REFTQSKKSV LIEHGIRRLT 

      1330       1340       1350       1360       1370       1380 
FLVAQKREFP KFFTFRARDK FEEDRIYRHL EPALAFQLEL NRMRNFDLTA IPCANHKMHL 

      1390       1400       1410       1420       1430       1440 
YLGAAKVEVG TEVTDYRFFV RAIIRHSDLV TKEASFEYLQ NEGERLLLEA MDELEVAFNN 

      1450       1460       1470       1480       1490       1500 
TNVRTDCNHI FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEL KINIRLTPTG 

      1510       1520       1530       1540       1550       1560 
KAIPIRLFLT NESGYYLDIS LYKEVTDSRT GQIMFQAYGD KQGPLHGMLI NTPYVTKDLL 

      1570       1580       1590       1600       1610       1620 
QSKRFQAQSL GTSYVYDIPE MFRQSLIKLW DSMNEHAFLP TPPLPSDILT YTELVLDDQG 

      1630       1640       1650       1660       1670       1680 
QLVHMNRLPG GNEIGMVAWK MTLKTPEYPE GRDIIVIGND ITYRIGSFGP QEDVLFLRAS 

      1690       1700       1710       1720       1730       1740 
ELARTHGIPR IYVAANSGAR IGLAEEIRHM FHVAWEDPDD PYKGYKYLYL TPQDYKKVSA 

      1750       1760       1770       1780       1790       1800 
LNSVHCEHVE DNGESRYKIT DIIGKEDGLG IENLRGSGMI AGESSLAYES IITINLVTCR 

      1810       1820       1830       1840       1850       1860 
AIGIGAYLVR LGQRTIQVEN SHIILTGCGA LNKVLGREVY TSNNQLGGIQ IMHNNGVTHG 

      1870       1880       1890       1900       1910       1920 
TVCDDFEGVY TILLWLSYMP KSVYSPVPIL KVKDPIDRTI DFVPTKTPYD PRWMLAGRPN 

      1930       1940       1950       1960       1970       1980 
PSQKGQWQSG FFDNGSFLEI MQPWAQTVVV GRARLGGIPV GVVAVETRTV ELSIPADPAN 

      1990       2000       2010       2020       2030       2040 
LDSEAKIIQQ AGQVWFPDSA FKTAQAINDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF 

      2050       2060       2070       2080       2090       2100 
GAYIVDGLRE YRQPVLIYIP PQAELRGGSW AVIDPTINPR HMEMYADRES RGGILEPEGT 

      2110       2120       2130       2140       2150       2160 
VEIKFRRKDL VKTMRRVDPV YMRLAERLGT PELSAADRKD LESKLKEREE FLIPIYHQVA 

      2170       2180       2190       2200       2210       2220 
MQFADLHDTP GRMQEKGAIT DILDWKTSRT FFYWRLRRLL LEDVVKKKIH DANPELTDGQ 

      2230       2240       2250       2260       2270       2280 
IQAMLRRWFV EVEGTVKAYL WDSNKDLVEW LEKQLMEEEG VRSVVDENIK YISRDYILKQ 

      2290       2300       2310       2320 
IRSLVQANPE VAMDSIVHMT QHISPTQRAE IVRILSTMDS PSST 

« Hide

References

[1]"Primary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence."
Takai T., Yokoyama C., Wada K., Tanabe T.
J. Biol. Chem. 263:2651-2657(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Primary structure of the biotin-binding site of chicken liver acetyl-CoA carboxylase."
Takai T., Wada K., Tanabe T.
FEBS Lett. 212:98-102(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 493-820.
Tissue: Liver.
[3]Bienvenut W.V., Black E.J., Gillespie D.A.
Submitted (JAN-2007) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03541 mRNA. Translation: AAA48701.1.
X05019 mRNA. Translation: CAA28675.1.
PIRA29924.
RefSeqNP_990836.1. NM_205505.1.
UniGeneGga.1480.

3D structure databases

ProteinModelPortalP11029.
SMRP11029. Positions 97-616, 742-834, 1551-2285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676751. 1 interaction.

Proteomic databases

PaxDbP11029.
PRIDEP11029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396504.
KEGGgga:396504.

Organism-specific databases

CTD31.

Phylogenomic databases

eggNOGCOG0511.
HOVERGENHBG005371.
KOK11262.
PhylomeDBP11029.

Enzyme and pathway databases

SABIO-RKP11029.
UniPathwayUPA00655; UER00711.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.226.10. 3 hits.
InterProIPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF08326. ACC_central. 1 hit.
PF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816543.
PROP11029.

Entry information

Entry nameACAC_CHICK
AccessionPrimary (citable) accession number: P11029
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 11, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways