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P11029

- ACAC_CHICK

UniProt

P11029 - ACAC_CHICK

Protein

Acetyl-CoA carboxylase

Gene

ACAC

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    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 activityi

    ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
    ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

    Cofactori

    Biotin.By similarity
    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    By phosphorylation.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi424 – 4241Manganese 1By similarity
    Metal bindingi437 – 4371Manganese 1By similarity
    Metal bindingi437 – 4371Manganese 2By similarity
    Metal bindingi439 – 4391Manganese 2By similarity
    Active sitei441 – 4411By similarity
    Binding sitei1800 – 18001Coenzyme ABy similarity
    Binding sitei2104 – 21041Coenzyme ABy similarity
    Binding sitei2106 – 21061Coenzyme ABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi315 – 3206ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA carboxylase activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW
    3. biotin carboxylase activity Source: UniProtKB-EC
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW
    2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKP11029.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA carboxylase (EC:6.4.1.2)
    Short name:
    ACC
    Including the following 1 domains:
    Biotin carboxylase (EC:6.3.4.14)
    Gene namesi
    Name:ACAC
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23242324Acetyl-CoA carboxylasePRO_0000146768Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei78 – 781PhosphoserineBy similarity
    Modified residuei80 – 801PhosphoserineBy similarity
    Modified residuei786 – 7861N6-biotinyllysine1 Publication
    Modified residuei1193 – 11931PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP11029.
    PRIDEiP11029.

    Interactioni

    Protein-protein interaction databases

    BioGridi676751. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP11029.
    SMRiP11029. Positions 97-616, 742-834, 1551-2285.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini117 – 618502Biotin carboxylationAdd
    BLAST
    Domaini275 – 466192ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini752 – 81867Biotinyl-bindingAdd
    BLAST
    Domaini1675 – 2171497CarboxyltransferaseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated
    Contains 1 carboxyltransferase domain.Curated

    Phylogenomic databases

    eggNOGiCOG0511.
    HOVERGENiHBG005371.
    KOiK11262.
    PhylomeDBiP11029.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProiIPR013537. 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]
    PfamiPF08326. 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]
    SMARTiSM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEiPS50975. 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]

    Sequencei

    Sequence statusi: Complete.

    P11029-1 [UniParc]FASTAAdd to Basket

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    MEESSQPAKP LEMNPHSRFI IGSVSEDNSE DETSSLVKLD LLEEKERSLS     50
    PVSVCSDSLS DLGLPSAQDG LANHMRPSMS GLHLVKQGRD RKKVDVQRDF 100
    TVASPAEFVT RFGGNRVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA 150
    IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI 200
    PVQAVWAGWG HASENPKLPE LLHKNGIAFM GPPSQAMWAL GDKIASSIVA 250
    QTAGIPTLPW NGSGLRVDWQ ENDLQKRILN VPQELYEKGY VKDADDGLRA 300
    AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR 350
    LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APASIATSVV 400
    FEHMEQCAVK LAKMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE 450
    MVADVNLPAA QLQIAMGIPL HRIKDIRVMY GVSPWGDGSI DFENSAHVPC 500
    PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH 550
    EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET 600
    ESFQQNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSFRNSVSN 650
    FLHSLERGQV LPAHTLLNTV DVELIYEGRK YVLKVTRQSP NSYVVIMNSS 700
    CVEVDVHRLS DGGLLLSYDG SSYTTYMKEE VDRYRITIGN KTCVFEKEND 750
    PSILRSPSAG KLIQYVVEDG GHVFAGQCFA EIEVMKMVMT LTAGESGCIH 800
    YVKRPGAVLD PGCVIAKLQL DDPSRVQQAE LHTGTLPQIQ STALRGEKLH 850
    RIFHYVLDNL VNVMNGYCLP EPYFSSKVKG WVERLMKTLR DPSLPLLELQ 900
    DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA 950
    TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLKVETQ 1000
    FQHGHYDKCV FALREENKSD MNAVLNYIFS HAQVTKKNLL VTMLIDQLCG 1050
    RDPTLTDELI NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRHNQV 1100
    ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL 1150
    EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RMSFSSNLNH 1200
    YGMVHVASVS DVLLDNSFTP PCQRMGGMVS FRTFEDFVRI FDEVMSCFCD 1250
    SPPQSPTFPE AGHASLYDED KAAREEPIHI LNVAIKTDGD VDDDGLAAMF 1300
    REFTQSKKSV LIEHGIRRLT FLVAQKREFP KFFTFRARDK FEEDRIYRHL 1350
    EPALAFQLEL NRMRNFDLTA IPCANHKMHL YLGAAKVEVG TEVTDYRFFV 1400
    RAIIRHSDLV TKEASFEYLQ NEGERLLLEA MDELEVAFNN TNVRTDCNHI 1450
    FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEL KINIRLTPTG 1500
    KAIPIRLFLT NESGYYLDIS LYKEVTDSRT GQIMFQAYGD KQGPLHGMLI 1550
    NTPYVTKDLL QSKRFQAQSL GTSYVYDIPE MFRQSLIKLW DSMNEHAFLP 1600
    TPPLPSDILT YTELVLDDQG QLVHMNRLPG GNEIGMVAWK MTLKTPEYPE 1650
    GRDIIVIGND ITYRIGSFGP QEDVLFLRAS ELARTHGIPR IYVAANSGAR 1700
    IGLAEEIRHM FHVAWEDPDD PYKGYKYLYL TPQDYKKVSA LNSVHCEHVE 1750
    DNGESRYKIT DIIGKEDGLG IENLRGSGMI AGESSLAYES IITINLVTCR 1800
    AIGIGAYLVR LGQRTIQVEN SHIILTGCGA LNKVLGREVY TSNNQLGGIQ 1850
    IMHNNGVTHG TVCDDFEGVY TILLWLSYMP KSVYSPVPIL KVKDPIDRTI 1900
    DFVPTKTPYD PRWMLAGRPN PSQKGQWQSG FFDNGSFLEI MQPWAQTVVV 1950
    GRARLGGIPV GVVAVETRTV ELSIPADPAN LDSEAKIIQQ AGQVWFPDSA 2000
    FKTAQAINDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF GAYIVDGLRE 2050
    YRQPVLIYIP PQAELRGGSW AVIDPTINPR HMEMYADRES RGGILEPEGT 2100
    VEIKFRRKDL VKTMRRVDPV YMRLAERLGT PELSAADRKD LESKLKEREE 2150
    FLIPIYHQVA MQFADLHDTP GRMQEKGAIT DILDWKTSRT FFYWRLRRLL 2200
    LEDVVKKKIH DANPELTDGQ IQAMLRRWFV EVEGTVKAYL WDSNKDLVEW 2250
    LEKQLMEEEG VRSVVDENIK YISRDYILKQ IRSLVQANPE VAMDSIVHMT 2300
    QHISPTQRAE IVRILSTMDS PSST 2324
    Length:2,324
    Mass (Da):262,720
    Last modified:July 1, 1989 - v1
    Checksum:i3F1C541F01BBBEF6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03541 mRNA. Translation: AAA48701.1.
    X05019 mRNA. Translation: CAA28675.1.
    PIRiA29924.
    RefSeqiNP_990836.1. NM_205505.1.
    UniGeneiGga.1480.

    Genome annotation databases

    GeneIDi396504.
    KEGGigga:396504.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03541 mRNA. Translation: AAA48701.1 .
    X05019 mRNA. Translation: CAA28675.1 .
    PIRi A29924.
    RefSeqi NP_990836.1. NM_205505.1.
    UniGenei Gga.1480.

    3D structure databases

    ProteinModelPortali P11029.
    SMRi P11029. Positions 97-616, 742-834, 1551-2285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 676751. 1 interaction.

    Proteomic databases

    PaxDbi P11029.
    PRIDEi P11029.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396504.
    KEGGi gga:396504.

    Organism-specific databases

    CTDi 31.

    Phylogenomic databases

    eggNOGi COG0511.
    HOVERGENi HBG005371.
    KOi K11262.
    PhylomeDBi P11029.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .
    SABIO-RK P11029.

    Miscellaneous databases

    NextBioi 20816543.
    PROi P11029.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProi IPR013537. 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 ]
    Pfami PF08326. 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 ]
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEi PS50975. 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 ]
    ProtoNeti Search...

    Publicationsi

    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, BIOTINYLATION AT LYS-786.
      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
      Tissue: B-cell lymphoma.

    Entry informationi

    Entry nameiACAC_CHICK
    AccessioniPrimary (citable) accession number: P11029
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3