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Q9TTS3

- ACACA_BOVIN

UniProt

Q9TTS3 - ACACA_BOVIN

Protein

Acetyl-CoA carboxylase 1

Gene

ACACA

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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 By similarity.By similarity

    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 By similarity. Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization By similarity.By similarity

    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 sitei1823 – 18231Coenzyme ABy similarity
    Binding sitei2127 – 21271Coenzyme ABy similarity
    Binding sitei2129 – 21291Coenzyme ABy similarity

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. acetyl-CoA metabolic process Source: UniProtKB
    2. fatty acid biosynthetic process Source: UniProtKB
    3. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
    4. protein homotetramerization Source: UniProtKB

    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

    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA carboxylase 1 (EC:6.4.1.2)
    Short name:
    ACC1
    Alternative name(s):
    ACC-alpha
    Including the following 1 domains:
    Biotin carboxylase (EC:6.3.4.14)
    Gene namesi
    Name:ACACA
    Synonyms:ACAC, ACCA
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23462346Acetyl-CoA carboxylase 1PRO_0000146763Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei5 – 51PhosphoserineBy similarity
    Modified residuei23 – 231PhosphoserineBy similarity
    Modified residuei25 – 251PhosphoserineBy similarity
    Modified residuei29 – 291PhosphoserineBy similarity
    Modified residuei53 – 531PhosphoserineBy similarity
    Modified residuei78 – 781PhosphoserineBy similarity
    Modified residuei80 – 801Phosphoserine; by AMPKBy similarity
    Modified residuei786 – 7861N6-biotinyllysineBy similarity
    Modified residuei1201 – 12011PhosphoserineBy similarity
    Modified residuei1216 – 12161PhosphoserineBy similarity
    Modified residuei1263 – 12631PhosphoserineBy similarity
    Modified residuei1334 – 13341N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylation on Ser-1263 is required for interaction with BRCA1.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9TTS3.
    PRIDEiQ9TTS3.

    Interactioni

    Subunit structurei

    Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9TTS3.
    SMRiQ9TTS3. Positions 97-616, 742-834, 1574-2308.
    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
    Domaini1698 – 2194497CarboxyltransferaseAdd
    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.
    HOGENOMiHOG000214115.
    HOVERGENiHBG005371.
    InParanoidiQ9TTS3.
    KOiK11262.

    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.

    Q9TTS3-1 [UniParc]FASTAAdd to Basket

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    MDEPSSLAKP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS     50
    PASVSSDTLS DLGISSLQDG LALHMRSSMS GLHLVKQGRD RKKIDSQRDF 100
    TVASPAEFVT RFGGNKVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA 150
    IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI 200
    PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL GDKIASSIVA 250
    QTAGIPTLPW SGSGLCVDWH ENDFSKRILN VPQELYEKGY VKDVDDGLKA 300
    AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR 350
    LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APAAIATPAV 400
    FEHMEQCAVK LARMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE 450
    MVADVNLPAA QLQIAMGIPL YRIKDIRMMY GVSPWGDAPI DFENSAHVPC 500
    PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH 550
    EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET 600
    ESFQLNRIGT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSISN 650
    FLHSLERGQV LTAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS 700
    CVEVDVHRLS DGGLLLSYDV SSYTTYMKEE VDRYRITIGN KTCVFEKEND 750
    PSVLRSPSAG KLIQYIVEDG GHVFAGQCYA EIEVMKMVMT LTAAESGCIH 800
    YVKRPGAALD PGCVIAKMQL DNPSKVQQAE LHTGSLPRIQ STALRGEKLH 850
    RVFHYVLDNL VNVMNGYCLP DPFFSSRVKD WVERLMKTLR DPSLPLLELQ 900
    DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA 950
    TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ 1000
    FQNGHYDKCV FALREENKSD MNTVLNYIFS HAQVTRKNLL VTMLIDQLCG 1050
    RGPTLTDELL NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRLNQV 1100
    ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL 1150
    EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM 1200
    SFSSNLNHYG MTHVASVSDV LLDNAFTPPC QRMGGMVSFR TFEDFVRIFD 1250
    EVMGCFCDSP PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE 1300
    DDSLAAMFRE FTQQNKATLV EHGIRRLTFL VAQKDFRKQV NYEVDQRFHR 1350
    EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ LELNRMRNFD LTAIPCANHK 1400
    MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE YLQNEGERLL 1450
    LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG 1500
    SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD 1550
    SRTAQIMFQA YGDKQGPLHG MLINTPYVTK DQLQSKRFQA QSLGTTYIYD 1600
    IPEMFRQSLI KLWESMSSQA FLPPPPLPSD ILTYTELVLD DQGQLVHMNR 1650
    LPGGNEIGMV AWKMTLKSPE YPDGRDIIVI GNDITYRIGS FGPQEDLLFL 1700
    RASELARAEG IPRIYVAANS GARIGLAEEI RHMFHVAWVD PEDPYKGYKY 1750
    LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GLGAENLRGS 1800
    GMIAGESSLA YDEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG 1850
    AGALNKVLGR EVYTSNNQLG GIQIMHNNGV THSTVCDDFE GVFTVLHWLS 1900
    YMPKSVYSSV PLLNSKDPID RVIEFVPTKA PYDPRWMLAG RPHPTQKGQW 1950
    LSGFFDYGSF SEIMQPWAQT VVVGRARLGG IPVGVVAVET RTVELSIPAD 2000
    PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL MVFANWRGFS 2050
    GGMKDMYDQV LKFGAYIVDG LRECSQPVMV YIPPQAELRG GSWVVIDPTI 2100
    NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER 2150
    LGTPELSVAE RKELESKLKE REEFLLPIYH QVAVQFADLH DTPGRMQEKG 2200
    VINDILDWKT SRTFFYWRLR RLLLEDLVKK KIHNANPELT DGQIQAMLRR 2250
    WFVEVEGTVK AYVWDNNKDL VEWLEKQLTE EDGVRSVIEE NIKYISRDYV 2300
    LKQIRSLVQA NPEVAMDSIV HMTQHISPTQ RAEVVRILST MDSPST 2346
    Length:2,346
    Mass (Da):265,303
    Last modified:May 1, 2000 - v1
    Checksum:i32886C5D03EEAE0E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132890 mRNA. Translation: CAB56826.1.
    RefSeqiNP_776649.1. NM_174224.2.
    UniGeneiBt.88312.

    Genome annotation databases

    GeneIDi281590.
    KEGGibta:281590.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132890 mRNA. Translation: CAB56826.1 .
    RefSeqi NP_776649.1. NM_174224.2.
    UniGenei Bt.88312.

    3D structure databases

    ProteinModelPortali Q9TTS3.
    SMRi Q9TTS3. Positions 97-616, 742-834, 1574-2308.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q9TTS3.
    PRIDEi Q9TTS3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 281590.
    KEGGi bta:281590.

    Organism-specific databases

    CTDi 31.

    Phylogenomic databases

    eggNOGi COG0511.
    HOGENOMi HOG000214115.
    HOVERGENi HBG005371.
    InParanoidi Q9TTS3.
    KOi K11262.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .

    Miscellaneous databases

    NextBioi 20805535.

    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. "Genomic distribution of three promoters of the bovine gene encoding acetyl-CoA carboxylase alpha and evidence that the nutritionally regulated promoter I contains a repressive element different from that in rat."
      Mao J., Marcos S., Davis S.K., Burzlaff J., Seyfert H.-M.
      Biochem. J. 358:127-135(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.

    Entry informationi

    Entry nameiACACA_BOVIN
    AccessioniPrimary (citable) accession number: Q9TTS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 112 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

    Allosteric enzyme, Complete proteome, 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