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Q9TTS3

- ACACA_BOVIN

UniProt

Q9TTS3 - ACACA_BOVIN

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Protein
Acetyl-CoA carboxylase 1
Gene
ACACA, ACAC, ACCA
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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.

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi424 – 4241Manganese 1 By similarity
Metal bindingi437 – 4371Manganese 1 By similarity
Metal bindingi437 – 4371Manganese 2 By similarity
Metal bindingi439 – 4391Manganese 2 By similarity
Active sitei441 – 4411 By similarity
Binding sitei1823 – 18231Coenzyme A By similarity
Binding sitei2127 – 21271Coenzyme A By similarity
Binding sitei2129 – 21291Coenzyme A By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi315 – 3206ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. acetyl-CoA carboxylase activity Source: UniProtKB
  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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei5 – 51Phosphoserine By similarity
Modified residuei23 – 231Phosphoserine By similarity
Modified residuei25 – 251Phosphoserine By similarity
Modified residuei29 – 291Phosphoserine By similarity
Modified residuei53 – 531Phosphoserine By similarity
Modified residuei78 – 781Phosphoserine By similarity
Modified residuei80 – 801Phosphoserine; by AMPK By similarity
Modified residuei786 – 7861N6-biotinyllysine By similarity
Modified residuei1201 – 12011Phosphoserine By similarity
Modified residuei1216 – 12161Phosphoserine By similarity
Modified residuei1263 – 12631Phosphoserine By similarity
Modified residuei1334 – 13341N6-acetyllysine By 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.

Structurei

3D structure databases

ProteinModelPortaliQ9TTS3.
SMRiQ9TTS3. Positions 97-616, 742-834, 1574-2308.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 618502Biotin carboxylation
Add
BLAST
Domaini275 – 466192ATP-grasp
Add
BLAST
Domaini752 – 81867Biotinyl-binding
Add
BLAST
Domaini1698 – 2194497Carboxyltransferase
Add
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.

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: June 11, 2014
This is version 111 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

Similar proteinsi