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Q9TTS3

- ACACA_BOVIN

UniProt

Q9TTS3 - ACACA_BOVIN

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Protein

Acetyl-CoA carboxylase 1

Gene

ACACA

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).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

Protein has several cofactor binding sites:
  • biotinBy similarityNote: Biotin.By similarity
  • Mn2+By similarityNote: 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
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 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 similarityPROSITE-ProRule annotation
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
Domaini745 – 81975Biotinyl-bindingPROSITE-ProRule annotationAdd
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.CuratedPROSITE-ProRule annotation
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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        10         20         30         40         50
MDEPSSLAKP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS
60 70 80 90 100
PASVSSDTLS DLGISSLQDG LALHMRSSMS GLHLVKQGRD RKKIDSQRDF
110 120 130 140 150
TVASPAEFVT RFGGNKVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA
160 170 180 190 200
IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI
210 220 230 240 250
PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL GDKIASSIVA
260 270 280 290 300
QTAGIPTLPW SGSGLCVDWH ENDFSKRILN VPQELYEKGY VKDVDDGLKA
310 320 330 340 350
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR
360 370 380 390 400
LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APAAIATPAV
410 420 430 440 450
FEHMEQCAVK LARMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE
460 470 480 490 500
MVADVNLPAA QLQIAMGIPL YRIKDIRMMY GVSPWGDAPI DFENSAHVPC
510 520 530 540 550
PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH
560 570 580 590 600
EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
610 620 630 640 650
ESFQLNRIGT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSISN
660 670 680 690 700
FLHSLERGQV LTAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS
710 720 730 740 750
CVEVDVHRLS DGGLLLSYDV SSYTTYMKEE VDRYRITIGN KTCVFEKEND
760 770 780 790 800
PSVLRSPSAG KLIQYIVEDG GHVFAGQCYA EIEVMKMVMT LTAAESGCIH
810 820 830 840 850
YVKRPGAALD PGCVIAKMQL DNPSKVQQAE LHTGSLPRIQ STALRGEKLH
860 870 880 890 900
RVFHYVLDNL VNVMNGYCLP DPFFSSRVKD WVERLMKTLR DPSLPLLELQ
910 920 930 940 950
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA
960 970 980 990 1000
TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ
1010 1020 1030 1040 1050
FQNGHYDKCV FALREENKSD MNTVLNYIFS HAQVTRKNLL VTMLIDQLCG
1060 1070 1080 1090 1100
RGPTLTDELL NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRLNQV
1110 1120 1130 1140 1150
ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL
1160 1170 1180 1190 1200
EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM
1210 1220 1230 1240 1250
SFSSNLNHYG MTHVASVSDV LLDNAFTPPC QRMGGMVSFR TFEDFVRIFD
1260 1270 1280 1290 1300
EVMGCFCDSP PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE
1310 1320 1330 1340 1350
DDSLAAMFRE FTQQNKATLV EHGIRRLTFL VAQKDFRKQV NYEVDQRFHR
1360 1370 1380 1390 1400
EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ LELNRMRNFD LTAIPCANHK
1410 1420 1430 1440 1450
MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE YLQNEGERLL
1460 1470 1480 1490 1500
LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG
1510 1520 1530 1540 1550
SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD
1560 1570 1580 1590 1600
SRTAQIMFQA YGDKQGPLHG MLINTPYVTK DQLQSKRFQA QSLGTTYIYD
1610 1620 1630 1640 1650
IPEMFRQSLI KLWESMSSQA FLPPPPLPSD ILTYTELVLD DQGQLVHMNR
1660 1670 1680 1690 1700
LPGGNEIGMV AWKMTLKSPE YPDGRDIIVI GNDITYRIGS FGPQEDLLFL
1710 1720 1730 1740 1750
RASELARAEG IPRIYVAANS GARIGLAEEI RHMFHVAWVD PEDPYKGYKY
1760 1770 1780 1790 1800
LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GLGAENLRGS
1810 1820 1830 1840 1850
GMIAGESSLA YDEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG
1860 1870 1880 1890 1900
AGALNKVLGR EVYTSNNQLG GIQIMHNNGV THSTVCDDFE GVFTVLHWLS
1910 1920 1930 1940 1950
YMPKSVYSSV PLLNSKDPID RVIEFVPTKA PYDPRWMLAG RPHPTQKGQW
1960 1970 1980 1990 2000
LSGFFDYGSF SEIMQPWAQT VVVGRARLGG IPVGVVAVET RTVELSIPAD
2010 2020 2030 2040 2050
PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL MVFANWRGFS
2060 2070 2080 2090 2100
GGMKDMYDQV LKFGAYIVDG LRECSQPVMV YIPPQAELRG GSWVVIDPTI
2110 2120 2130 2140 2150
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER
2160 2170 2180 2190 2200
LGTPELSVAE RKELESKLKE REEFLLPIYH QVAVQFADLH DTPGRMQEKG
2210 2220 2230 2240 2250
VINDILDWKT SRTFFYWRLR RLLLEDLVKK KIHNANPELT DGQIQAMLRR
2260 2270 2280 2290 2300
WFVEVEGTVK AYVWDNNKDL VEWLEKQLTE EDGVRSVIEE NIKYISRDYV
2310 2320 2330 2340
LKQIRSLVQA NPEVAMDSIV HMTQHISPTQ RAEVVRILST MDSPST
Length:2,346
Mass (Da):265,303
Last modified:May 1, 2000 - v1
Checksum:i32886C5D03EEAE0E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 113 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