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Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene

ACAT1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Plays a major role in ketone body metabolism.By similarity

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

Enzyme regulationi

Activated by potassium ions, but not sodium ions.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei121Acyl-thioester intermediateBy similarity1
Metal bindingi214PotassiumBy similarity1
Binding sitei214Coenzyme ABy similarity1
Binding sitei258Coenzyme ABy similarity1
Metal bindingi275Potassium; via carbonyl oxygenBy similarity1
Metal bindingi276Potassium; via carbonyl oxygenBy similarity1
Metal bindingi278Potassium; via carbonyl oxygenBy similarity1
Binding sitei279Coenzyme ABy similarity1
Metal bindingi376Potassium; via carbonyl oxygenBy similarity1
Active sitei380Proton acceptorPROSITE-ProRule annotation1
Active sitei408Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
LigandMetal-binding, Potassium

Enzyme and pathway databases

ReactomeiR-BTA-70895 Branched-chain amino acid catabolism
R-BTA-77108 Utilization of Ketone Bodies
R-BTA-77111 Synthesis of Ketone Bodies

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase, mitochondrial (EC:2.3.1.9)
Alternative name(s):
Acetoacetyl-CoA thiolase
Gene namesi
Name:ACAT1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Organism-specific databases

VGNCiVGNC:25529 ACAT1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 28MitochondrionBy similarityAdd BLAST28
ChainiPRO_000035627429 – 422Acetyl-CoA acetyltransferase, mitochondrialAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei61N6-acetyllysine; alternateBy similarity1
Modified residuei61N6-succinyllysine; alternateBy similarity1
Modified residuei73N6-succinyllysineBy similarity1
Modified residuei169N6-acetyllysine; alternateBy similarity1
Modified residuei169N6-succinyllysine; alternateBy similarity1
Modified residuei176N6-acetyllysine; alternateBy similarity1
Modified residuei176N6-succinyllysine; alternateBy similarity1
Modified residuei185N6-acetyllysine; alternateBy similarity1
Modified residuei185N6-succinyllysine; alternateBy similarity1
Modified residuei197N6-acetyllysine; alternateBy similarity1
Modified residuei197N6-succinyllysine; alternateBy similarity1
Modified residuei218N6-acetyllysine; alternateBy similarity1
Modified residuei218N6-succinyllysine; alternateBy similarity1
Modified residuei238N6-succinyllysineBy similarity1
Modified residuei240N6-acetyllysine; alternateBy similarity1
Modified residuei240N6-succinyllysine; alternateBy similarity1
Modified residuei246N6-acetyllysineBy similarity1
Modified residuei252N6-acetyllysineBy similarity1
Modified residuei258N6-acetyllysine; alternateBy similarity1
Modified residuei258N6-succinyllysine; alternateBy similarity1
Modified residuei261N6-succinyllysineBy similarity1
Modified residuei263N6-succinyllysineBy similarity1
Modified residuei333N6-acetyllysineBy similarity1

Post-translational modificationi

Succinylation at Lys-263, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ29RZ0
PeptideAtlasiQ29RZ0
PRIDEiQ29RZ0

Expressioni

Gene expression databases

BgeeiENSBTAG00000012885

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ29RZ0, 1 interactor
STRINGi9913.ENSBTAP00000017122

Structurei

3D structure databases

ProteinModelPortaliQ29RZ0
SMRiQ29RZ0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni253 – 255Coenzyme A bindingBy similarity3

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1390 Eukaryota
COG0183 LUCA
GeneTreeiENSGT00390000009412
HOGENOMiHOG000012238
HOVERGENiHBG003112
InParanoidiQ29RZ0
KOiK00626
OMAiWDVYNKF
OrthoDBiEOG091G09C6
TreeFamiTF300650

Family and domain databases

CDDicd00751 thiolase, 1 hit
Gene3Di3.40.47.10, 4 hits
InterProiView protein in InterPro
IPR002155 Thiolase
IPR016039 Thiolase-like
IPR020615 Thiolase_acyl_enz_int_AS
IPR020610 Thiolase_AS
IPR020617 Thiolase_C
IPR020613 Thiolase_CS
IPR020616 Thiolase_N
PfamiView protein in Pfam
PF02803 Thiolase_C, 1 hit
PF00108 Thiolase_N, 1 hit
PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
SUPFAMiSSF53901 SSF53901, 2 hits
TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
PROSITEiView protein in PROSITE
PS00098 THIOLASE_1, 1 hit
PS00737 THIOLASE_2, 1 hit
PS00099 THIOLASE_3, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q29RZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVLAALLRR GPLLQRRVQE IRYAERSYVS KPTLNEVVIV SAIRTPIGSF
60 70 80 90 100
LGSLSSLPAT KLGSIAIQGA IEKAGIPKEE VKEAYMGNVL QGGEGQAPTR
110 120 130 140 150
QAVLGAGLPI STPCTTINKV CASGMKAIMM ASQNLMCGHQ DVMVAGGMES
160 170 180 190 200
MSNVPYVMNR GATPYGGVKL EDLIVKDGLT DVYNKIHMGN CAENTAKKLN
210 220 230 240 250
ITREEQDTYA LNSYTRSKAA WEAGRFGNEV VPVTITVKGK PDVVVKEDEE
260 270 280 290 300
YKRVDFSKIP KLKTVFQREN GTVTAANAST LNDGAAAVVL MTADAAKRLN
310 320 330 340 350
VKPLARIAAF ADAAVEPIDF PLAPAYAVPK VLKDAGLKKE DITMWEVNEA
360 370 380 390 400
FSVVVLANIK MLEMDPQKVN INGGAVSLGH PIGMSGARIV VHLAHALKQG
410 420
EYGLASICNG GGGASAMLIQ KL
Length:422
Mass (Da):44,889
Last modified:April 4, 2006 - v1
Checksum:i17B8975F0DB3FE9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC113328 mRNA Translation: AAI13329.1
RefSeqiNP_001039540.1, NM_001046075.1
UniGeneiBt.57598

Genome annotation databases

EnsembliENSBTAT00000017122; ENSBTAP00000017122; ENSBTAG00000012885
GeneIDi511082
KEGGibta:511082

Similar proteinsi

Entry informationi

Entry nameiTHIL_BOVIN
AccessioniPrimary (citable) accession number: Q29RZ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 4, 2006
Last modified: May 23, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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