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Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene

Acat1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Plays a major role in ketone body metabolism.

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 sitei123Acyl-thioester intermediateBy similarity1
Metal bindingi216PotassiumBy similarity1
Binding sitei216Coenzyme ABy similarity1
Binding sitei260Coenzyme ABy similarity1
Metal bindingi277Potassium; via carbonyl oxygenBy similarity1
Metal bindingi278Potassium; via carbonyl oxygenBy similarity1
Metal bindingi280Potassium; via carbonyl oxygenBy similarity1
Binding sitei281Coenzyme ABy similarity1
Metal bindingi378Potassium; via carbonyl oxygenBy similarity1
Active sitei382Proton acceptorPROSITE-ProRule annotation1
Active sitei410Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

  • acetyl-CoA C-acetyltransferase activity Source: RGD
  • carbon-carbon lyase activity Source: Ensembl
  • coenzyme binding Source: RGD
  • enzyme binding Source: RGD
  • ligase activity, forming carbon-carbon bonds Source: Ensembl
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • acetyl-CoA biosynthetic process Source: Ensembl
  • acetyl-CoA catabolic process Source: Ensembl
  • adipose tissue development Source: RGD
  • brain development Source: RGD
  • coenzyme A biosynthetic process Source: Ensembl
  • fatty acid beta-oxidation Source: GO_Central
  • isoleucine catabolic process Source: Ensembl
  • ketone body catabolic process Source: Ensembl
  • liver development Source: RGD
  • metanephric proximal convoluted tubule development Source: RGD
  • propionyl-CoA biosynthetic process Source: Ensembl
  • protein homooligomerization Source: RGD
  • response to hormone Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to starvation Source: RGD

Keywordsi

Molecular functionAcyltransferase, Transferase
LigandMetal-binding, Potassium

Enzyme and pathway databases

ReactomeiR-RNO-70895 Branched-chain amino acid catabolism
R-RNO-77108 Utilization of Ketone Bodies
R-RNO-77111 Synthesis of Ketone Bodies
SABIO-RKiP17764

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi2016 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

Pathology & Biotechi

Chemistry databases

GuidetoPHARMACOLOGYi2435

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30Mitochondrion1 PublicationAdd BLAST30
ChainiPRO_000003408831 – 424Acetyl-CoA acetyltransferase, mitochondrialAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei63N6-acetyllysine; alternateBy similarity1
Modified residuei63N6-succinyllysine; alternateBy similarity1
Modified residuei75N6-succinyllysineBy similarity1
Modified residuei171N6-acetyllysine; alternateBy similarity1
Modified residuei171N6-succinyllysine; alternateBy similarity1
Modified residuei178N6-acetyllysine; alternateBy similarity1
Modified residuei178N6-succinyllysine; alternateBy similarity1
Modified residuei187N6-acetyllysine; alternateBy similarity1
Modified residuei187N6-succinyllysine; alternateBy similarity1
Modified residuei199N6-acetyllysine; alternateBy similarity1
Modified residuei199N6-succinyllysine; alternateBy similarity1
Modified residuei204PhosphoserineBy similarity1
Modified residuei220N6-acetyllysine; alternateBy similarity1
Modified residuei220N6-succinyllysine; alternateBy similarity1
Modified residuei227N6-acetyllysine; alternateBy similarity1
Modified residuei227N6-succinyllysine; alternateBy similarity1
Modified residuei240N6-succinyllysineBy similarity1
Modified residuei242N6-acetyllysine; alternateBy similarity1
Modified residuei242N6-succinyllysine; alternateBy similarity1
Modified residuei248N6-acetyllysineBy similarity1
Modified residuei254N6-acetyllysineBy similarity1
Modified residuei260N6-acetyllysine; alternateBy similarity1
Modified residuei260N6-succinyllysine; alternateBy similarity1
Modified residuei263N6-succinyllysineBy similarity1
Modified residuei265N6-succinyllysineBy similarity1
Modified residuei270N6-acetyllysineBy similarity1
Modified residuei335N6-acetyllysineBy similarity1

Post-translational modificationi

Succinylation at Lys-265, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP17764
PRIDEiP17764

PTM databases

CarbonylDBiP17764
iPTMnetiP17764
PhosphoSitePlusiP17764

Expressioni

Gene expression databases

BgeeiENSRNOG00000007862
GenevisibleiP17764 RN

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • enzyme binding Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP17764, 3 interactors
MINTiP17764
STRINGi10116.ENSRNOP00000010573

Structurei

3D structure databases

ProteinModelPortaliP17764
SMRiP17764
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni255 – 257Coenzyme A bindingBy similarity3

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1390 Eukaryota
COG0183 LUCA
GeneTreeiENSGT00390000009412
HOGENOMiHOG000012238
HOVERGENiHBG003112
InParanoidiP17764
KOiK00626
OMAiWDVYNKF
OrthoDBiEOG091G09C6
PhylomeDBiP17764
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.

P17764-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALAVLHGV VRRPLLRGLL QEVRCLGRSY ASKPTLNDVV IVSATRTPIG
60 70 80 90 100
SFLGSLASQP ATKLGTIAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP
110 120 130 140 150
TRQATLGAGL PIATPCTTVN KVCASGMKAI MMASQSLMCG HQDVMVAGGM
160 170 180 190 200
ESMSNVPYVM SRGATPYGGV KLEDLIVKDG LTDVYNKIHM GNCAENTAKK
210 220 230 240 250
LSISREEQDK YAIGSYTRSK EAWDAGKFAN EITPITISVK GKPDVVVKED
260 270 280 290 300
EEYKRVDFSK VPKLKTVFQK ENGTVTAANA STLNDGAAAV VLMTAEAAQR
310 320 330 340 350
LKVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN
360 370 380 390 400
EAFSVVVLAN IKMLEIDPQK VNVHGGAVSL GHPIGMSGAR IVVHLAHALK
410 420
QGEFGLASIC NGGGGASAVL IEKL
Length:424
Mass (Da):44,695
Last modified:August 1, 1990 - v1
Checksum:i79E8881DB242EFEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00512 mRNA Translation: BAA00401.1 Sequence problems.
D13921 mRNA Translation: BAA03016.1
PIRiJU0072 XXRTAC
RefSeqiNP_058771.2, NM_017075.2
UniGeneiRn.4054

Genome annotation databases

EnsembliENSRNOT00000010573; ENSRNOP00000010573; ENSRNOG00000007862
GeneIDi25014
KEGGirno:25014
UCSCiRGD:2016 rat

Similar proteinsi

Entry informationi

Entry nameiTHIL_RAT
AccessioniPrimary (citable) accession number: P17764
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 20, 2018
This is version 150 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, Direct protein sequencing, Reference proteome

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