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Protein

Acetyl-CoA acetyltransferase, mitochondrial

Gene

ACAT1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei121 – 1211Acyl-thioester intermediateBy similarity
Metal bindingi214 – 2141PotassiumBy similarity
Binding sitei214 – 2141Coenzyme ABy similarity
Binding sitei258 – 2581Coenzyme ABy similarity
Metal bindingi275 – 2751Potassium; via carbonyl oxygenBy similarity
Metal bindingi276 – 2761Potassium; via carbonyl oxygenBy similarity
Metal bindingi278 – 2781Potassium; via carbonyl oxygenBy similarity
Binding sitei279 – 2791Coenzyme ABy similarity
Metal bindingi376 – 3761Potassium; via carbonyl oxygenBy similarity
Active sitei380 – 3801Proton acceptorPROSITE-ProRule annotation
Active sitei408 – 4081Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Metal-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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionBy similarityAdd
BLAST
Chaini29 – 422394Acetyl-CoA acetyltransferase, mitochondrialPRO_0000356274Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611N6-acetyllysine; alternateBy similarity
Modified residuei61 – 611N6-succinyllysine; alternateBy similarity
Modified residuei73 – 731N6-succinyllysineBy similarity
Modified residuei169 – 1691N6-acetyllysine; alternateBy similarity
Modified residuei169 – 1691N6-succinyllysine; alternateBy similarity
Modified residuei176 – 1761N6-acetyllysine; alternateBy similarity
Modified residuei176 – 1761N6-succinyllysine; alternateBy similarity
Modified residuei185 – 1851N6-acetyllysine; alternateBy similarity
Modified residuei185 – 1851N6-succinyllysine; alternateBy similarity
Modified residuei197 – 1971N6-acetyllysine; alternateBy similarity
Modified residuei197 – 1971N6-succinyllysine; alternateBy similarity
Modified residuei218 – 2181N6-acetyllysine; alternateBy similarity
Modified residuei218 – 2181N6-succinyllysine; alternateBy similarity
Modified residuei238 – 2381N6-succinyllysineBy similarity
Modified residuei240 – 2401N6-acetyllysine; alternateBy similarity
Modified residuei240 – 2401N6-succinyllysine; alternateBy similarity
Modified residuei246 – 2461N6-acetyllysineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity
Modified residuei258 – 2581N6-acetyllysine; alternateBy similarity
Modified residuei258 – 2581N6-succinyllysine; alternateBy similarity
Modified residuei261 – 2611N6-succinyllysineBy similarity
Modified residuei263 – 2631N6-succinyllysineBy similarity
Modified residuei333 – 3331N6-acetyllysineBy similarity

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.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ29RZ0. 1 interaction.
STRINGi9913.ENSBTAP00000017122.

Structurei

3D structure databases

ProteinModelPortaliQ29RZ0.
SMRiQ29RZ0. Positions 30-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni253 – 2553Coenzyme A bindingBy similarity

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1390. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ29RZ0.
KOiK00626.
OMAiAPVGAMN.
OrthoDBiEOG7JQBNG.
TreeFamiTF300650.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ29RZ0.
SMRiQ29RZ0. Positions 30-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ29RZ0. 1 interaction.
STRINGi9913.ENSBTAP00000017122.

Proteomic databases

PaxDbiQ29RZ0.
PeptideAtlasiQ29RZ0.
PRIDEiQ29RZ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000017122; ENSBTAP00000017122; ENSBTAG00000012885.
GeneIDi511082.
KEGGibta:511082.

Organism-specific databases

CTDi38.

Phylogenomic databases

eggNOGiKOG1390. Eukaryota.
COG0183. LUCA.
GeneTreeiENSGT00390000009412.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiQ29RZ0.
KOiK00626.
OMAiAPVGAMN.
OrthoDBiEOG7JQBNG.
TreeFamiTF300650.

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.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Uterus.

Entry informationi

Entry nameiTHIL_BOVIN
AccessioniPrimary (citable) accession number: Q29RZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: April 4, 2006
Last modified: July 6, 2016
This is version 79 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.