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Protein

3-ketoacyl-CoA thiolase, mitochondrial

Gene

Acaa2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Abolishes BNIP3-mediated apoptosis and mitochondrial damage.By similarity

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei92Acyl-thioester intermediateBy similarity1
Active sitei352Proton acceptorPROSITE-ProRule annotation1
Active sitei382Proton acceptorPROSITE-ProRule annotation1

GO - Molecular functioni

  • acetyl-CoA C-acyltransferase activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

SABIO-RKP13437.
UniPathwayiUPA00199.

Chemistry databases

SwissLipidsiSLP:000001412.

Names & Taxonomyi

Protein namesi
Recommended name:
3-ketoacyl-CoA thiolase, mitochondrial (EC:2.3.1.16)
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Mitochondrial 3-oxoacyl-CoA thiolase
Gene namesi
Name:Acaa2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620482. Acaa2.

Subcellular locationi

  • Mitochondrion By similarity

  • Note: Colocalizes with BNIP3 in the mitochondria.By similarity

GO - Cellular componenti

  • mitochondrial matrix Source: RGD
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002233011 – 3973-ketoacyl-CoA thiolase, mitochondrialAdd BLAST397
Transit peptidei1 – 16Mitochondrion; not cleavedAdd BLAST16

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25N6-acetyllysine; alternateBy similarity1
Modified residuei25N6-succinyllysine; alternateBy similarity1
Modified residuei45N6-succinyllysineBy similarity1
Modified residuei119PhosphothreonineBy similarity1
Modified residuei121PhosphoserineBy similarity1
Modified residuei127PhosphotyrosineBy similarity1
Modified residuei136PhosphothreonineBy similarity1
Modified residuei137N6-acetyllysine; alternateBy similarity1
Modified residuei137N6-succinyllysine; alternateBy similarity1
Modified residuei143N6-acetyllysine; alternateBy similarity1
Modified residuei143N6-succinyllysine; alternateBy similarity1
Modified residuei158N6-acetyllysine; alternateBy similarity1
Modified residuei158N6-succinyllysine; alternateBy similarity1
Modified residuei171N6-acetyllysine; alternateBy similarity1
Modified residuei171N6-succinyllysine; alternateBy similarity1
Modified residuei191N6-acetyllysine; alternateBy similarity1
Modified residuei191N6-succinyllysine; alternateBy similarity1
Modified residuei209N6-acetyllysine; alternateBy similarity1
Modified residuei209N6-succinyllysine; alternateBy similarity1
Modified residuei211N6-succinyllysineBy similarity1
Modified residuei212N6-succinyllysineBy similarity1
Modified residuei214N6-succinyllysineBy similarity1
Modified residuei240N6-succinyllysineBy similarity1
Modified residuei241N6-acetyllysineBy similarity1
Modified residuei269N6-acetyllysineBy similarity1
Modified residuei270N6-acetyllysineBy similarity1
Modified residuei305N6-acetyllysine; alternateBy similarity1
Modified residuei305N6-succinyllysine; alternateBy similarity1
Modified residuei310PhosphoserineBy similarity1
Modified residuei312N6-acetyllysine; alternateBy similarity1
Modified residuei312N6-succinyllysine; alternateBy similarity1
Modified residuei333PhosphoserineBy similarity1
Modified residuei340N6-acetyllysineBy similarity1
Modified residuei344PhosphoserineBy similarity1
Modified residuei375N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP13437.
PRIDEiP13437.

PTM databases

iPTMnetiP13437.
PhosphoSitePlusiP13437.

Interactioni

Subunit structurei

Homotetramer. Interacts with BNIP3 (By similarity).By similarity

Protein-protein interaction databases

IntActiP13437. 1 interactor.
STRINGi10116.ENSRNOP00000060140.

Structurei

3D structure databases

ProteinModelPortaliP13437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1391. Eukaryota.
COG0183. LUCA.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP13437.
KOiK07508.
PhylomeDBiP13437.

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.

P13437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLRGVFIV AAKRTPFGAY GGLLKDFTAT DLTEFAARAA LSAGKVPPET
60 70 80 90 100
IDSVIVGNVM QSSSDAAYLA RHVGLRVGVP TETGALTLNR LCGSGFQSIV
110 120 130 140 150
SGCQEICSKD AEVVLCGGTE SMSQSPYSVR NVRFGTKFGL DLKLEDTLWA
160 170 180 190 200
GLTDQHVKLP MGMTAENLAA KYNISREDCD RYALQSQQRW KAANEAGYFN
210 220 230 240 250
EEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQNLPPVFK KEGTVTAGNA
260 270 280 290 300
SGMSDGAGVV IIASEDAVKK HNFTPLARVV GYFVSGCDPA IMGIGPVPAI
310 320 330 340 350
TGALKKAGLS LKDMDLIDVN EAFAPQFLAV QKSLDLDPSK TNVSGGAIAL
360 370 380 390
GHPLGGSGSR ITAHLVHELR RRGGKYAVGS ACIGGGQGIS LIIQNTA
Length:397
Mass (Da):41,871
Last modified:January 1, 1990 - v1
Checksum:i8344FB7271C3E2E1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05341 mRNA. Translation: CAA28952.1.
PIRiA29452. XURT.
RefSeqiNP_569117.1. NM_130433.1.
UniGeneiRn.3786.

Genome annotation databases

GeneIDi170465.
KEGGirno:170465.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05341 mRNA. Translation: CAA28952.1.
PIRiA29452. XURT.
RefSeqiNP_569117.1. NM_130433.1.
UniGeneiRn.3786.

3D structure databases

ProteinModelPortaliP13437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP13437. 1 interactor.
STRINGi10116.ENSRNOP00000060140.

Chemistry databases

SwissLipidsiSLP:000001412.

PTM databases

iPTMnetiP13437.
PhosphoSitePlusiP13437.

Proteomic databases

PaxDbiP13437.
PRIDEiP13437.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi170465.
KEGGirno:170465.

Organism-specific databases

CTDi10449.
RGDi620482. Acaa2.

Phylogenomic databases

eggNOGiKOG1391. Eukaryota.
COG0183. LUCA.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP13437.
KOiK07508.
PhylomeDBiP13437.

Enzyme and pathway databases

UniPathwayiUPA00199.
SABIO-RKP13437.

Miscellaneous databases

PROiP13437.

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...

Entry informationi

Entry nameiTHIM_RAT
AccessioniPrimary (citable) accession number: P13437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 123 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.