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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.

Pathway:ifatty 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Acyl-thioester intermediateBy similarity
Active sitei352 – 3521Proton acceptorPROSITE-ProRule annotation
Active sitei382 – 3821Proton acceptorPROSITE-ProRule annotation

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.

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
ProteomesiUP000002494 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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3973973-ketoacyl-CoA thiolase, mitochondrialPRO_0000223301Add
BLAST
Transit peptidei1 – 1616Mitochondrion; not cleavedAdd
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251N6-acetyllysine; alternateBy similarity
Modified residuei25 – 251N6-succinyllysine; alternateBy similarity
Modified residuei45 – 451N6-succinyllysineBy similarity
Modified residuei119 – 1191PhosphothreonineBy similarity
Modified residuei121 – 1211PhosphoserineBy similarity
Modified residuei127 – 1271PhosphotyrosineBy similarity
Modified residuei137 – 1371N6-acetyllysine; alternateBy similarity
Modified residuei137 – 1371N6-succinyllysine; alternateBy similarity
Modified residuei143 – 1431N6-acetyllysine; alternateBy similarity
Modified residuei143 – 1431N6-succinyllysine; alternateBy similarity
Modified residuei158 – 1581N6-acetyllysine; alternateBy similarity
Modified residuei158 – 1581N6-succinyllysine; alternateBy similarity
Modified residuei171 – 1711N6-acetyllysine; alternateBy similarity
Modified residuei171 – 1711N6-succinyllysine; alternateBy similarity
Modified residuei191 – 1911N6-acetyllysine; alternateBy similarity
Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
Modified residuei209 – 2091N6-acetyllysine; alternateBy similarity
Modified residuei209 – 2091N6-succinyllysine; alternateBy similarity
Modified residuei211 – 2111N6-succinyllysineBy similarity
Modified residuei212 – 2121N6-succinyllysineBy similarity
Modified residuei214 – 2141N6-succinyllysineBy similarity
Modified residuei240 – 2401N6-succinyllysineBy similarity
Modified residuei241 – 2411N6-acetyllysineBy similarity
Modified residuei269 – 2691N6-acetyllysineBy similarity
Modified residuei270 – 2701N6-acetyllysineBy similarity
Modified residuei305 – 3051N6-acetyllysine; alternateBy similarity
Modified residuei305 – 3051N6-succinyllysine; alternateBy similarity
Modified residuei312 – 3121N6-acetyllysine; alternateBy similarity
Modified residuei312 – 3121N6-succinyllysine; alternateBy similarity
Modified residuei333 – 3331PhosphoserineBy similarity
Modified residuei340 – 3401N6-acetyllysineBy similarity
Modified residuei375 – 3751N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP13437.
PRIDEiP13437.

Expressioni

Gene expression databases

GenevisibleiP13437. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP13437. 1 interaction.
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

eggNOGiCOG0183.
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 interaction.
STRINGi10116.ENSRNOP00000060140.

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

eggNOGiCOG0183.
HOGENOMiHOG000012238.
HOVERGENiHBG003112.
InParanoidiP13437.
KOiK07508.
PhylomeDBiP13437.

Enzyme and pathway databases

UniPathwayiUPA00199.
SABIO-RKP13437.

Miscellaneous databases

NextBioi620987.
PROiP13437.

Gene expression databases

GenevisibleiP13437. RN.

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. "cDNA-derived amino acid sequence of rat mitochondrial 3-oxoacyl-CoA thiolase with no transient presequence: structural relationship with peroxisomal isozyme."
    Arakawa H., Takiguchi M., Amaya Y., Nagata S., Hayashi H., Mori M.
    EMBO J. 6:1361-1366(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.

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: July 22, 2015
This is version 116 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

External Data

Dasty 3

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 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.