Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-ketoacyl-CoA thiolase, mitochondrial

Gene

ACAA2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921Acyl-thioester intermediateBy similarity
Active sitei352 – 3521Proton acceptorPROSITE-ProRule annotation
Active sitei382 – 3821Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

  • Mitochondrion By similarity

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3973973-ketoacyl-CoA thiolase, mitochondrialPRO_0000270499Add
BLAST
Transit peptidei1 – 1616Mitochondrion; not cleavedBy similarityAdd
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 residuei136 – 1361PhosphothreonineBy similarity
Modified residuei137 – 1371N6-acetyllysine; alternateBy similarity
Modified residuei137 – 1371N6-succinyllysine; alternateBy similarity
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei143 – 1431N6-acetyllysine; alternateBy similarity
Modified residuei143 – 1431N6-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 residuei234 – 2341N6-acetyllysine; alternateBy similarity
Modified residuei234 – 2341N6-succinyllysine; alternateBy 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 residuei310 – 3101PhosphoserineBy 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

PRIDEiQ5RES5.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ5RES5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG003112.
InParanoidiQ5RES5.
KOiK07508.

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.

Q5RES5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLRGVFVV AAKRTPFGAY GGLLKDFTAT DLSEFAAKAA LSAGKVSPET
60 70 80 90 100
VDSVIMGNVL QSSSDAIYLA RHVGLRVGIP KETPALTINR LCGSGFQSIV
110 120 130 140 150
NGCQEICVKE AEVVLCGGTE SMSQAPYCVR TVRFGTKLGS DIKLEDSLWV
160 170 180 190 200
SLTDQHVQLP IAMTAENLAV KHKISREECD KYALQSQQRW KAANDAGYFN
210 220 230 240 250
DEMAPIEVKT KKGKQTMQVD EHARPQTTLE QLQKLPPVFK KDGTVTAGNA
260 270 280 290 300
SGIADGAGAV IIASEDAVKK HNFTPLARIV GYFVSGCDPS IMGIGPVPAI
310 320 330 340 350
SGALKKAGLS LKDMDLVEVN EAFAPQYLAV ERSLDLDISK TNVNGGAIAL
360 370 380 390
GHPLGGSGSR ITAHLVHELR RRGGKYAVGS ACIGGGQGIA VIIQSTA
Length:397
Mass (Da):41,907
Last modified:December 21, 2004 - v1
Checksum:i5AFC50C22C39F82D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857441 mRNA. Translation: CAH89732.1.
RefSeqiNP_001124791.1. NM_001131319.1.

Genome annotation databases

GeneIDi100171644.
KEGGipon:100171644.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857441 mRNA. Translation: CAH89732.1.
RefSeqiNP_001124791.1. NM_001131319.1.

3D structure databases

ProteinModelPortaliQ5RES5.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5RES5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100171644.
KEGGipon:100171644.

Organism-specific databases

CTDi10449.

Phylogenomic databases

HOVERGENiHBG003112.
InParanoidiQ5RES5.
KOiK07508.

Enzyme and pathway databases

UniPathwayiUPA00199.

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. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiTHIM_PONAB
AccessioniPrimary (citable) accession number: Q5RES5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 21, 2004
Last modified: October 14, 2015
This is version 65 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.