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Protein

3-ketoacyl-CoA thiolase B, peroxisomal

Gene

Acaa1b

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

Functioni

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 sitei123 – 1231Acyl-thioester intermediateBy similarity
Active sitei377 – 3771Proton acceptorPROSITE-ProRule annotation
Active sitei408 – 4081Proton 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

SABIO-RKP07871.
UniPathwayiUPA00199.

Chemistry

SwissLipidsiSLP:000001213.

Names & Taxonomyi

Protein namesi
Recommended name:
3-ketoacyl-CoA thiolase B, peroxisomal (EC:2.3.1.16)
Alternative name(s):
Acetyl-CoA acyltransferase B
Beta-ketothiolase B
Peroxisomal 3-oxoacyl-CoA thiolase B
Gene namesi
Name:Acaa1b
Synonyms:Acaa1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1562373. Acaa1b.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626Peroxisome1 PublicationAdd
BLAST
Chaini27 – 4243983-ketoacyl-CoA thiolase B, peroxisomalPRO_0000034071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731N6-acetyllysineBy similarity
Modified residuei234 – 2341N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP07871.

PTM databases

iPTMnetiP07871.

Expressioni

Inductioni

Peroxisomal thiolase is markedly induced (at the level of transcription) by various hypolipidemic compounds in parallel with the other two enzymes of the peroxisomal beta-oxidation system.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP07871. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP07871.
SMRiP07871. Positions 31-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000012239.
HOVERGENiHBG003112.
InParanoidiP07871.
KOiK07513.
PhylomeDBiP07871.

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.

P07871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHRLQVVLGH LAGRSESSSA LQAAPCSAGF PQASASDVVV VHGRRTPIGR
60 70 80 90 100
AGRGGFKDTT PDELLSAVLT AVLQDVKLKP ECLGDISVGN VLQPGAGAAM
110 120 130 140 150
ARIAQFLSGI PETVPLSAVN RQCSSGLQAV ANIAGGIRNG SYDIGMACGV
160 170 180 190 200
ESMTLSERGN PGNISSRLLE NEKARDCLIP MGITSENVAE RFGISRQKQD
210 220 230 240 250
AFALASQQKA ASAQSKGCFR AEIVPVTTTV LDDKGDRKTI TVSQDEGVRP
260 270 280 290 300
STTMEGLAKL KPAFKDGGST TAGNSSQVSD GAAAVLLARR SKAEELGLPI
310 320 330 340 350
LGVLRSYAVV GVPPDIMGIG PAYAIPAALQ KAGLTVNDID IFEINEAFAS
360 370 380 390 400
QALYCVEKLG IPAEKVNPLG GAIALGHPLG CTGARQVVTL LNELKRRGRR
410 420
AYGVVSMCIG TGMGAAAVFE YPGN
Length:424
Mass (Da):43,820
Last modified:May 1, 1991 - v2
Checksum:iE1D41A3C65477D77
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441R → Q in AAA41497 (PubMed:3036803).Curated
Sequence conflicti78 – 781L → P in AAA41497 (PubMed:3036803).Curated
Sequence conflicti359 – 3591L → V in BAA14107 (PubMed:2307679).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02749 mRNA. Translation: AAA41497.1.
D90063 Genomic DNA. Translation: BAA14107.1.
BC098757 mRNA. Translation: AAH98757.1.
PIRiB35725. XURTAB.
RefSeqiNP_001035108.1. NM_001040019.1.
UniGeneiRn.154995.

Genome annotation databases

GeneIDi501072.
KEGGirno:501072.
UCSCiRGD:1562373. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02749 mRNA. Translation: AAA41497.1.
D90063 Genomic DNA. Translation: BAA14107.1.
BC098757 mRNA. Translation: AAH98757.1.
PIRiB35725. XURTAB.
RefSeqiNP_001035108.1. NM_001040019.1.
UniGeneiRn.154995.

3D structure databases

ProteinModelPortaliP07871.
SMRiP07871. Positions 31-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07871. 1 interaction.

Chemistry

SwissLipidsiSLP:000001213.

PTM databases

iPTMnetiP07871.

Proteomic databases

PRIDEiP07871.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi501072.
KEGGirno:501072.
UCSCiRGD:1562373. rat.

Organism-specific databases

CTDi235674.
RGDi1562373. Acaa1b.

Phylogenomic databases

HOGENOMiHOG000012239.
HOVERGENiHBG003112.
InParanoidiP07871.
KOiK07513.
PhylomeDBiP07871.

Enzyme and pathway databases

UniPathwayiUPA00199.
SABIO-RKP07871.

Miscellaneous databases

PROiP07871.

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

« Hide 'large scale' publications
  1. "Structural analysis of cDNA for rat peroxisomal 3-ketoacyl-CoA thiolase."
    Hijikata M., Ishii N., Kagamiyama H., Osumi T., Hashimoto T.
    J. Biol. Chem. 262:8151-8158(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Rat peroxisomal 3-ketoacyl-CoA thiolase gene. Occurrence of two closely related but differentially regulated genes."
    Hijikata M., Wen J.K., Osumi T., Hashimoto T.
    J. Biol. Chem. 265:4600-4606(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. "A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase."
    Swinkels B.W., Gould S.J., Bodnar A.G., Rachubinski R.A., Subramani S.
    EMBO J. 10:3255-3262(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSIT PEPTIDE CLEAVAGE SITE.

Entry informationi

Entry nameiTHIKB_RAT
AccessioniPrimary (citable) accession number: P07871
Secondary accession number(s): Q4G049
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 1991
Last modified: June 8, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There exist at least 2 rat liver peroxisomal 3-ketoacyl-CoA thiolases.

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.