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Reviewed, UniProtKB/Swiss-Prot P07871 (THIKB_RAT)

Last modified February 9, 2010. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    3-ketoacyl-CoA thiolase B, peroxisomal
    EC=2.3.1.16
Alternative name(s):
    Beta-ketothiolase B
    Acetyl-CoA acyltransferase B
    Peroxisomal 3-oxoacyl-CoA thiolase B
Gene names
Name: Acaa1b
Synonyms: Acaa1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid metabolism.

Subunit structure

Homodimer.

Subcellular location

Peroxisome.

Induction

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.

Miscellaneous

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

Sequence similarities

Belongs to the thiolase family.

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Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Peroxisome
Chain27 – 4243983-ketoacyl-CoA thiolase B, peroxisomal
PRO_0000034071

Sites

Active site1231Acyl-thioester intermediate By similarity
Active site3771Proton acceptor By similarity
Active site4081Proton acceptor By similarity

Experimental info

Sequence conflict441R → Q in AAA41497. Ref.1
Sequence conflict781L → P in AAA41497. Ref.1
Sequence conflict3591L → V in BAA14107. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P07871-1 [UniParc].

Last modified May 1, 1991. Version 2.
Checksum: E1D41A3C65477D77

FASTA42443,820
        10         20         30         40         50         60 
MHRLQVVLGH LAGRSESSSA LQAAPCSAGF PQASASDVVV VHGRRTPIGR AGRGGFKDTT 

        70         80         90        100        110        120 
PDELLSAVLT AVLQDVKLKP ECLGDISVGN VLQPGAGAAM ARIAQFLSGI PETVPLSAVN 

       130        140        150        160        170        180 
RQCSSGLQAV ANIAGGIRNG SYDIGMACGV ESMTLSERGN PGNISSRLLE NEKARDCLIP 

       190        200        210        220        230        240 
MGITSENVAE RFGISRQKQD AFALASQQKA ASAQSKGCFR AEIVPVTTTV LDDKGDRKTI 

       250        260        270        280        290        300 
TVSQDEGVRP STTMEGLAKL KPAFKDGGST TAGNSSQVSD GAAAVLLARR SKAEELGLPI 

       310        320        330        340        350        360 
LGVLRSYAVV GVPPDIMGIG PAYAIPAALQ KAGLTVNDID IFEINEAFAS QALYCVEKLG 

       370        380        390        400        410        420 
IPAEKVNPLG GAIALGHPLG CTGARQVVTL LNELKRRGRR AYGVVSMCIG TGMGAAAVFE 


YPGN

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References

« Hide 'large scale' references
[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: 3036803] [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: 2307679] [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: 15489334] [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: 1680677] [Abstract]
Cited for: TRANSIT PEPTIDE.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J02749 mRNA. Translation: AAA41497.1.
D90063 Genomic DNA. Translation: BAA14107.1.
BC098757 mRNA. Translation: AAH98757.1.
IPIIPI00370596.
PIRXURTAB. B35725.
RefSeqNP_001035108.1.
XP_001077387.1.
UniGeneRn.154995

3D structure databases

SMRP07871. Positions 31-424.
ModBaseSearch...

Protein-protein interaction databases

STRINGP07871.

Genome annotation databases

EnsemblENSRNOT00000045049; ENSRNOP00000050691; ENSRNOG00000032908; Rattus norvegicus. [Genome view]
GeneID501072.
KEGGrno:501072.

Organism-specific databases

CTD501072.
RGD1562373. RGD1562373.

Phylogenomic databases

eggNOGroNOG07340.
HOVERGENP07871.
InParanoidP07871.
PhylomeDBP07871.

Enzyme and pathway databases

BRENDA2.3.1.16. 248.

Gene expression databases

GenevestigatorP07871.
GermOnlineENSRNOG00000032908. Rattus norvegicus.

Family and domain databases

InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio708193.

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Entry information

Entry nameTHIKB_RAT
AccessionPrimary (citable) accession number: P07871
Secondary accession number(s): Q4G049
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 1991
Last modified: February 9, 2010
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents