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Reviewed, UniProtKB/Swiss-Prot Q60587 (ECHB_RAT)

Last modified February 9, 2010. Version 77. 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:
    Trifunctional enzyme subunit beta, mitochondrial
Alternative name(s):
    TP-beta
Including the following 1 domains:
    1- Recommended name:
            3-ketoacyl-CoA thiolase
              EC=2.3.1.16
        Alternative name(s):
            Acetyl-CoA acyltransferase
            Beta-ketothiolase
Gene names
Name: Hadhb
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 length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. Ref.3

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the thiolase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion By similarity
Chain35 – 475441Trifunctional enzyme subunit beta, mitochondrial
PRO_0000034084

Sites

Active site1391Acyl-thioester intermediate By similarity
Active site4291Proton acceptor By similarity
Active site4591Proton acceptor By similarity

Amino acid modifications

Modified residue731N6-acetyllysine By similarity
Modified residue1891N6-acetyllysine By similarity
Modified residue2021N6-acetyllysine By similarity
Modified residue3491N6-acetyllysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q60587-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 59231029C8BA2A13

FASTA47551,414
        10         20         30         40         50         60 
MTTILTSTFR NLSTTSKWAL RFSVRPLSCS SQVQSAPAVQ TKSKKTLAKP NLKNIVVVEG 

        70         80         90        100        110        120 
VRIPFLLSGT SYKDLMPHDL ARAALSGLLY RTNIPKDVVD YIIFGTVIQE VKTSNVAREA 

       130        140        150        160        170        180 
ALGAGFSDKT PAHTVTMACI SSNQAMTTAV GLIASGQCDV VVAGGVELMS DVPIRHSRNM 

       190        200        210        220        230        240 
RKMMLDLNKA KTLAQRLSLL TKFRLNFLSP ELPAVAEFST NETMGHSADR LAAAFAVSRM 

       250        260        270        280        290        300 
EQDKYALRSH SLAKKAQDEG HLSDIVPFKV PGKDTVSKDN GIRPSSLEQM AKLKPAFIKP 

       310        320        330        340        350        360 
YGTVTAANSS FLTDGASAML IMSEDRALAM GYKPKAYLRD FIYVSQDPKD QLLLGPTYAT 

       370        380        390        400        410        420 
PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA QNYMGRKTKV GAPPLEKFNI 

       430        440        450        460        470 
WGGSLSLGHP FGATGCRLVM AAANRLRKDG GQYALVAACA AGGQGHAMIV EAYPK

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid beta-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal beta-oxidation enzymes."
Kamijo T., Aoyama T., Miyazaki J., Hashimoto T.
J. Biol. Chem. 268:26452-26460(1993) [PubMed: 8253773] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
[2]"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: Pituitary.
[3]"Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein."
Uchida Y., Izai K., Orii T., Hashimoto T.
J. Biol. Chem. 267:1034-1041(1992) [PubMed: 1730633] [Abstract]
Cited for: SUBUNIT.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D16479 mRNA. Translation: BAA03940.1.
BC060545 mRNA. Translation: AAH60545.1.
IPIIPI00198467.
PIRB49681.
RefSeqNP_598302.1.
UniGeneRn.11253

3D structure databases

SMRQ60587. Positions 55-472.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ60587.

Proteomic databases

PRIDEQ60587.

Genome annotation databases

EnsemblENSRNOT00000014637; ENSRNOP00000014637; ENSRNOG00000010800; Rattus norvegicus. [Genome view]
GeneID171155.
KEGGrno:171155.
NMPDRfig|10116.3.peg.24830.
UCSCNM_133618. rat.

Organism-specific databases

CTD171155.
RGD620513. Hadhb.

Phylogenomic databases

eggNOGroNOG05435.
HOVERGENQ60587.
InParanoidQ60587.
OMAKAGLTMN.
OrthoDBEOG9BGCFC.
PhylomeDBQ60587.

Enzyme and pathway databases

BRENDA2.3.1.16. 248.

Gene expression databases

ArrayExpressQ60587.
GenevestigatorQ60587.
GermOnlineENSRNOG00000010800. Rattus norvegicus.

Family and domain databases

InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
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

NextBio621992.

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Entry information

Entry nameECHB_RAT
AccessionPrimary (citable) accession number: Q60587
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 9, 2010
This is version 77 of the entry and version 1 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