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Q60587 (ECHB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trifunctional enzyme subunit beta, mitochondrial
Alternative name(s):
TP-beta

Including the following 1 domains:

  1. 3-ketoacyl-CoA thiolase
    EC=2.3.1.16
    Alternative name(s):
    Acetyl-CoA acyltransferase
    Beta-ketothiolase
Gene names
Name:Hadhb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. Interacts with RSAD2/viperin By similarity. Ref.3

Subcellular location

Mitochondrion By similarity. Mitochondrion inner membrane By similarity. Mitochondrion outer membrane By similarity. Endoplasmic reticulum By similarity.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion inner membrane
Mitochondrion outer membrane
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from direct assay Ref.3. Source: RGD

   Cellular_componentendoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial fatty acid beta-oxidation multienzyme complex

Inferred from direct assay Ref.3. Source: RGD

mitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial nucleoid

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.3. Source: RGD

   Molecular_function3-hydroxyacyl-CoA dehydrogenase activity

Inferred from direct assay Ref.3. Source: RGD

NAD binding

Inferred from direct assay Ref.3. Source: RGD

acetyl-CoA C-acyltransferase activity

Inferred from direct assay Ref.3. Source: RGD

enoyl-CoA hydratase activity

Inferred from direct assay Ref.3. Source: RGD

fatty-acyl-CoA binding

Inferred from direct assay Ref.3. Source: RGD

long-chain-3-hydroxyacyl-CoA dehydrogenase activity

Inferred from direct assay Ref.3. Source: RGD

long-chain-enoyl-CoA hydratase activity

Inferred from direct assay Ref.3. Source: RGD

protein complex binding

Inferred from mutant phenotype PubMed 20132223. Source: RGD

Complete GO annotation...

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 residue531N6-succinyllysine By similarity
Modified residue731N6-acetyllysine; alternate By similarity
Modified residue731N6-succinyllysine; alternate By similarity
Modified residue1891N6-acetyllysine; alternate By similarity
Modified residue1891N6-succinyllysine; alternate By similarity
Modified residue1911N6-succinyllysine By similarity
Modified residue2731N6-succinyllysine By similarity
Modified residue2921N6-succinyllysine By similarity
Modified residue2941N6-acetyllysine; alternate By similarity
Modified residue2941N6-succinyllysine; alternate By similarity
Modified residue2991N6-acetyllysine By similarity
Modified residue3331N6-acetyllysine; alternate By similarity
Modified residue3331N6-succinyllysine; alternate By similarity
Modified residue3491N6-acetyllysine By similarity
Modified residue3621N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60587 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16479 mRNA. Translation: BAA03940.1.
BC060545 mRNA. Translation: AAH60545.1.
PIRB49681.
RefSeqNP_598302.1. NM_133618.2.
XP_006239850.1. XM_006239788.1.
XP_006239851.1. XM_006239789.1.
UniGeneRn.11253.

3D structure databases

ProteinModelPortalQ60587.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ60587. 2 interactions.
MINTMINT-4596988.
STRING10116.ENSRNOP00000014637.

Proteomic databases

PaxDbQ60587.
PRIDEQ60587.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014637; ENSRNOP00000014637; ENSRNOG00000010800.
GeneID171155.
KEGGrno:171155.

Organism-specific databases

CTD3032.
RGD620513. Hadhb.

Phylogenomic databases

eggNOGCOG0183.
GeneTreeENSGT00390000009412.
HOGENOMHOG000012240.
HOVERGENHBG104782.
InParanoidQ60587.
KOK07509.
OMAKMFASDK.
OrthoDBEOG7DRJ2Z.
PhylomeDBQ60587.
TreeFamTF315243.

Enzyme and pathway databases

UniPathwayUPA00659.

Gene expression databases

GenevestigatorQ60587.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
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]
PANTHERPTHR18919. PTHR18919. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 2 hits.
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

NextBio621992.
PROQ60587.

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: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways