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Reviewed, UniProtKB/Swiss-Prot Q5R1W7 (ECHB_PANTR)

Last modified February 9, 2010. Version 45. 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

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
OrganismPan troglodytes (Chimpanzee)
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the thiolase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion Potential
Chain35 – 475441Trifunctional enzyme subunit beta, mitochondrial
PRO_0000034083

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

Sequences

Sequence LengthMass (Da)Tools
Q5R1W7-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 123CA01ABD00CBAE

FASTA47551,396
        10         20         30         40         50         60 
MTTILTYPFK NLPTASKWAL RFSIRPLSCS SQLRAAPAVQ TKTKKTLAKP NIRNVVVVDG 

        70         80         90        100        110        120 
VRTPFLLSGT SYKDLMPHDL ARAALTGLLH RTSVPKEVVD YIIFGTVIQE VKTSNVAREA 

       130        140        150        160        170        180 
ALGAGFSDKT PAHTVTMACI SANQAMTTGV GLIASGQCDV IVAGGVELMS DVPIRHSRKM 

       190        200        210        220        230        240 
RKLMLDLNKA KSMGQRLSLI SKFRFNFLAP ELPAVSEFST SETMGHSADR LAAAFAVSRL 

       250        260        270        280        290        300 
EQDEYALRSH SLAKKAQDEG LLSDVVPFKV PGKDTVTKDN GIRPSSLEQM AKLKPAFIKP 

       310        320        330        340        350        360 
YGTVTAANSS FLTDGASAML IMAEEKALAM GYKPKAYLRD FMYVSQDPKD QLLLGPTYAT 

       370        380        390        400        410        420 
PKVLEKAGLT MNDIDAFEFH EAFSGQILAN FKAMDSDWFA ENYMGRKTKV GLPPLEKFNN 

       430        440        450        460        470 
WGGSLSLGHP FGATGCRLVM AAANRLRKEG GQYGLVAACA AGGQGHAMIV EAYPK 

« Hide

References

[1]Hirai M., Sakate R., Hida M., Sugano S., Hayasaka I., Suto Y., Osada N., Hashimoto K.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skin.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB188280 mRNA. Translation: BAD74031.1.
RefSeqNP_001029291.1.

3D structure databases

SMRQ5R1W7. Positions 51-472.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5R1W7.

Genome annotation databases

EnsemblENSPTRT00000021854; ENSPTRP00000020160; ENSPTRG00000011733; Pan troglodytes. [Genome view]
GeneID459080.
KEGGptr:459080.

Organism-specific databases

CTD459080.

Phylogenomic databases

eggNOGprNOG08749.
HOVERGENQ5R1W7.
InParanoidQ5R1W7.
OMAKAGLTMN.
PhylomeDBQ5R1W7.

Enzyme and pathway databases

BRENDA2.3.1.16. 264977.

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]
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameECHB_PANTR
AccessionPrimary (citable) accession number: Q5R1W7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: January 4, 2005
Last modified: February 9, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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