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Reviewed, UniProtKB/Swiss-Prot Q8HXX4 (ECHB_MACFA)

Last modified October 13, 2009. Version 35. 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
ORF Names: QtrA-13435
OrganismMacaca fascicularis (Crab eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

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

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 By similarity
Chain35 – 475441Trifunctional enzyme subunit beta, mitochondrial
PRO_0000034081

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
Q8HXX4-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 411A85F52B2502DA

FASTA47551,356
        10         20         30         40         50         60 
MTTILTCPFK KLPTTSKWAL RFAIRPLSCS 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 DIPIRHSRKM 

       190        200        210        220        230        240 
RKLMLDLNKA KSMGQRLSLI SKFRLNFLAP ELPAVAEFST SETMGHSADR LAAAFAVSRL 

       250        260        270        280        290        300 
EQDEYALRSH SLAKKAQDEG LLSDVVPFRV 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 

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References

[1]"Isolation and characterization of cDNA for macaque neurological disease genes."
Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Temporal cortex.

Cross-references

Sequence databases

AB083315 mRNA. Translation: BAC20594.1.

3D structure databases

HSSPHSSP built from PDB template 1AFW based on UniProtKB P27796.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ8HXX4.

Enzyme and pathway databases

BRENDA2.3.1.16. 3438.

Family and domain databases

InterProIPR002155. Thiolase.
[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...

Entry information

Entry nameECHB_MACFA
AccessionPrimary (citable) accession number: Q8HXX4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: October 13, 2009
This is version 35 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