Q5R1W7 (ECHB_PANTR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Pan troglodytes (Chimpanzee)

Taxonomic identifier

9598 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 34	34	Mitochondrion Potential
	Chain	35 – 475	441	Trifunctional enzyme subunit beta, mitochondrial		PRO_0000034083
Sites
	Active site	139	1	Acyl-thioester intermediate By similarity
	Active site	429	1	Proton acceptor By similarity
	Active site	459	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	73	1	N6-acetyllysine By similarity
	Modified residue	189	1	N6-acetyllysine By similarity
	Modified residue	202	1	N6-acetyllysine By similarity
	Modified residue	349	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R1W7 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 123CA01ABD00CBAE	FASTA	475	51,396
	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

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.
RefSeq	NP_001029291.1. NM_001034119.1.
UniGene	Ptr.216.
3D structure databases
ProteinModelPortal	Q5R1W7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5R1W7.
Proteomic databases
PRIDE	Q5R1W7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSPTRT00000021854; ENSPTRP00000020160; ENSPTRG00000011733.
GeneID	459080.
KEGG	ptr:459080.
Organism-specific databases
CTD	3032.
Phylogenomic databases
eggNOG	prNOG08749.
GeneTree	ENSGT00390000009412.
HOVERGEN	HBG104782.
InParanoid	Q5R1W7.
OMA	QILANFK.
OrthoDB	EOG4Q2DFK.
PhylomeDB	Q5R1W7.
Family and domain databases
InterPro	IPR002155. 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]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KO	K07509.
PANTHER	PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
SUPFAM	SSF53901. Thiolase-like. 2 hits.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ECHB_PANTR

Accession

Primary (citable) accession number: Q5R1W7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	January 4, 2005
Last modified:	November 16, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program