Q60587 (ECHB_RAT) 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

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 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 process	Fatty acid metabolism Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane Mitochondrion Mitochondrion inner membrane Mitochondrion outer membrane
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from direct assay Ref.3. Source: RGD
Cellular_component	endoplasmic 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: Compara mitochondrial outer membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	3-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 34	34	Mitochondrion By similarity
	Chain	35 – 475	441	Trifunctional enzyme subunit beta, mitochondrial		PRO_0000034084
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)
	Q60587 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 59231029C8BA2A13	FASTA	475	51,414
	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

References

	« Hide 'large scale' referencesShow '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.
IPI	IPI00198467.
PIR	B49681.
RefSeq	NP_598302.1. NM_133618.2.
UniGene	Rn.11253.
3D structure databases
ProteinModelPortal	Q60587.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q60587. 1 interaction.
MINT	MINT-4596988.
STRING	10116.ENSRNOP00000014637.
Proteomic databases
PaxDb	Q60587.
PRIDE	Q60587.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000014637; ENSRNOP00000014637; ENSRNOG00000010800.
GeneID	171155.
KEGG	rno:171155.
Organism-specific databases
CTD	3032.
RGD	620513. Hadhb.
Phylogenomic databases
eggNOG	COG0183.
GeneTree	ENSGT00620000087956.
HOGENOM	HOG000012240.
HOVERGEN	HBG104782.
InParanoid	Q60587.
KO	K07509.
OMA	CRQNTAY.
OrthoDB	EOG4Q2DFK.
Enzyme and pathway databases
UniPathway	UPA00659.
Gene expression databases
Genevestigator	Q60587.
GermOnline	ENSRNOG00000010800. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.47.10. 4 hits.
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]
PANTHER	PTHR18919. PTHR18919. 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...
Other
NextBio	621992.

Entry information

Entry name

ECHB_RAT

Accession

Primary (citable) accession number: Q60587

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program