Reviewed, UniProtKB/Swiss-Prot P17764 (THIL_RAT)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA acetyltransferase, mitochondrial
    EC=2.3.1.9
Alternative name(s):
    Acetoacetyl-CoA thiolase

Gene names

Name:

Acat1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	424 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)

Function	Plays a major role in ketone body metabolism.
Catalytic activity	2 acetyl-CoA = CoA + acetoacetyl-CoA.
Enzyme regulation	Activated by potassium ions, but not sodium ions By similarity.
Subunit structure	Homotetramer.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Potassium
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	acetyl-CoA C-acetyltransferase activity Ref.1 Inferred from direct assay. Source: RGD potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 30	30	Mitochondrion Ref.1
	Chain	31 – 424	394	Acetyl-CoA acetyltransferase, mitochondrial		PRO_0000034088
Regions
	Region	255 – 257	3	Coenzyme A binding By similarity
Sites
	Active site	123	1	Acyl-thioester intermediate By similarity
	Active site	382	1	Proton acceptor By similarity
	Active site	410	1	Proton acceptor By similarity
	Metal binding	216	1	Potassium By similarity
	Metal binding	277	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	278	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	280	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	378	1	Potassium; via carbonyl oxygen By similarity
	Binding site	216	1	Coenzyme A By similarity
	Binding site	260	1	Coenzyme A By similarity
	Binding site	281	1	Coenzyme A By similarity
Amino acid modifications
	Modified residue	80	1	N6-acetyllysine By similarity
	Modified residue	171	1	N6-acetyllysine By similarity
	Modified residue	178	1	N6-acetyllysine By similarity
	Modified residue	187	1	N6-acetyllysine By similarity
	Modified residue	227	1	N6-acetyllysine By similarity
	Modified residue	248	1	N6-acetyllysine By similarity
	Modified residue	260	1	N6-acetyllysine By similarity
	Modified residue	335	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17764-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 79E8881DB242EFEE	FASTA	424	44,695
	10 20 30 40 50 60 MAALAVLHGV VRRPLLRGLL QEVRCLGRSY ASKPTLNDVV IVSATRTPIG SFLGSLASQP 70 80 90 100 110 120 ATKLGTIAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP TRQATLGAGL PIATPCTTVN 130 140 150 160 170 180 KVCASGMKAI MMASQSLMCG HQDVMVAGGM ESMSNVPYVM SRGATPYGGV KLEDLIVKDG 190 200 210 220 230 240 LTDVYNKIHM GNCAENTAKK LSISREEQDK YAIGSYTRSK EAWDAGKFAN EITPITISVK 250 260 270 280 290 300 GKPDVVVKED EEYKRVDFSK VPKLKTVFQK ENGTVTAANA STLNDGAAAV VLMTAEAAQR 310 320 330 340 350 360 LKVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN EAFSVVVLAN 370 380 390 400 410 420 IKMLEIDPQK VNVHGGAVSL GHPIGMSGAR IVVHLAHALK QGEFGLASIC NGGGGASAVL IEKL

References

[1]

"Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat mitochondrial acetoacetyl-CoA thiolase." Fukao T., Kamijo K., Osumi T., Fujiki Y., Yamaguchi S., Orii T., Hashimoto T. J. Biochem. 106:197-204(1989) [PubMed: 2478525] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-50.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D00512 mRNA. Translation: BAA00401.1. Sequence problems. D13921 mRNA. Translation: BAA03016.1.
IPI	IPI00324302.
PIR	XXRTAC. JU0072.
RefSeq	NP_058771.1.
UniGene	Rn.4054
3D structure databases
HSSP	HSSP built from PDB template 1M4T based on UniProtKB P07097.
SMR	P17764. Positions 32-424.
ModBase	Search...
Protein-protein interaction databases
STRING	P17764.
PTM databases
PhosphoSite	P17764.
Proteomic databases
PRIDE	P17764.
Genome annotation databases
Ensembl	ENSRNOT00000010573; ENSRNOP00000010573; ENSRNOG00000007862; Rattus norvegicus. [Genome view]
GeneID	25014.
KEGG	rno:25014.
UCSC	NM_017075. rat.
Organism-specific databases
CTD	25014.
RGD	2016. Acat1.
Phylogenomic databases
HOVERGEN	P17764.
OMA	AYAVPKV.
Enzyme and pathway databases
BRENDA	2.3.1.9. 248.
Gene expression databases
ArrayExpress	P17764.
Genevestigator	P17764.
GermOnline	ENSRNOG00000007862. Rattus norvegicus.
Family and domain databases
InterPro	IPR002155. Thiolase. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHER	PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
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 Resources
NextBio	605101.

Entry information

Entry name

THIL_RAT

Accession

Primary (citable) accession number: P17764

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	November 3, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)