Reviewed, UniProtKB/Swiss-Prot Q8HXY6 (THIL_MACFA)

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
ORF Names:	QtrA-14294

Organism

Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey)

Taxonomic identifier

9541 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length	427 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)

Function	Plays a major role in ketone body metabolism By similarity.
Catalytic activity	2 acetyl-CoA = CoA + acetoacetyl-CoA.
Enzyme regulation	Activated by potassium ions, but not sodium ions By similarity.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion By similarity.
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
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acetyltransferase activity Inferred from electronic annotation. Source: EC 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 – 33	33	Mitochondrion By similarity
	Chain	34 – 427	394	Acetyl-CoA acetyltransferase, mitochondrial		PRO_0000034086
Regions
	Region	258 – 260	3	Coenzyme A binding By similarity
Sites
	Active site	126	1	Acyl-thioester intermediate By similarity
	Active site	385	1	Proton acceptor By similarity
	Active site	413	1	Proton acceptor By similarity
	Metal binding	219	1	Potassium By similarity
	Metal binding	280	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	281	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	283	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	381	1	Potassium; via carbonyl oxygen By similarity
	Binding site	219	1	Coenzyme A By similarity
	Binding site	263	1	Coenzyme A By similarity
	Binding site	284	1	Coenzyme A By similarity
Amino acid modifications
	Modified residue	83	1	N6-acetyllysine By similarity
	Modified residue	174	1	N6-acetyllysine By similarity
	Modified residue	181	1	N6-acetyllysine By similarity
	Modified residue	190	1	N6-acetyllysine By similarity
	Modified residue	230	1	N6-acetyllysine By similarity
	Modified residue	251	1	N6-acetyllysine By similarity
	Modified residue	263	1	N6-acetyllysine By similarity
	Modified residue	338	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8HXY6-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: D44BEC44A38AF478	FASTA	427	45,200
	10 20 30 40 50 60 MAVLAALLRG GARSRSPLLR RLVQEIRYVE RSYVSKPTLK EVVIVSATRT PIGSFLGSLS 70 80 90 100 110 120 LLPTTKLGSI AMQGAIEKAG IPKEEVKEAY MGNVLQGGEG QAPARQAVLG AGLPISTPRT 130 140 150 160 170 180 TINKVCASGM KAIMMASQSL MCGHQDVMVA GGMESMSNVP YVMNRGSTPY GGVKLEDLIV 190 200 210 220 230 240 KDGLTDVYNK IHMGSCAENT AKKLNIARDE QDAYAINSYT RSKAAWEAGK FGNEVIPVTV 250 260 270 280 290 300 TVKGQPDVVV KEDEEYKRVD FSKVPKLKTV FQKENGTITA ANASTLNDGA AALVLMTAGA 310 320 330 340 350 360 AKRLNVTPLA RIVAFADAAV EPIDFPIAPV HAVSMVLKDV GLKKEDIAMW EVNEAFSLVV 370 380 390 400 410 420 LANIKMLEID PQKVNINGGA VSLGHPIGMS GARIVGHLTH ALKQGEYGLA SICNGGGGAS AMLIQKL

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
EMBLGenBankDDBJ	AB083303 mRNA. Translation: BAC20582.1.
3D structure databases
HSSP	HSSP built from PDB template 1M4T based on UniProtKB P07097.
SMR	Q8HXY6. Positions 35-427.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q8HXY6.
Enzyme and pathway databases
BRENDA	2.3.1.9. 3438.
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...

Entry information

Entry name

THIL_MACFA

Accession

Primary (citable) accession number: Q8HXY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	March 1, 2003
Last modified:	October 13, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)