Reviewed, UniProtKB/Swiss-Prot P41338 (THIL_YEAST)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA acetyltransferase
    EC=2.3.1.9
Alternative name(s):
    Acetoacetyl-CoA thiolase
    Ergosterol biosynthesis protein 10

Gene names

Name:	ERG10
Ordered Locus Names:	YPL028W
ORF Names:	LPB3

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	398 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	Catalyzes the formation of acetoacetyl-CoA in the biosynthesis of mevalonate, an intermediate required for the biosynthesis of sterols and nonsterol isoprenoids.
Catalytic activity	2 acetyl-CoA = CoA + acetoacetyl-CoA.
Pathway	Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Subunit structure	Multimeric.
Subcellular location	Cytoplasm.
Induction	Induced by low intracellular sterol levels. Ref.5
Miscellaneous	Present with 60895 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the thiolase family.
Biophysicochemical properties	Kinetic parameters: KM=0.16 mM for CoA KM=0.35 mM for acetoacetyl-CoA pH dependence: Optimum pH is 8.8.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Potassium
Molecular function	Acyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acetyltransferase activity Ref.1 Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-19240,EBI-19240
HSV2	P50079	1	EBI-19240,EBI-23505
SKS1	Q12505	1	EBI-19240,EBI-17297
SSA2	P10592	1	EBI-19240,EBI-8603

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 398	397	Acetyl-CoA acetyltransferase		PRO_0000206416
Sites
	Active site	91	1	Acyl-thioester intermediate By similarity
	Active site	354	1	Proton acceptor By similarity
	Active site	384	1	Proton acceptor By similarity
	Metal binding	186	1	Potassium By similarity
	Metal binding	248	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	249	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	251	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	350	1	Potassium; via carbonyl oxygen By similarity
	Binding site	186	1	Coenzyme A By similarity
	Binding site	231	1	Coenzyme A By similarity
	Binding site	252	1	Coenzyme A By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.3
	Modified residue	24	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P41338-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E835A8E040629A5C	FASTA	398	41,729
	10 20 30 40 50 60 MSQNVYIVST ARTPIGSFQG SLSSKTAVEL GAVALKGALA KVPELDASKD FDEIIFGNVL 70 80 90 100 110 120 SANLGQAPAR QVALAAGLSN HIVASTVNKV CASAMKAIIL GAQSIKCGNA DVVVAGGCES 130 140 150 160 170 180 MTNAPYYMPA ARAGAKFGQT VLVDGVERDG LNDAYDGLAM GVHAEKCARD WDITREQQDN 190 200 210 220 230 240 FAIESYQKSQ KSQKEGKFDN EIVPVTIKGF RGKPDTQVTK DEEPARLHVE KLRSARTVFQ 250 260 270 280 290 300 KENGTVTAAN ASPINDGAAA VILVSEKVLK EKNLKPLAII KGWGEAAHQP ADFTWAPSLA 310 320 330 340 350 360 VPKALKHAGI EDINSVDYFE FNEAFSVVGL VNTKILKLDP SKVNVYGGAV ALGHPLGCSG 370 380 390 ARVVVTLLSI LQQEGGKIGV AAICNGGGGA SSIVIEKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ERG10 from Saccharomyces cerevisiae encodes acetoacetyl-CoA thiolase." Hiser L.M., Basson M.E., Rine J. J. Biol. Chem. 269:31383-31389(1994) [PubMed: 7989303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Bienvenut W.V., Peters C. Submitted (JUN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-36 AND 137-148, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY.
[4]	"Two forms of acetoacetyl coenzyme A thiolase in yeast. I. Separation and properties." Kornblatt J.A., Rudney H. J. Biol. Chem. 246:4417-4423(1971) [PubMed: 5571829] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[5]	"Transcriptional regulation of a sterol-biosynthetic enzyme by sterol levels in Saccharomyces cerevisiae." Dimster-Denk D., Rine J. Mol. Cell. Biol. 16:3981-3989(1996) [PubMed: 8754796] [Abstract] Cited for: INDUCTION.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L20428 Genomic DNA. Translation: AAA62378.1. U36624 Genomic DNA. Translation: AAB68159.1.
PIR	A55654.
RefSeq	NP_015297.1.
3D structure databases
HSSP	HSSP built from PDB template 1PXT based on UniProtKB P27796.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6396N.
IntAct	P41338. 8 interactions.
STRING	P41338.
Proteomic databases
PeptideAtlas	P41338.
PRIDE	P41338.
Genome annotation databases
Ensembl	YPL028W; YPL028W; YPL028W; Saccharomyces cerevisiae. [Genome view]
GeneID	856079.
GenomeReviews	Gene locus YPL028W in contig U00094_GR.
KEGG	sce:YPL028W.
NMPDR	fig|4932.3.peg.6431.
Organism-specific databases
CYGD	YPL028w.
SGD	S000005949. ERG10.
Phylogenomic databases
HOGENOM	P41338.
OMA	KVCASAM.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-647.
BRENDA	2.3.1.9. 250.
Gene expression databases
ArrayExpress	P41338.
Genevestigator	P41338.
GermOnline	YPL028W. Saccharomyces cerevisiae.
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	981086.

Entry information

Entry name

THIL_YEAST

Accession

Primary (citable) accession number: P41338

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)