Reviewed, UniProtKB/Swiss-Prot Q9UQW6 (THIL_SCHPO)

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
ORF Names:	SPBC215.09c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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 By similarity.
Catalytic activity	2 acetyl-CoA = CoA + acetoacetyl-CoA.
Pathway	Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Subcellular location	Cytoplasm. Ref.3
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Potassium
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Ref.3 Inferred from direct assay. Source: GeneDB_SPombe
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
	Chain	1 – 395	395	Acetyl-CoA acetyltransferase		PRO_0000310395
Sites
	Active site	90	1	Acyl-thioester intermediate By similarity
	Active site	351	1	Proton acceptor By similarity
	Active site	381	1	Proton acceptor By similarity
	Metal binding	185	1	Potassium By similarity
	Metal binding	246	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	247	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	249	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	347	1	Potassium; via carbonyl oxygen By similarity
	Binding site	185	1	Coenzyme A By similarity
	Binding site	230	1	Coenzyme A By similarity
	Binding site	250	1	Coenzyme A By similarity
Experimental info
	Sequence conflict	387	1	A → P in BAA13846. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UQW6-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 382822A9EF686544	FASTA	395	40,998
	10 20 30 40 50 60 MVNTEVYIVS AVRTPMGSFG GSFASLPATK LGSIAIKGAL ERVNIKPSDV DEVFMGNVVS 70 80 90 100 110 120 ANLGQNPARQ CALGAGLPRS IVCTTVNKVC ASGMKATILG AQTIMTGNAE IVVAGGTESM 130 140 150 160 170 180 SNAPYYAPKN RFGAKYGNVE LVDGLLRDGL SDAYDGLPMG NAAELCAEEH SIDRASQDAF 190 200 210 220 230 240 AISSYKRAQN AQATKAFEQE IVPVEVPVGR GKPNKLVTED EEPKNLNEDK LKSVRAVFKS 250 260 270 280 290 300 NGTVTAANAS TLNDGASALV LMSAAKVKEL GLKPLAKIIG WGEAAQDPER FTTSPSLAIP 310 320 330 340 350 360 KALKHAGIEA SQVDYYEINE AFSVVAVANT KILGLDPERV NINGGGVAMG HPLGSSGSRI 370 380 390 ICTLAYILAQ KDAKIGVAAV CNGGGGASSI VIERV

References

[1]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: PR745.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D89184 mRNA. Translation: BAA13846.1. CU329671 Genomic DNA. Translation: CAA22123.1.
PIR	T39899. T42741.
RefSeq	NP_596686.1.
3D structure databases
HSSP	HSSP built from PDB template 1M3K based on UniProtKB P07097.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UQW6.
Genome annotation databases
GeneID	2540616.
GenomeReviews	Gene locus erg10 in contig CU329671_GR.
KEGG	spo:SPBC215.09c.
NMPDR	fig|4896.1.peg.2552.
Organism-specific databases
GeneDB_Spombe	SPBC215.09c.
Phylogenomic databases
OMA	KVCASAM.
Enzyme and pathway databases
BRENDA	2.3.1.9. 653.
Gene expression databases
ArrayExpress	Q9UQW6.
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	PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THIL_SCHPO

Accession

Primary (citable) accession number: Q9UQW6
Secondary accession number(s): P78835, Q1L848

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)