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Acetyl-CoA acetyltransferase (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) (Ergosterol biosynthesis protein 10)

 THIL_SCHPO              Reviewed;         395 AA.
Q9UQW6; P78835; Q1L848;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 109.
RecName: Full=Acetyl-CoA acetyltransferase;
EC=2.3.1.9;
AltName: Full=Acetoacetyl-CoA thiolase;
AltName: Full=Ergosterol biosynthesis protein 10;
Name=erg10; ORFNames=SPBC215.09c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=PR745;
PubMed=9501991; DOI=10.1093/dnares/4.6.363;
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
"Identification of open reading frames in Schizosaccharomyces pombe
cDNAs.";
DNA Res. 4:363-369(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
-!- FUNCTION: Catalyzes the formation of acetoacetyl-CoA in the
biosynthesis of mevalonate, an intermediate required for the
biosynthesis of sterols and nonsterol isoprenoids. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
{ECO:0000255|PROSITE-ProRule:PRU10020}.
-!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
-!- SIMILARITY: Belongs to the thiolase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D89184; BAA13846.1; -; mRNA.
EMBL; CU329671; CAA22123.1; -; Genomic_DNA.
PIR; T39899; T39899.
PIR; T42741; T42741.
RefSeq; NP_596686.1; NM_001022609.2.
ProteinModelPortal; Q9UQW6; -.
SMR; Q9UQW6; -.
BioGrid; 277142; 3.
MINT; MINT-4706810; -.
STRING; 4896.SPBC215.09c.1; -.
iPTMnet; Q9UQW6; -.
MaxQB; Q9UQW6; -.
PRIDE; Q9UQW6; -.
EnsemblFungi; SPBC215.09c.1; SPBC215.09c.1:pep; SPBC215.09c.
GeneID; 2540616; -.
KEGG; spo:SPBC215.09c; -.
EuPathDB; FungiDB:SPBC215.09c; -.
PomBase; SPBC215.09c; erg10.
HOGENOM; HOG000012238; -.
InParanoid; Q9UQW6; -.
KO; K00626; -.
OMA; LMAGQGQ; -.
OrthoDB; EOG092C2K2G; -.
PhylomeDB; Q9UQW6; -.
Reactome; R-SPO-70895; Branched-chain amino acid catabolism.
Reactome; R-SPO-77108; Utilization of Ketone Bodies.
Reactome; R-SPO-77111; Synthesis of Ketone Bodies.
UniPathway; UPA00058; UER00101.
PRO; PR:Q9UQW6; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0005829; C:cytosol; IDA:PomBase.
GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; ISS:PomBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006696; P:ergosterol biosynthetic process; ISS:PomBase.
GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
CDD; cd00751; thiolase; 1.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR002155; Thiolase.
InterPro; IPR016039; Thiolase-like.
InterPro; IPR020610; Thiolase_AS.
InterPro; IPR020617; Thiolase_C.
InterPro; IPR020613; Thiolase_CS.
InterPro; IPR020616; Thiolase_N.
Pfam; PF02803; Thiolase_C; 1.
Pfam; PF00108; Thiolase_N; 1.
PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
SUPFAM; SSF53901; SSF53901; 2.
TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
PROSITE; PS00737; THIOLASE_2; 1.
PROSITE; PS00099; THIOLASE_3; 1.
2: Evidence at transcript level;
Acyltransferase; Complete proteome; Cytoplasm; Metal-binding;
Potassium; Reference proteome; Transferase.
CHAIN 1 395 Acetyl-CoA acetyltransferase.
/FTId=PRO_0000310395.
ACT_SITE 90 90 Acyl-thioester intermediate.
{ECO:0000250}.
ACT_SITE 351 351 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10020}.
ACT_SITE 381 381 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10020}.
METAL 185 185 Potassium. {ECO:0000250}.
METAL 246 246 Potassium; via carbonyl oxygen.
{ECO:0000250}.
METAL 247 247 Potassium; via carbonyl oxygen.
{ECO:0000250}.
METAL 249 249 Potassium; via carbonyl oxygen.
{ECO:0000250}.
METAL 347 347 Potassium; via carbonyl oxygen.
{ECO:0000250}.
BINDING 185 185 Coenzyme A. {ECO:0000250}.
BINDING 230 230 Coenzyme A. {ECO:0000250}.
BINDING 250 250 Coenzyme A. {ECO:0000250}.
CONFLICT 387 387 A -> P (in Ref. 1; BAA13846).
{ECO:0000305}.
SEQUENCE 395 AA; 40998 MW; 382822A9EF686544 CRC64;
MVNTEVYIVS AVRTPMGSFG GSFASLPATK LGSIAIKGAL ERVNIKPSDV DEVFMGNVVS
ANLGQNPARQ CALGAGLPRS IVCTTVNKVC ASGMKATILG AQTIMTGNAE IVVAGGTESM
SNAPYYAPKN RFGAKYGNVE LVDGLLRDGL SDAYDGLPMG NAAELCAEEH SIDRASQDAF
AISSYKRAQN AQATKAFEQE IVPVEVPVGR GKPNKLVTED EEPKNLNEDK LKSVRAVFKS
NGTVTAANAS TLNDGASALV LMSAAKVKEL GLKPLAKIIG WGEAAQDPER FTTSPSLAIP
KALKHAGIEA SQVDYYEINE AFSVVAVANT KILGLDPERV NINGGGVAMG HPLGSSGSRI
ICTLAYILAQ KDAKIGVAAV CNGGGGASSI VIERV


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