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

 THIL_SACMO              Reviewed;         398 AA.
P10551; F8KA90;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
30-AUG-2017, entry version 94.
RecName: Full=Acetyl-CoA acetyltransferase;
EC=2.3.1.9;
AltName: Full=Acetoacetyl-CoA thiolase;
AltName: Full=Ergosterol biosynthesis protein 10;
Name=ERG10;
Saccharomyces pastorianus (strain ATCC 76670 / Carlsberg bottom yeast
no.2 / CBS 1503 / CLIB 180 / NBRC 10610 / NRRL Y-1525) (Saaz-type
lager yeast) (Saccharomyces monacensis).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=1429090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2900076; DOI=10.1007/BF02427752;
Dequin S., Gloeckler R., Herbert C.J., Boutelet B.;
"Cloning, sequencing and analysis of the yeast S. uvarum ERG10 gene
encoding acetoacetyl CoA thiolase.";
Curr. Genet. 13:471-478(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 76670 / Carlsberg bottom yeast no.2 / CBS 1503 / CLIB 180
/ NBRC 10610 / NRRL Y-1525;
PubMed=21998701; DOI=10.1371/journal.pone.0025821;
Nguyen H.V., Legras J.L., Neuveglise C., Gaillardin C.;
"Deciphering the hybridisation history leading to the Lager lineage
based on the mosaic genomes of Saccharomyces bayanus strains NBRC1948
and CBS380.";
PLoS ONE 6:E25821-E25821(2011).
-!- FUNCTION: Catalyzes the formation of acetoacetyl-CoA in the
biosynthesis of mevalonate, an intermediate required for the
biosynthesis of sterols and nonsterol isoprenoids. {ECO:0007001}.
-!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
{ECO:0000270|PROSITE-ProRule:PRU10020}.
-!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
-!- SUBUNIT: Multimeric.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the thiolase family. {ECO:0000320}.
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EMBL; X07976; CAA30788.1; -; Genomic_DNA.
EMBL; FR845802; CCA60782.1; -; Genomic_DNA.
ProteinModelPortal; P10551; -.
SMR; P10551; -.
UniPathway; UPA00058; UER00101.
GO; GO:0005737; C:cytoplasm; RCA:UniProtKB-SubCell.
GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; RCA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; RCA:UniProtKB-KW.
GO; GO:0008152; P:metabolic process; RCA:InterPro.
CDD; cd00751; thiolase; 1.
Gene3D; 3.40.47.10; -; 3.
InterPro; IPR002155; Thiolase.
InterPro; IPR016039; Thiolase-like.
InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
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; PS00098; THIOLASE_1; 1.
PROSITE; PS00737; THIOLASE_2; 1.
PROSITE; PS00099; THIOLASE_3; 1.
3: Inferred from homology;
Acetylation; Acyltransferase; Cytoplasm; Metal-binding; Potassium;
Transferase.
INIT_MET 1 1 Removed. {ECO:0007001}.
CHAIN 2 398 Acetyl-CoA acetyltransferase.
/FTId=PRO_0000206417.
ACT_SITE 91 91 Acyl-thioester intermediate.
{ECO:0007001}.
ACT_SITE 354 354 Proton acceptor. {ECO:0000270|PROSITE-
ProRule:PRU10020}.
ACT_SITE 384 384 Proton acceptor. {ECO:0000270|PROSITE-
ProRule:PRU10020}.
METAL 186 186 Potassium. {ECO:0007001}.
METAL 248 248 Potassium; via carbonyl oxygen.
{ECO:0007001}.
METAL 249 249 Potassium; via carbonyl oxygen.
{ECO:0007001}.
METAL 251 251 Potassium; via carbonyl oxygen.
{ECO:0007001}.
METAL 350 350 Potassium; via carbonyl oxygen.
{ECO:0007001}.
BINDING 186 186 Coenzyme A. {ECO:0007001}.
BINDING 231 231 Coenzyme A. {ECO:0007001}.
BINDING 252 252 Coenzyme A. {ECO:0007001}.
MOD_RES 2 2 N-acetylserine. {ECO:0007001}.
SEQUENCE 398 AA; 41659 MW; C0AC394C17A925AB CRC64;
MSQNVYIVST ARTPIGSFQG SLSSKTAVEL GAAALKGALA KVPELDASKD FDEIIFGNVL
SANLGQAPAR QVALTAGLGN HIVATTVNKV CASAMKAIIL GAQSIKCGNA DVVVAGGCES
MTNAPYYMPA ARGGAKFGQT VLIDGVERDG LNDAYDGLAM GVHAEKCARD WDITRDQQDS
FAIESYQKSQ QSQKEGKFDN EIVPVTIKGF RGKPDTQVTN DEEPARLHVE KLKSARTVFQ
RENGTVTAAN ASPINDGAAA IILVSERVLK EKNLKPLAIV KGWGEAAHLP ADFTWAPSLA
VPKALKHAGI EDINSVDYFE FNEAFSVVGL VNTKILKLDP SKVNVYGGAV ALGHPLGCSG
ARVVVTLLSI LQQEGGKIGV AAICNGGGGA SSVVIEKL


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