ERG10_SACMO
ID ERG10_SACMO Reviewed; 398 AA.
AC P10551; F8KA90;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000303|PubMed:2900076};
DE EC=2.3.1.9 {ECO:0000269|PubMed:2900076};
DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000303|PubMed:2900076};
DE AltName: Full=Ergosterol biosynthesis protein 10 {ECO:0000303|PubMed:2900076};
GN Name=ERG10 {ECO:0000303|PubMed:2900076};
OS Saccharomyces pastorianus (strain ATCC 76670 / Carlsberg bottom yeast no.2
OS / CBS 1503 / CLIB 180 / NBRC 10610 / NRRL Y-1525) (Saaz-type lager yeast)
OS (Saccharomyces monacensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1429090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND PATHWAY.
RX PubMed=2900076; DOI=10.1007/bf02427752;
RA Dequin S., Gloeckler R., Herbert C.J., Boutelet B.;
RT "Cloning, sequencing and analysis of the yeast S. uvarum ERG10 gene
RT encoding acetoacetyl CoA thiolase.";
RL Curr. Genet. 13:471-478(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76670 / Carlsberg bottom yeast no.2 / CBS 1503 / CLIB 180 /
RC NBRC 10610 / NRRL Y-1525;
RX PubMed=21998701; DOI=10.1371/journal.pone.0025821;
RA Nguyen H.V., Legras J.L., Neuveglise C., Gaillardin C.;
RT "Deciphering the hybridisation history leading to the Lager lineage based
RT on the mosaic genomes of Saccharomyces bayanus strains NBRC1948 and
RT CBS380.";
RL PLoS ONE 6:E25821-E25821(2011).
CC -!- FUNCTION: Acetyl-CoA acetyltransferase; part of the first module of
CC ergosterol biosynthesis pathway that includes the early steps of the
CC pathway, conserved across all eukaryotes, and which results in the
CC formation of mevalonate from acetyl-coenzyme A (acetyl-CoA)
CC (PubMed:2900076). In this module, the acetyl-CoA acetyltransferase
CC ERG10 catalyzes the formation of acetoacetyl-CoA (PubMed:2900076). The
CC hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with
CC acetoacetyl-CoA to form HMG-CoA (By similarity). The rate-limiting step
CC of the early module is the reduction to mevalonate by the 3-hydroxy-3-
CC methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are
CC derived from a single ancestral HMGR gene by gene duplication (By
CC similarity). {ECO:0000250|UniProtKB:P41338,
CC ECO:0000269|PubMed:2900076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10020,
CC ECO:0000269|PubMed:2900076};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC {ECO:0000269|PubMed:2900076}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P41338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2900076}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; X07976; CAA30788.1; -; Genomic_DNA.
DR EMBL; FR845802; CCA60782.1; -; Genomic_DNA.
DR AlphaFoldDB; P10551; -.
DR SMR; P10551; -.
DR UniPathway; UPA00058; UER00101.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cytoplasm; Metal-binding; Potassium;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT CHAIN 2..398
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000206417"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT BINDING 186
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 231
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 248
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 249
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 251
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 252
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 350
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P24752"
SQ 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
