ERG10_CANAL
ID ERG10_CANAL Reviewed; 402 AA.
AC A0A1D8PH52;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000303|PubMed:15215138};
DE EC=2.3.1.9 {ECO:0000250|UniProtKB:P41338};
DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000303|PubMed:15215138};
DE AltName: Full=Ergosterol biosynthesis protein 10 {ECO:0000303|PubMed:15215138};
GN Name=ERG10 {ECO:0000303|PubMed:15215138};
GN Synonyms=POT14 {ECO:0000303|PubMed:15820985}; OrderedLocusNames=orf19.1591;
GN ORFNames=CAALFM_C204310WA;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION.
RX PubMed=11353609; DOI=10.1128/aac.45.6.1660-1670.2001;
RA De Backer M.D., Ilyina T., Ma X.J., Vandoninck S., Luyten W.H.,
RA Vanden Bossche H.;
RT "Genomic profiling of the response of Candida albicans to itraconazole
RT treatment using a DNA microarray.";
RL Antimicrob. Agents Chemother. 45:1660-1670(2001).
RN [5]
RP FUNCTION.
RX PubMed=14653518; DOI=10.1080/1369378031000137233;
RA Song J.L., Lyons C.N., Holleman S., Oliver B.G., White T.C.;
RT "Antifungal activity of fluconazole in combination with lovastatin and
RT their effects on gene expression in the ergosterol and prenylation pathways
RT in Candida albicans.";
RL Med. Mycol. 41:417-425(2003).
RN [6]
RP INDUCTION.
RX PubMed=15215138; DOI=10.1128/aac.48.7.2733-2735.2004;
RA Hooshdaran M.Z., Barker K.S., Hilliard G.M., Kusch H., Morschhaeuser J.,
RA Rogers P.D.;
RT "Proteomic analysis of azole resistance in Candida albicans clinical
RT isolates.";
RL Antimicrob. Agents Chemother. 48:2733-2735(2004).
RN [7]
RP INDUCTION.
RX PubMed=15820985; DOI=10.1093/jac/dki088;
RA Copping V.M.S., Barelle C.J., Hube B., Gow N.A.R., Brown A.J.P., Odds F.C.;
RT "Exposure of Candida albicans to antifungal agents affects expression of
RT SAP2 and SAP9 secreted proteinase genes.";
RL J. Antimicrob. Chemother. 55:645-654(2005).
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) (By
CC similarity). ERG10 catalyzes the formation of acetoacetyl-CoA from
CC acetyl-CoA (By similarity). The first module starts with the action of
CC the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the
CC formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase
CC ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA.
CC The 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase HMG1
CC finally reduces HMG-CoA to produce mevalonate (Probable).
CC {ECO:0000250|UniProtKB:P41338, ECO:0000305|PubMed:14653518}.
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:0000250|UniProtKB:P41338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037;
CC Evidence={ECO:0000250|UniProtKB:P41338};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC {ECO:0000250|UniProtKB:P41338}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P41338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P41338}.
CC -!- INDUCTION: Expression is up-regulated in azole resistant clinical
CC isolates (PubMed:15215138). Expression is induced by exposure to arole
CC antifungals such as fluconazole, ketoconazole or itraconazole
CC (PubMed:11353609, PubMed:15820985). {ECO:0000269|PubMed:11353609,
CC ECO:0000269|PubMed:15215138, ECO:0000269|PubMed:15820985}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; CP017624; AOW27457.1; -; Genomic_DNA.
DR RefSeq; XP_710124.1; XM_705032.1.
DR AlphaFoldDB; A0A1D8PH52; -.
DR SMR; A0A1D8PH52; -.
DR STRING; 237561.A0A1D8PH52; -.
DR GeneID; 3648275; -.
DR KEGG; cal:CAALFM_C204310WA; -.
DR CGD; CAL0000184591; ERG10.
DR VEuPathDB; FungiDB:C2_04310W_A; -.
DR eggNOG; KOG1390; Eukaryota.
DR OMA; ICPSIAI; -.
DR OrthoDB; 1011220at2759; -.
DR UniPathway; UPA00058; UER00101.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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; 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.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Potassium; Reference proteome; Steroid biosynthesis;
KW Transferase.
FT CHAIN 1..402
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000454163"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT ACT_SITE 352
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT BINDING 185
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 185
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 230
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 250
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 251
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 348
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
SQ SEQUENCE 402 AA; 41935 MW; 4407A400CCE29D09 CRC64;
MVPPVYIVST ARTPIGSFQG TLSSLTYSDL GAHAVKAALN KVPQIKPEDV DEIVFGGVLQ
ANVGQAPARQ VALKAGLTDK IVASTVNKVC ASGLKAIIIG AQNIICGTSD IVVVGGAESM
TNTPYYLPTA RNGARFGDST LIDGIQKDGL LDVYEQKLMG VAAEKCAADH GFTREQQDEF
AIKSYQKAGN ALKQGKFNQE IAPVTIKGVR GKPDVVVEKD EEIEKFNEAK LKSARAVFQK
ENGTVTGPNA SKINDGAAAL ILVSEAKLKE LGLKPLAKIN GWGEAARNPI DFTIAPALAV
PKAVKHAGLT LDQVDFFELN EAFSVVGLAN AEICQIPLEK LNAYGGAVAL GHPLGCSGAR
IVVTLLSVLI QEGGKIGCAG VCNGGGGASS IVIEKVDSDF KL
