ERG20_CANAL
ID ERG20_CANAL Reviewed; 351 AA.
AC A0A1D8PH78;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Farnesyl pyrophosphate synthase {ECO:0000250|UniProtKB:P08524};
DE Short=FPP synthase {ECO:0000250|UniProtKB:P08524};
DE Short=FPS {ECO:0000250|UniProtKB:P08524};
DE EC=2.5.1.10 {ECO:0000305|PubMed:14653518};
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000303|PubMed:14653518};
DE AltName: Full=Dimethylallyltranstransferase {ECO:0000250|UniProtKB:P08524};
DE EC=2.5.1.1 {ECO:0000305|PubMed:14653518};
DE AltName: Full=Farnesyl diphosphate synthase {ECO:0000303|PubMed:14653518};
DE AltName: Full=Geranyltranstransferase {ECO:0000303|PubMed:14653518};
GN Name=ERG20 {ECO:0000303|PubMed:14653518}; OrderedLocusNames=orf19.4491;
GN ORFNames=CAALFM_C204580WA;
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 FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND PATHWAY.
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).
CC -!- FUNCTION: Farnesyl pyrophosphate synthase; part of the second module of
CC ergosterol biosynthesis pathway that includes the middle steps of the
CC pathway (PubMed:14653518). ERG20 catalyzes the sequential condensation
CC of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then
CC with the resultant geranylpyrophosphate to the ultimate product
CC farnesyl pyrophosphate (PubMed:14653518). The second module is carried
CC out in the vacuole and involves the formation of farnesyl diphosphate,
CC which is also an important intermediate in the biosynthesis of
CC ubiquinone, dolichol, heme and prenylated proteins. Activity by the
CC mevalonate kinase ERG12 first converts mevalonate into 5-
CC phosphomevalonate. 5-phosphomevalonate is then further converted to 5-
CC diphosphomevalonate by the phosphomevalonate kinase ERG8. The
CC diphosphomevalonate decarboxylase MVD then produces isopentenyl
CC diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then
CC catalyzes the 1,3-allylic rearrangement of the homoallylic substrate
CC isopentenyl (IPP) to its highly electrophilic allylic isomer,
CC dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate
CC synthase ERG20 catalyzes the sequential condensation of isopentenyl
CC pyrophosphate with dimethylallyl pyrophosphate, and then with the
CC resultant geranylpyrophosphate to the ultimate product farnesyl
CC pyrophosphate (Probable). {ECO:0000269|PubMed:14653518,
CC ECO:0000305|PubMed:14653518}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-
CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:128769; EC=2.5.1.1;
CC Evidence={ECO:0000305|PubMed:14653518};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409;
CC Evidence={ECO:0000305|PubMed:14653518};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:175763; EC=2.5.1.10;
CC Evidence={ECO:0000305|PubMed:14653518};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362;
CC Evidence={ECO:0000305|PubMed:14653518};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000269|PubMed:14653518}.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000269|PubMed:14653518}.
CC -!- INDUCTION: Expression is increased in the presence of fluconazole and
CC decreased in the presence of lovastatin. {ECO:0000269|PubMed:14653518}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; CP017624; AOW27484.1; -; Genomic_DNA.
DR RefSeq; XP_712917.2; XM_707824.2.
DR AlphaFoldDB; A0A1D8PH78; -.
DR SMR; A0A1D8PH78; -.
DR STRING; 237561.A0A1D8PH78; -.
DR GeneID; 3645440; -.
DR KEGG; cal:CAALFM_C204580WA; -.
DR CGD; CAL0000188232; ERG20.
DR VEuPathDB; FungiDB:C2_04580W_A; -.
DR eggNOG; KOG0711; Eukaryota.
DR OrthoDB; 1066656at2759; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; ISS:CGD.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:EnsemblFungi.
DR GO; GO:0004337; F:geranyltranstransferase activity; ISS:CGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006696; P:ergosterol biosynthetic process; ISS:CGD.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; ISS:CGD.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR039702; FPS1-like.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR PANTHER; PTHR11525; PTHR11525; 1.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Reference proteome; Steroid biosynthesis; Transferase.
FT CHAIN 1..351
FT /note="Farnesyl pyrophosphate synthase"
FT /id="PRO_0000454170"
FT BINDING 51
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 54
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 92
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 108
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 109
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 196
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 197
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 236
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 253
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 262
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 351 AA; 40712 MW; C52EB77D6E5FBAF5 CRC64;
MSDKLAARER FLDVFEDLVE ELKQILVSYN MPQEAIEWFV RSLNYNTPGG KLNRGLSVVD
TFAILNNTTS DKLNDTEYKK VALLGWAIEL LQAYFLVADD MMDQSKTRRG QPCWYLVEGV
NNIAINDSFM LEGAIYILLK KHFRQDPYYV DLLDLFHEVT FQTELGQLLD LITADEEIVD
LDKFSLEKHS FIVIFKTAYY SFYLPVALAM YMSGINDEKD LKQVRDILIP LGEYFQIQDD
YLDCFGTPEQ IGKIGTDIKD NKCSWVINQA LLIATPEQRQ LLDNNYGKKD DESEQKCKDL
FKQLGIEKIY HDYEESIVAK LRKQIDQIDE SRGLKKDVLT AFLGKVYKRS K
