ERG20_GANLU
ID ERG20_GANLU Reviewed; 360 AA.
AC B4YA15;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Farnesyl pyrophosphate synthase {ECO:0000250|UniProtKB:P08524};
DE Short=FPP synthase {ECO:0000250|UniProtKB:P08524};
DE Short=FPS {ECO:0000303|PubMed:18540102};
DE EC=2.5.1.10 {ECO:0000250|UniProtKB:P08524};
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000250|UniProtKB:P08524};
DE AltName: Full=Dimethylallyltranstransferase {ECO:0000250|UniProtKB:P08524};
DE EC=2.5.1.1 {ECO:0000250|UniProtKB:P08524};
DE AltName: Full=Farnesyl diphosphate synthase {ECO:0000303|PubMed:18540102};
DE AltName: Full=Geranyltranstransferase {ECO:0000250|UniProtKB:P08524};
GN Name=FPS {ECO:0000303|PubMed:18540102};
OS Ganoderma lucidum (Ling zhi medicinal fungus) (Bracket fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=5315;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND INDUCTION.
RX PubMed=18540102; DOI=10.1271/bbb.80067;
RA Ding Y.X., Ou-Yang X., Shang C.H., Ren A., Shi L., Li Y.X., Zhao M.W.;
RT "Molecular cloning, characterization, and differential expression of a
RT farnesyl-diphosphate synthase gene from the basidiomycetous fungus
RT Ganoderma lucidum.";
RL Biosci. Biotechnol. Biochem. 72:1571-1579(2008).
RN [2]
RP FUNCTION.
RC STRAIN=HG;
RX PubMed=22203490; DOI=10.1007/s11033-011-1431-9;
RA Shi L., Qin L., Xu Y., Ren A., Fang X., Mu D., Tan Q., Zhao M.;
RT "Molecular cloning, characterization, and function analysis of a mevalonate
RT pyrophosphate decarboxylase gene from Ganoderma lucidum.";
RL Mol. Biol. Rep. 39:6149-6159(2012).
RN [3]
RP INDUCTION.
RX PubMed=30821132; DOI=10.1111/1751-7915.13381;
RA Xu J.W., Yue T.H., Yu X., Zhao P., Li T., Li N.;
RT "Enhanced production of individual ganoderic acids by integrating
RT Vitreoscilla haemoglobin expression and calcium ion induction in liquid
RT static cultures of Ganoderma lingzhi.";
RL Microb. Biotechnol. 12:1180-1187(2019).
RN [4]
RP FUNCTION, AND PATHWAY.
RX PubMed=31253150; DOI=10.1186/s12934-019-1164-3;
RA Fei Y., Li N., Zhang D.H., Xu J.W.;
RT "Increased production of ganoderic acids by overexpression of homologous
RT farnesyl diphosphate synthase and kinetic modeling of ganoderic acid
RT production in Ganoderma lucidum.";
RL Microb. Cell Fact. 18:115-115(2019).
CC -!- FUNCTION: Farnesyl pyrophosphate synthase; part of the second module of
CC ergosterol biosynthesis pathway that includes the middle steps of the
CC pathway (By similarity). The second module involves the formation of
CC farnesyl diphosphate, which is also an important intermediate in the
CC biosynthesis of ubiquinone, dolichol, heme and prenylated proteins (By
CC similarity). This module also plays a key role in the biosynthesis of
CC triterpenes such as ganoderic acids (GA), a group of highly oxygenated
CC lanostane-type triterpenoids which are well recognized as a main group
CC of unique bioactive compounds in the medicinal mushroom Ganoderma
CC lucidum (PubMed:22203490, PubMed:31253150). Activity by the mevalonate
CC kinase first converts mevalonate into 5-phosphomevalonate (By
CC similarity). 5-phosphomevalonate is then further converted to 5-
CC diphosphomevalonate by the phosphomevalonate kinase (By similarity).
CC The diphosphomevalonate decarboxylase MVD then produces isopentenyl
CC diphosphate (PubMed:22203490). The isopentenyl-diphosphate delta-
CC isomerase then catalyzes the 1,3-allylic rearrangement of the
CC homoallylic substrate isopentenyl (IPP) to its highly electrophilic
CC allylic isomer, dimethylallyl diphosphate (DMAPP) (By similarity).
CC Finally the farnesyl diphosphate synthase FPS catalyzes the sequential
CC condensation of isopentenyl pyrophosphate with dimethylallyl
CC pyrophosphate, and then with the resultant geranylpyrophosphate to the
CC ultimate product farnesyl pyrophosphate (PubMed:18540102,
CC PubMed:31253150). {ECO:0000250|UniProtKB:P32377,
CC ECO:0000269|PubMed:18540102, ECO:0000269|PubMed:22203490,
CC ECO:0000269|PubMed:31253150}.
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:0000250|UniProtKB:P08524};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409;
CC Evidence={ECO:0000250|UniProtKB:P08524};
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:0000250|UniProtKB:P08524};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362;
CC Evidence={ECO:0000250|UniProtKB:P08524};
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:0000250|UniProtKB:P08524}.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000250|UniProtKB:P08524}.
CC -!- INDUCTION: Expression is induced in ganoderic acid (GA) producing
CC conditions. {ECO:0000269|PubMed:30821132}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; EU399544; ACB37020.1; -; Genomic_DNA.
DR EMBL; EU399545; ACB37021.1; -; mRNA.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Transferase.
FT CHAIN 1..360
FT /note="Farnesyl pyrophosphate synthase"
FT /id="PRO_0000454392"
FT BINDING 52
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 55
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 90
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 106
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 107
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 194
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 195
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 237
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 254
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 263
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 360 AA; 41014 MW; CEEB90B7CC631C56 CRC64;
MADAKAQKRQ KFDNVFPKLR EELLAYLNQE GMPQDAVSWF QRNLDYNVPG GKLNRGISVV
DSVEILKGRK LNDDEYFKAA LLGWCVEFLQ AFFLVSDDMM DQSVTRRGQP CWFRVEGINL
IAINDSFMLE GAIYYLLKKH FRSEPYYVHL LELFHDTTFQ TEIGQLIDLI TAPEDHVDLS
KFSLAKHQKI VIYKTAYYSF YLPVALAMYT CGVPHAPAND PYALAQSILI PLGEYFQVQD
DFLDFAAPPE VLGKVGTDIV DNKCSWCVNA ALARASPAQR RVLDDNYGLK DKEAEARVKA
LYEELGIRDE FAAYEERAYA RIVGLIETIP AEGADVGAGD VRLKREVFKA FLDKIYKRQK
