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Database: UniProt
Entry: I2JUQ2_DEKBR
LinkDB: I2JUQ2_DEKBR
Original site: I2JUQ2_DEKBR 
ID   I2JUQ2_DEKBR            Unreviewed;       353 AA.
AC   I2JUQ2;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Farnesyl pyrophosphate synthetase {ECO:0000313|EMBL:EIF46704.1};
GN   ORFNames=AWRI1499_3415 {ECO:0000313|EMBL:EIF46704.1};
OS   Brettanomyces bruxellensis AWRI1499.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Brettanomyces.
OX   NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF46704.1, ECO:0000313|Proteomes:UP000004997};
RN   [1] {ECO:0000313|EMBL:EIF46704.1, ECO:0000313|Proteomes:UP000004997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF46704.1,
RC   ECO:0000313|Proteomes:UP000004997};
RX   PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA   Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT   "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the
RT   Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL   PLoS ONE 7:E33840-E33840(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC       {ECO:0000256|RuleBase:RU004466}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIF46704.1}.
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DR   EMBL; AHIQ01000197; EIF46704.1; -; Genomic_DNA.
DR   AlphaFoldDB; I2JUQ2; -.
DR   Proteomes; UP000004997; Unassembled WGS sequence.
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:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 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:SF0; FARNESYL PYROPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR11525; FARNESYL-PYROPHOSPHATE SYNTHETASE; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01017; Polyprenyl_Transferase_Like; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004997};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004466}.
SQ   SEQUENCE   353 AA;  41128 MW;  7C30AF99C0947E00 CRC64;
     MKIDKKQSRE KFLTVFPQIV KETTDVLKSY GMPQDAIEWY TKNLNYNTPS GKLNRGLSVV
     DTYGILKGYE TYDDFSEDEY KLSAILGWCI ELLQAYFLVA DDIMDKSLTR RGHTCWYRVE
     EVQEIAVNDA FMLEGAIYIL LKKYFSKKPY YVKVMELFHD VTFKTECGQL LDLITAPEDK
     VDLAKFSLNK QMFIITYKTA FYSFYLPVAL AMHMAGVDDE SDLKQASDVL IPLGQYFQIQ
     DDYLDCFGKP EDIGKIGTDI QDNKCSWVVN TALEICNAEQ RKLLDENYGR KDPVKEKKCK
     DLFIALKIDD RFHQYEEDIV SKIRKNISNI DETRGFKKQT LTAFLDKIYK RKK
//
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