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Database: UniProt
Entry: A0A0N8GJS7_9SPHN
LinkDB: A0A0N8GJS7_9SPHN
Original site: A0A0N8GJS7_9SPHN 
ID   A0A0N8GJS7_9SPHN        Unreviewed;       302 AA.
AC   A0A0N8GJS7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Farnesyl-diphosphate synthase {ECO:0000313|EMBL:KPL67730.1};
GN   ORFNames=SZ64_06120 {ECO:0000313|EMBL:KPL67730.1};
OS   Erythrobacter sp. SG61-1L.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL67730.1, ECO:0000313|Proteomes:UP000049978};
RN   [1] {ECO:0000313|EMBL:KPL67730.1, ECO:0000313|Proteomes:UP000049978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG61-1L {ECO:0000313|EMBL:KPL67730.1,
RC   ECO:0000313|Proteomes:UP000049978};
RA   Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA   Pandey G.;
RT   "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT   from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT   of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL   Appl. Environ. Microbiol. 0:0-0(2015).
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:KPL67730.1}.
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DR   EMBL; JXQC01000003; KPL67730.1; -; Genomic_DNA.
DR   RefSeq; WP_054530002.1; NZ_JXQC01000003.1.
DR   AlphaFoldDB; A0A0N8GJS7; -.
DR   STRING; 1603897.SZ64_06120; -.
DR   PATRIC; fig|1603897.4.peg.1131; -.
DR   OrthoDB; 9805316at2; -.
DR   Proteomes; UP000049978; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; 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; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   PANTHER; PTHR43281; FARNESYL DIPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR43281:SF1; FARNESYL DIPHOSPHATE SYNTHASE; 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; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW   Transferase {ECO:0000256|RuleBase:RU004466}.
SQ   SEQUENCE   302 AA;  32761 MW;  D34E76382F65FE9F CRC64;
     MAISGLEDGV LARGLERIAI DIDKAFDDLL PLPEDARRRL VEAMRYATIG GGKRLRPLLL
     AATADLYGVD RAQAVRAGAA IEAIHVYSLI HDDLPCMDND DLRHGKPTLH KKFDEATAVL
     AGDSLHALAF EILSDPRMSG DPFMRAELVV TLARASGHDG MAGGQMMDMA AETETFDLHT
     ITRLQQLKTG ALLGAAVEMG AILGRVPHEG RAHLRNYARD IGLAFQIVDD LLDHEGDPEK
     AGKALRKDDA QGKQTFVSLL GPERARDQAH ALVDQAIGHL AGHGKEADLL RAIARFIVER
     DR
//
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