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Database: UniProt
Entry: V4P4X9_9CAUL
LinkDB: V4P4X9_9CAUL
Original site: V4P4X9_9CAUL 
ID   V4P4X9_9CAUL            Unreviewed;       303 AA.
AC   V4P4X9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Farnesyl-diphosphate synthase {ECO:0000313|EMBL:ESQ83141.1};
GN   ORFNames=AEAC466_14860 {ECO:0000313|EMBL:ESQ83141.1};
OS   Asticcacaulis sp. AC466.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ83141.1, ECO:0000313|Proteomes:UP000017826};
RN   [1] {ECO:0000313|EMBL:ESQ83141.1, ECO:0000313|Proteomes:UP000017826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC466 {ECO:0000313|EMBL:ESQ83141.1,
RC   ECO:0000313|Proteomes:UP000017826};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
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:ESQ83141.1}.
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DR   EMBL; AWGE01000014; ESQ83141.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4P4X9; -.
DR   STRING; 1282362.AEAC466_14860; -.
DR   PATRIC; fig|1282362.3.peg.2937; -.
DR   eggNOG; COG0142; Bacteria.
DR   OrthoDB; 9805316at2; -.
DR   Proteomes; UP000017826; 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; PS00723; POLYPRENYL_SYNTHASE_1; 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:UP000017826};
KW   Transferase {ECO:0000256|RuleBase:RU004466}.
SQ   SEQUENCE   303 AA;  32748 MW;  8016B9D6AF81A741 CRC64;
     MTPVAANSDL PPLMARMAET ADLVTMALDE LLPRGEGPEA RLTEAMRYAA LGPGKRLRPF
     FALEAARLFD AEENAVLRAA CALECIHAYS LIHDDLPCMD DDDIRRGQLT VHRAYDEATA
     VLAGDALQSV AFEILASEDT HEDPQVRVDL IRMLAQASGA QGMAGGQMID LIGVSDDLGG
     VARMQRLKTG ALIVYAFQIP LIIADAPEKD GMALMHFAQD LGLAYQIADD LLDVEGDPDL
     LGKGAGGKDA AKGKTNFVTL LGLDEAKSRV QILSEQAKSR LDIFGARARY LRESVDFVLN
     RRN
//
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