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Database: UniProt
Entry: Q2S1E5_SALRD
LinkDB: Q2S1E5_SALRD
Original site: Q2S1E5_SALRD 
ID   Q2S1E5_SALRD            Unreviewed;       342 AA.
AC   Q2S1E5;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Polyprenyl synthetase {ECO:0000313|EMBL:ABC46321.1};
GN   Name=idsA {ECO:0000313|EMBL:ABC46321.1};
GN   OrderedLocusNames=SRU_1874 {ECO:0000313|EMBL:ABC46321.1};
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC   Salinibacter.
OX   NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC46321.1, ECO:0000313|Proteomes:UP000008674};
RN   [1] {ECO:0000313|EMBL:ABC46321.1, ECO:0000313|Proteomes:UP000008674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31
RC   {ECO:0000313|Proteomes:UP000008674};
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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}.
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DR   EMBL; CP000159; ABC46321.1; -; Genomic_DNA.
DR   RefSeq; YP_445986.1; NC_007677.1.
DR   AlphaFoldDB; Q2S1E5; -.
DR   STRING; 309807.SRU_1874; -.
DR   EnsemblBacteria; ABC46321; ABC46321; SRU_1874.
DR   KEGG; sru:SRU_1874; -.
DR   PATRIC; fig|309807.25.peg.1942; -.
DR   eggNOG; COG0142; Bacteria.
DR   HOGENOM; CLU_014015_2_1_10; -.
DR   OrthoDB; 9805316at2; -.
DR   Proteomes; UP000008674; Chromosome.
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:UP000008674};
KW   Transferase {ECO:0000256|RuleBase:RU004466}.
SQ   SEQUENCE   342 AA;  36978 MW;  6746E1D7346FDBE8 CRC64;
     MSPLADPNSP MASSTQSVSS DERVAALRAR IDEALPAVVD GRSPASLYDA VEHVLRAGGK
     RVRPVLLLLV AQSYGTSVDR ALPAALAVEV FHNFTLVHDD LMDEDDERRG GATVHAKWNP
     GTAILAGDLM MGLSYDLLGQ VEGTDAEALY AVYHPMVERL CAGQALDASF ETDDAVTVEA
     YLDMIDRKTG ALLSAAFELG SVIGGAPSPE RDRLGTAGRL VGRAFQIQDD LLDLTADDEA
     WGRGVGGDLV QGKKTFLTLR ALERAEGAEH DWFARLVTDG GLPRDDVPEA RERMADLGIF
     EEAREAVHTY TEKAHDHLHL LPETAAAETL HWLLDRLQAR GH
//
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