ID   IDSA_METTH              Reviewed;         325 AA.
AC   O26156;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Bifunctional short chain isoprenyl diphosphate synthase;
DE   Includes:
DE     RecName: Full=Farnesyl pyrophosphate synthetase;
DE              Short=FPP synthetase;
DE              EC=2.5.1.1;
DE     AltName: Full=Dimethylallyltranstransferase;
DE   Includes:
DE     RecName: Full=Geranyltranstransferase;
DE              EC=2.5.1.10;
GN   Name=idsA; OrderedLocusNames=MTH_50;
OS   Methanobacterium thermoautotrophicum.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Delta H;
RX   MEDLINE=98037514; PubMed=9371463;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K.,
RA   Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA   Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA   Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA   McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA   Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum
RT   deltaH: functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
CC       diphosphate = diphosphate + geranyl diphosphate.
CC   -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
CC       = diphosphate + trans,trans-farnesyl diphosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   EMBL; AE000666; AAB84557.1; -; Genomic_DNA.
DR   PIR; G69165; G69165.
DR   RefSeq; NP_275193.1; -.
DR   GeneID; 1470012; -.
DR   GenomeReviews; AE000666_GR; MTH_50.
DR   KEGG; mth:MTH50; -.
DR   NMPDR; fig|187420.1.peg.48; -.
DR   HOGENOM; O26156; -.
DR   OMA; O26156; SKACVEV.
DR   BioCyc; MTHE187420:MTH50-MON; -.
DR   BRENDA; 2.5.1.1; 270.
DR   BRENDA; 2.5.1.10; 270.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR017446; Polyprenyl_synth-rel.
DR   InterPro; IPR008949; Terpenoid_synth.
DR   Gene3D; G3DSA:1.10.600.10; Terpenoid_synth; 1.
DR   PANTHER; PTHR12001; Polyprenyl_synt; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHET_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHET_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Isoprene biosynthesis; Lipid synthesis;
KW   Magnesium; Multifunctional enzyme; Transferase.
FT   CHAIN         1    325       Bifunctional short chain isoprenyl
FT                                diphosphate synthase.
FT                                /FTId=PRO_0000123971.
SQ   SEQUENCE   325 AA;  35485 MW;  BCF3A285A207916E CRC64;
     MMEVMDILRK YSEMADERIR ESISDITPET LLRASEHLIT AGGKKIRPSL ALLSSEAVGG
     DPGDAAGVAA AIELIHTFSL IHDDIMDDDE IRRGEPAVHV LWGEPMAILA GDVLFSKAFE
     AVIRNGDSEM VKEALAVVVD SCVKICEGQA LDMGFEERLD VTEEEYMEMI YKKTAALIAA
     ATKAGAIMGG GSPQEIAALE DYGRCIGLAF QIHDDYLDVV SDEESLGKPV GSDIAEGKMT
     LMVVKALERA SEKDRERLIS ILGSGDEKLV AEAIEIFERY GATEYAHAVA LDHVRMAKER
     LEVLEESDAR EALAMIADFV LEREH
//