(data stored in SCRATCH zone)

SWISSPROT: ISPA_BACSU

ID   ISPA_BACSU              Reviewed;         296 AA.
AC   P54383;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   11-DEC-2019, entry version 120.
DE   RecName: Full=Farnesyl diphosphate synthase;
DE            Short=FPP synthase;
DE            EC=2.5.1.10;
DE   AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE   AltName: Full=Geranyltranstransferase;
GN   Name=ispA; Synonyms=yqiD; OrderedLocusNames=BSU24280;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 166; 184 AND C-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC         farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC         ChEBI:CHEBI:175763; EC=2.5.1.10;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
DR   EMBL; D84432; BAA12575.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14359.2; -; Genomic_DNA.
DR   PIR; A69961; A69961.
DR   RefSeq; NP_390308.2; NC_000964.3.
DR   RefSeq; WP_003230262.1; NZ_JNCM01000036.1.
DR   SMR; P54383; -.
DR   STRING; 224308.BSU24280; -.
DR   PaxDb; P54383; -.
DR   PRIDE; P54383; -.
DR   EnsemblBacteria; CAB14359; CAB14359; BSU24280.
DR   GeneID; 938652; -.
DR   KEGG; bsu:BSU24280; -.
DR   PATRIC; fig|224308.179.peg.2646; -.
DR   eggNOG; ENOG4105CTB; Bacteria.
DR   eggNOG; COG0142; LUCA.
DR   HOGENOM; HOG000009101; -.
DR   InParanoid; P54383; -.
DR   KO; K13789; -.
DR   OMA; CEGQALD; -.
DR   PhylomeDB; P54383; -.
DR   BioCyc; BSUB:BSU24280-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; P54383.
DR   SWISS-2DPAGE; P54383.
KW   Cytoplasm; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..296
FT                   /note="Farnesyl diphosphate synthase"
FT                   /id="PRO_0000123986"
FT   METAL           85
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   METAL           85
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   METAL           91
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   METAL           91
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         46
FT                   /note="Isopentenyl diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         49
FT                   /note="Isopentenyl diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         78
FT                   /note="Isopentenyl diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         96
FT                   /note="Geranyl diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /note="Isopentenyl diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         182
FT                   /note="Geranyl diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /note="Geranyl diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /note="Geranyl diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /note="Geranyl diphosphate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        166
FT                   /note="E -> G (in Ref. 1; BAA12575)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="A -> S (in Ref. 1; BAA12575)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271..296
FT                   /note="KRLIGGLSLQKDLLYELCDLIAARDH -> ND (in Ref. 1;
FT                   BAA12575)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  32503 MW;  EECDBE7B483F2ECB CRC64;
     MTNKLTSFLA DRKKTIENQL SVYTEKLDMP DSLKKSMLYS LQAGGKRLRP LIVLAVLNAY
     GKSEKDGIPV GCAVEMIHTY SLIHDDLPCM DDDDLRRGKP TNHKVFGEAT AVLAGDGLLT
     ESFKLITSHV SDEVSAEKRL RLVNELISAA GTEGMVGGQV ADMEAENRQV TLEELESIHE
     RKTAKLLGFC VIAGAILADA PEEDIETLRT FSSHIGIGFQ IRDDILDLEG SEEKIGKRVG
     SDTTNDKSTY PSLLSLEGAK HKLDVHIKEA KRLIGGLSLQ KDLLYELCDL IAARDH
//

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