(data stored in ACNUC7421 zone)

SWISSPROT: GGPPS_ASHGO

ID   GGPPS_ASHGO             Reviewed;         320 AA.
AC   Q758K0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 98.
DE   RecName: Full=Geranylgeranyl pyrophosphate synthase;
DE            Short=GGPP synthase;
DE            Short=GGPPSase;
DE            EC=2.5.1.-;
DE   AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE   AltName: Full=Dimethylallyltranstransferase;
DE            EC=2.5.1.1;
DE   AltName: Full=Farnesyl diphosphate synthase;
DE   AltName: Full=Farnesyltranstransferase;
DE            EC=2.5.1.29;
DE   AltName: Full=Geranylgeranyl diphosphate synthase;
DE   AltName: Full=Geranyltranstransferase;
DE            EC=2.5.1.10;
GN   Name=BTS1; OrderedLocusNames=AEL238C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Catalyzes the trans-addition of the 3 molecules of IPP onto
CC       DMAPP to form geranylgeranyl pyrophosphate. May be involved in vesicle
CC       trafficking and protein sorting (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-
CC         geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC         ChEBI:CHEBI:128769; EC=2.5.1.1;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = all-
CC         trans-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769,
CC         ChEBI:CHEBI:175763; EC=2.5.1.29;
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   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC       farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC       diphosphate: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC       geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC       diphosphate: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC       biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC       isopentenyl diphosphate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
DR   EMBL; AE016818; AAS52447.1; -; Genomic_DNA.
DR   RefSeq; NP_984623.1; NM_209976.1.
DR   SMR; Q758K0; -.
DR   STRING; 33169.AAS52447; -.
DR   EnsemblFungi; AAS52447; AAS52447; AGOS_AEL238C.
DR   GeneID; 4620805; -.
DR   KEGG; ago:AGOS_AEL238C; -.
DR   HOGENOM; HOG000169461; -.
DR   InParanoid; Q758K0; -.
DR   KO; K00804; -.
DR   OMA; TRANDVF; -.
DR   UniPathway; UPA00259; UER00368.
DR   UniPathway; UPA00260; UER00369.
DR   UniPathway; UPA00389; UER00564.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015031; P:protein transport; 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; Q758K0.
DR   SWISS-2DPAGE; Q758K0.
KW   Carotenoid biosynthesis; Cytoplasm; Isoprene biosynthesis; Magnesium;
KW   Metal-binding; Protein transport; Reference proteome; Transferase;
KW   Transport.
FT   CHAIN           1..320
FT                   /note="Geranylgeranyl pyrophosphate synthase"
FT                   /id="PRO_0000228138"
FT   METAL           74
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   METAL           74
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   METAL           78
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   METAL           78
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         35
FT                   /note="Isopentenyl diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         38
FT                   /note="Isopentenyl diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         67
FT                   /note="Isopentenyl diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         83
FT                   /note="Dimethylallyl diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /note="Isopentenyl diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         168
FT                   /note="Dimethylallyl diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /note="Dimethylallyl diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /note="Dimethylallyl diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /note="Dimethylallyl diphosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /note="Dimethylallyl diphosphate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  35984 MW;  EFA9BE35C2F831BF CRC64;
     MDSVEGLALG PVIWTASQEE LLRQPYNHLV TQPGKNFRNT LIRVFNGFYG LSERQVAAVT
     ELVEMLHVAS LLIDDIEDNS AWRRGVAAAH VVYGSPMTIN TANYMYFVSM SLLGQLAAQR
     PAGPLQDLLK VFNEEMMNLH RGQGLDIYWR DTFTVPSEHD YLRMVMHKTG GLFRLTVRIM
     EALREGPDGP GSTLVPLSNL LGVLYQVRDD YLNLTDSRMS ENKGFADDIT EGKFSYPIIH
     GLQYARVHDP AGYDFLVSVL RQRTTDITTK RRVVRYLADV SGSLAYTKQR IIELATLIKT
     KYIPASGTEL CNVIDSLTSF
//

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