GGS1_PHOAM
ID GGS1_PHOAM Reviewed; 389 AA.
AC B2DBE8;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase A;
DE Short=GGPP synthase A;
DE Short=GGPPSase A;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase A;
DE AltName: Full=Farnesyl diphosphate synthase A;
DE AltName: Full=Farnesyltranstransferase A;
DE EC=2.5.1.29;
DE AltName: Full=Geranylgeranyl diphosphate synthase A;
DE AltName: Full=Geranyltranstransferase A;
DE EC=2.5.1.10;
GN Name=GGS-A;
OS Phomopsis amygdali (Fusicoccum amygdali).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214568;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=N2;
RX PubMed=18391465; DOI=10.1271/bbb.70790;
RA Toyomasu T., Niida R., Kenmoku H., Kanno Y., Miura S., Nakano C.,
RA Shiono Y., Mitsuhashi W., Toshima H., Oikawa H., Hoshino T., Dairi T.,
RA Kato N., Sassa T.;
RT "Identification of diterpene biosynthetic gene clusters and functional
RT analysis of labdane-related diterpene cyclases in Phomopsis amygdali.";
RL Biosci. Biotechnol. Biochem. 72:1038-1047(2008).
CC -!- FUNCTION: Catalyzes the trans-addition of the 2 molecules of
CC isopentenyl diphosphate (IPP) onto geranyl diphosphate (GDP) to form
CC geranylgeranyl pyrophosphate (GGDP). Does not catalyze the conversion
CC of dimethylallyl diphosphate (DMAPP). {ECO:0000269|PubMed:18391465}.
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 Evidence={ECO:0000269|PubMed:18391465};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000269|PubMed:18391465};
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; geranylgeranyl diphosphate
CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC isopentenyl diphosphate: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AB252830; BAG30959.1; -; mRNA.
DR AlphaFoldDB; B2DBE8; -.
DR SMR; B2DBE8; -.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isoprene biosynthesis; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..389
FT /note="Geranylgeranyl pyrophosphate synthase A"
FT /id="PRO_0000415668"
FT BINDING 99
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 102
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 131
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 147
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
SQ SEQUENCE 389 AA; 43082 MW; 7327E972AA35532E CRC64;
MTSGSKAHPV PATCTMESPP LHLDMGAARS SVCTELTIMP RPLAKSLQDS IDSNFPIDEG
FQSGGEDEDM RRLFCNILPE VSTAAVDAPF HYTSSLPSKG VRDKLIGGLN IWVGASPKAL
DSVTSVVVDV HNLSLMQDDV EDNSPLRRSR PSTHSIFGID QTVNSSTCGI VEVLRRSSEM
QNPAFLKIVI EELRSLLIGQ SLDLLWTHQI STPSVEEYLQ MVDGKTGGLF RMASKLMIAQ
SESSNMNPTD LDALMTLLGR YFQIRDDYMN LTSQEYTKSK GFCEDLDEGK YSLIMIHALE
NCDHKSRVLL DSMLLERRAT GAAGLGHKEL ILSMMQQTGS LQYAVEILSV LFNEIFELVE
LIDRRTGKVN KPIRDLLAAL EIKKDSPRK
