ID   GGDPS_MELLP             Reviewed;         364 AA.
AC   A0A858E7G0; F4RDE7;
DT   14-DEC-2022, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   02-OCT-2024, entry version 11.
DE   RecName: Full=Geranylgeranyl pyrophosphate synthase {ECO:0000303|PubMed:32913319};
DE            Short=GGPP synthase {ECO:0000303|PubMed:32913319};
DE            Short=GGPPSase {ECO:0000303|PubMed:32913319};
DE            EC=2.5.1.- {ECO:0000269|PubMed:32913319};
DE   AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000303|PubMed:32913319};
DE   AltName: Full=Dimethylallyltranstransferase {ECO:0000303|PubMed:32913319};
DE            EC=2.5.1.1 {ECO:0000269|PubMed:32913319};
DE   AltName: Full=Farnesyl diphosphate synthase {ECO:0000303|PubMed:32913319};
DE   AltName: Full=Farnesyltranstransferase {ECO:0000303|PubMed:32913319};
DE            EC=2.5.1.29 {ECO:0000269|PubMed:32913319};
DE   AltName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:32913319};
DE   AltName: Full=Geranyltranstransferase {ECO:0000303|PubMed:32913319};
DE            EC=2.5.1.10 {ECO:0000269|PubMed:32913319};
GN   Name=GGDPS {ECO:0000303|PubMed:32913319}; ORFNames=MELLADRAFT_47465;
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=32913319; DOI=10.1038/s41598-020-71219-z;
RA   Wei G., Eberl F., Chen X., Zhang C., Unsicker S.B., Koellner T.G.,
RA   Gershenzon J., Chen F.;
RT   "Evolution of isoprenyl diphosphate synthase-like terpene synthases in
RT   fungi.";
RL   Sci. Rep. 10:14944-14944(2020).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7;
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC   -!- FUNCTION: Geranylgeranyl pyrophosphate synthase that catalyzes the
CC       trans-addition of the three molecules of IPP onto DMAPP to form
CC       geranylgeranyl pyrophosphate (PubMed:32913319). Does not show any
CC       monoterpene nor sesquiterpene synthase activity (PubMed:32913319).
CC       {ECO:0000269|PubMed:32913319}.
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         Evidence={ECO:0000269|PubMed:32913319};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409;
CC         Evidence={ECO:0000269|PubMed:32913319};
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:32913319};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362;
CC         Evidence={ECO:0000269|PubMed:32913319};
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:32913319};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC         Evidence={ECO:0000269|PubMed:32913319};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q12051};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EGG09623.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; GL883097; EGG09623.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; MK946437; QIG55789.1; -; mRNA.
DR   RefSeq; XP_007407350.1; XM_007407288.1.
DR   AlphaFoldDB; A0A858E7G0; -.
DR   SMR; A0A858E7G0; -.
DR   STRING; 747676.F4RDE7; -.
DR   EnsemblFungi; EGG09623; EGG09623; MELLADRAFT_47465.
DR   GeneID; 18928434; -.
DR   KEGG; mlr:MELLADRAFT_47465; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_47465; -.
DR   eggNOG; KOG0777; Eukaryota.
DR   HOGENOM; CLU_014015_6_0_1; -.
DR   OrthoDB; 5770at2759; -.
DR   Proteomes; UP000001072; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:InterPro.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
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; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR12001:SF69; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   1: Evidence at protein level;
KW   Isoprene biosynthesis; Lyase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Reference proteome; Transferase.
FT   CHAIN           1..364
FT                   /note="Geranylgeranyl pyrophosphate synthase"
FT                   /id="PRO_0000457150"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           116..120
FT                   /note="DDXXD 2"
FT                   /evidence="ECO:0000250|UniProtKB:A1C8C3"
FT   COMPBIAS        20..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         77
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         80
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         109
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         125
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         126
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         210
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         211
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         246
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         249
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         253
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         262
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         272
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   SITE            148
FT                   /note="Important for determining product chain length"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
SQ   SEQUENCE   364 AA;  41198 MW;  172BE22D341F3076 CRC64;
     MKPVPSTNGK VDDKVEHHNL SSSSSSSSSS SSSDTKFNIS NRYGNFLQRL EALDIWPESN
     EQILLEPYTY LTNIPGKEIR SMMIDAFNHW LQVPRPALEI IKKIVGQLHT ASLLMDDVED
     DSDLRRGVPV THKIYGIPQT INTANYVYFL AYQELTKLKP CLRSDATTDL WSLVNDELLQ
     LHRGQGMDLY WRDSLTCPTE EEYLQMVNNK TGGLFRIAIK LMIALSPIPE TPDYLPLVNL
     VGIIFQIRDD LLNLSSVYTK NKGFCEDLTE GKFSFPIVHS IRSDSTNHQL MNILRQKPTD
     IGTKAFAVSY MKDRTKSLEY TRGVLICLEE QAIEEVTRLG GNPALESIFE LMHVLPSPPA
     TDQN
//