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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //