ID   GPPS_IPSPI              Reviewed;         416 AA.
AC   Q58GE8;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Geranyl diphosphate synthase {ECO:0000303|PubMed:15983375};
DE            EC=2.5.1.1 {ECO:0000305|PubMed:15983375};
GN   Name=GPPS {ECO:0000303|PubMed:15983375};
OS   Ips pini (Pine engraver beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Ips.
OX   NCBI_TaxID=102803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=15983375; DOI=10.1073/pnas.0503277102;
RA   Gilg A.B., Bearfield J.C., Tittiger C., Welch W.H., Blomquist G.J.;
RT   "Isolation and functional expression of an animal geranyl diphosphate
RT   synthase and its role in bark beetle pheromone biosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:9760-9765(2005).
CC   -!- FUNCTION: Geranyl diphosphate synthase involved in pheromone
CC       biosynthesis. {ECO:0000269|PubMed:15983375}.
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:0000305|PubMed:15983375};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409;
CC         Evidence={ECO:0000305|PubMed:15983375};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P14324};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};
CC   -!- PATHWAY: Pheromone biosynthesis. {ECO:0000269|PubMed:15983375}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in the anterior midgut of
CC       male beetles, the site of aggregation pheromone biosynthesis.
CC       {ECO:0000269|PubMed:15983375}.
CC   -!- INDUCTION: Specifically induced in the anterior midgut of males
CC       (PubMed:15983375). Expression levels are regulated by juvenile hormone
CC       III (JH III) (PubMed:15983375). {ECO:0000269|PubMed:15983375}.
CC   -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC       the catalytic activity, presumably through binding to Mg(2+).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; AY953508; AAX55632.1; -; mRNA.
DR   SMR; Q58GE8; -.
DR   BioCyc; MetaCyc:MON-18357; -.
DR   BRENDA; 2.5.1.1; 7894.
DR   BRENDA; 4.2.3.15; 7894.
DR   GO; GO:0044687; F:geranylfarnesyl diphosphate synthase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0042811; P:pheromone biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR039702; FPS1-like.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   PANTHER; PTHR11525; PTHR11525; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..416
FT                   /note="Geranyl diphosphate synthase"
FT                   /id="PRO_0000455288"
FT   MOTIF           157..161
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
SQ   SEQUENCE   416 AA;  48324 MW;  BC91E673F88D664F CRC64;
     MFKLAQRLPK SVSSLGSQLS KNAPNQLAAA TTSQLINTPG IRHKSRSSAV PSSLSKSMYD
     HNEEMKAAMK YMDEIYPEVM GQIEKVPQYE EIKPILVRLR EAIDYTVPYG KRFKGVHIVS
     HFKLLADPKF ITPENVKLSG VLGWCAEIIQ AYFCMLDDIM DDSDTRRGKP TWYKLPGIGL
     NAVTDVCLME MFTFELLKRY FPKHPSYADI HEILRNLLFL THMGQGYDFT FIDPVTRKIN
     FNDFTEENYT KLCRYKIIFS TFHNTLELTS AMANVYDPKK IKQLDPVLMR IGMMHQSQND
     FKDLYRDQGE VLKQAEKSVL GTDIKTGQLT WFAQKALSIC NDRQRKIIMD NYGKEDNKNS
     EAVREVYEEL DLKGKFMEFE EESFEWLKKE IPKINNGIPH KVFQDYTYGV FKRRPE