FPPS_MURHI
ID FPPS_MURHI Reviewed; 405 AA.
AC A0A343W970;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Farnesyl pyrophosphate synthase {ECO:0000303|PubMed:30139915};
DE Short=MhFPPS {ECO:0000303|PubMed:30139915};
DE Short=MhIDS-2 {ECO:0000303|PubMed:30139915};
DE EC=2.5.1.10 {ECO:0000269|PubMed:30139915};
GN Name=FPPS {ECO:0000303|PubMed:30139915};
OS Murgantia histrionica (Harlequin bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Pentatomomorpha; Pentatomoidea; Pentatomidae; Pentatominae; Murgantia.
OX NCBI_TaxID=460024;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP MUTAGENESIS OF 112-LYS--ARG-115 AND 153-PHE-PHE-154.
RX PubMed=30139915; DOI=10.1073/pnas.1800008115;
RA Lancaster J., Khrimian A., Young S., Lehner B., Luck K., Wallingford A.,
RA Ghosh S.K.B., Zerbe P., Muchlinski A., Marek P.E., Sparks M.E.,
RA Tokuhisa J.G., Tittiger C., Koellner T.G., Weber D.C.,
RA Gundersen-Rindal D.E., Kuhar T.P., Tholl D.;
RT "De novo formation of an aggregation pheromone precursor by an isoprenyl
RT diphosphate synthase-related terpene synthase in the harlequin bug.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E8634-E8641(2018).
CC -!- FUNCTION: Farnesyl pyrophosphate synthase involved in murgantiol
CC biosynthesis, a male-released aggregation pheromone, by catalyzing the
CC formation of (2E,6E)-farnesyl diphosphate.
CC {ECO:0000269|PubMed:30139915}.
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:30139915};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362;
CC Evidence={ECO:0000269|PubMed:30139915};
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:30139915}.
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; MG662379; AVZ23978.1; -; mRNA.
DR SMR; A0A343W970; -.
DR GO; GO:0004337; F:geranyltranstransferase 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 CDD; cd00685; Trans_IPPS_HT; 1.
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 InterPro; IPR033749; Polyprenyl_synt_CS.
DR PANTHER; PTHR11525; PTHR11525; 1.
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 1: Evidence at protein level;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..405
FT /note="Farnesyl pyrophosphate synthase"
FT /id="PRO_0000455289"
FT MOTIF 158..162
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT MUTAGEN 112..115
FT /note="KKVR->SDAW: Abolished farnesyl pyrophosphate
FT synthase activity."
FT /evidence="ECO:0000269|PubMed:30139915"
FT MUTAGEN 153..154
FT /note="FF->MS: Converts the enzyme into a 20-carbon
FT geranylgeranyl diphosphate synthase."
FT /evidence="ECO:0000269|PubMed:30139915"
SQ SEQUENCE 405 AA; 46364 MW; 8916467435B9FFFB CRC64;
MPFTKMCTSK LANPLMKYYL NLNGKSPLSK LSNSLNSSSF KFISCSPHIV CRELNTVSGV
AIRPQTITKD DKRDFMAVFP DIVRDLTQLN PGISDLSTLI SKLMQYNVSG GKKVRGLTVV
YSYRMLAPDH ALTPENIRLA QILGWCVEML QGFFVVIDDL ADQSVTRRGR PCWYRLPGVG
LRASSDALLI QSGCFQLLQQ HCKDKEFYVD LVELFLDALR RTTYGQTLDY VSSFPNINHL
TMDRYNFITK YKTAYYTYHL PVATAMYMAG IYNAELHRQA KSVLLEMGHY FQVQDDYLDV
FGDEEMIGKK GTDIQEGKCT WLAIIAFQRA SPPQREVLES CYGTKEPEKI KKVKDIFIEL
SLPAVYHAYE EETYNLITRQ IQQLSQGLPH ELFLTLLHKL YGRKQ
