ID FPPS2_ARTSI Reviewed; 342 AA.
AC Q7XYT0;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 22-FEB-2023, entry version 60.
DE RecName: Full=Farnesyl diphosphate synthase 2;
DE Includes:
DE RecName: Full=Dimethylallyltranstransferase;
DE EC=2.5.1.1;
DE Includes:
DE RecName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE EC=2.5.1.10;
GN Name=FDS-2;
OS Artemisia spiciformis (Spiked big sagebrush) (Artemisia tridentata
OS spiciformis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=235357;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=12782626; DOI=10.1074/jbc.m213045200;
RA Hemmerlin A., Rivera S.B., Erickson H.K., Poulter C.D.;
RT "Enzymes encoded by the farnesyl diphosphate synthase gene family in the
RT Big Sagebrush Artemisia tridentata ssp. spiciformis.";
RL J. Biol. Chem. 278:32132-32140(2003).
RN [2]
RP CATALYTIC ACTIVITY.
RX PubMed=12783539; DOI=10.1021/ja034520g;
RA Erickson H.K., Poulter C.D.;
RT "Chrysanthemyl diphosphate synthase. The relationship among chain
RT elongation, branching, and cyclopropanation reactions in the isoprenoid
RT biosynthetic pathway.";
RL J. Am. Chem. Soc. 125:6886-6888(2003).
CC -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
CC pyrophosphate (IPP) with the allylic pyrophosphates, dimethylallyl
CC pyrophosphate (DMAPP), and then with the resultant geranylpyrophosphate
CC (GPP) to the ultimate product farnesyl pyrophosphate (FPP). Has a
CC greater affinity for DMAPP versus GPP. {ECO:0000269|PubMed:12782626}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12782626};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12782626};
CC Note=Binds Mg(2+) or Mn(2+). {ECO:0000269|PubMed:12782626};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.0 uM for dimethylallyl diphosphate
CC {ECO:0000269|PubMed:12782626};
CC KM=13.1 uM for geranyl diphosphate {ECO:0000269|PubMed:12782626};
CC KM=5.8 uM for isopentenyl pyrophosphate
CC {ECO:0000269|PubMed:12782626};
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:12782626};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:12782626};
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- TISSUE SPECIFICITY: Expressed in shoots. {ECO:0000269|PubMed:12782626}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AY308476; AAP74719.1; -; mRNA.
DR AlphaFoldDB; Q7XYT0; -.
DR SMR; Q7XYT0; -.
DR SABIO-RK; Q7XYT0; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR GO; GO:0004161; F:dimethylallyltranstransferase 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:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 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:SF0; FARNESYL PYROPHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR11525; FARNESYL-PYROPHOSPHATE SYNTHETASE; 1.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR SFLD; SFLDG01017; Polyprenyl_Transferase_Like; 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; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..342
FT /note="Farnesyl diphosphate synthase 2"
FT /id="PRO_0000405124"
FT MOTIF 93..97
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT MOTIF 232..236
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 48
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 51
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 86
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 102
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 190
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 39598 MW; F6B251CA7CB3699F CRC64;
MSIDLKSRFL QVYDSLKSDL IHDPAFEFDD DSRNWVERML DYNVPGGKLN RGLSVVDSYK
LLKQEELTED EVFLACALGW CIEWLQAYFL VLDDIMDESH TRRGQPCWFR LPKVGMIAVN
DGVVLRNHIP RILKKHFRGK AYYADLLDLF NEVEFQTASG QMIDLITTLF GQKELSKYSL
STHQRIVKFK TAYYSFYLPV ACALLMFGEN LDDHVQVKDV LVEMGTYFQV QDDYLDCFGS
PEVIGKIGTD IEDFKCSWLV VKALELADEQ QKKLLNENYG RKDPASVAKV KELYHTLNLQ
GVFEDYENKS HEKIIKSIET HPSKAVQEVL KSFLGKIFKR QK
//
