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FPS_PANGI
ID   FPS_PANGI               Reviewed;         342 AA.
AC   Q4JHN6;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Farnesyl pyrophosphate synthase {ECO:0000303|PubMed:29509695, ECO:0000303|Ref.1};
DE            Short=FPP synthase {ECO:0000303|Ref.1};
DE            Short=PgFPS {ECO:0000303|PubMed:29509695, ECO:0000303|Ref.1};
DE            EC=2.5.1.10 {ECO:0000250|UniProtKB:P14324};
DE   AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000305};
DE   AltName: Full=Dimethylallyltranstransferase {ECO:0000305};
DE            EC=2.5.1.1 {ECO:0000250|UniProtKB:P14324};
DE   AltName: Full=Farnesyl diphosphate synthase {ECO:0000303|Ref.1};
DE   AltName: Full=Geranyltranstransferase {ECO:0000305};
GN   Name=FPS {ECO:0000303|PubMed:29509695, ECO:0000303|PubMed:30577538,
GN   ECO:0000303|Ref.1};
OS   Panax ginseng (Korean ginseng).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Araliaceae; Panax.
OX   NCBI_TaxID=4054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY METHYL JASMONATE, TISSUE
RP   SPECIFICITY, AND ACTIVITY REGULATION.
RX   DOI=10.1007/s10535-010-0007-1;
RA   Kim O.T., Bang K.H., Jung S.J., Kim Y.C., Hyun D.Y., Kim S.H., Cha S.W.;
RT   "Molecular characterization of ginseng farnesyl diphosphate synthase gene
RT   and its up-regulation by methyl jasmonate.";
RL   Biol. Plant. 54:47-53(2010).
RN   [2]
RP   INDUCTION BY METHYL JASMONATE.
RX   DOI=10.1007/s11240-009-9535-9;
RA   Kim O.T., Bang K.H., Kim Y.C., Hyun D.Y., Kim M.Y., Cha S.W.;
RT   "Upregulation of ginsenoside and gene expression related to triterpene
RT   biosynthesis in ginseng hairy root cultures elicited by methyl jasmonate.";
RL   Plant Cell Tissue Organ Cult. 98:25-33(2009).
RN   [3]
RP   FUNCTION.
RX   PubMed=24933610; DOI=10.1021/sb400194g;
RA   Kim Y.-K., Kim Y.B., Uddin M.R., Lee S., Kim S.-U., Park S.U.;
RT   "Enhanced triterpene accumulation in Panax ginseng hairy roots
RT   overexpressing mevalonate-5-pyrophosphate decarboxylase and farnesyl
RT   pyrophosphate synthase.";
RL   ACS Synth. Biol. 3:773-779(2014).
RN   [4]
RP   INDUCTION BY SALICYLIC ACID AND YEAST EXTRACT.
RX   DOI=10.1134/S1021443714060156;
RA   Rahimi S., Devi B.S.R., Khorolragchaa A., Kim Y.J., Kim J.H., Jung S.K.,
RA   Yang D.C.;
RT   "Effect of salicylic acid and yeast extract on the accumulation of jasmonic
RT   acid and sesquiterpenoids in Panax ginseng adventitious roots.";
RL   Russ. J. Plant Physiol. 61:811-817(2014).
RN   [5]
RP   FUNCTION, AND INDUCTION BY ASPERGILLUS NIGER.
RX   PubMed=27746309; DOI=10.1016/j.jbiotec.2016.10.011;
RA   Li J., Liu S., Wang J., Li J., Liu D., Li J., Gao W.;
RT   "Fungal elicitors enhance ginsenosides biosynthesis, expression of
RT   functional genes as well as signal molecules accumulation in adventitious
RT   roots of Panax ginseng C. A. Mey.";
RL   J. Biotechnol. 239:106-114(2016).
RN   [6]
RP   REVIEW.
RX   PubMed=29378087; DOI=10.1002/bab.1649;
RA   Lu J., Li J., Wang S., Yao L., Liang W., Wang J., Gao W.;
RT   "Advances in ginsenoside biosynthesis and metabolic regulation.";
RL   Biotechnol. Appl. Biochem. 65:514-522(2018).
RN   [7]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=29509695; DOI=10.3390/molecules23030589;
RA   Yang J.-L., Hu Z.-F., Zhang T.-T., Gu A.-D., Gong T., Zhu P.;
RT   "Progress on the studies of the key enzymes of ginsenoside biosynthesis.";
RL   Molecules 23:0-0(2018).
RN   [8]
RP   DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND INDUCTION BY ABIOTIC FACTORS.
RX   PubMed=30577538; DOI=10.3390/molecules24010014;
RA   Zhang T., Han M., Yang L., Han Z., Cheng L., Sun Z., Yang L.;
RT   "The effects of environmental factors on ginsenoside biosynthetic enzyme
RT   gene expression and saponin abundance.";
RL   Molecules 24:0-0(2018).
CC   -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
CC       pyrophosphate with the allylic pyrophosphates, dimethylallyl
CC       pyrophosphate, and then with the resultant geranylpyrophosphate to the
CC       ultimate product farnesyl pyrophosphate (By similarity). Component of
CC       the triterpene saponins (e.g. ginsenosides or panaxosides) and
CC       phytosterols biosynthetic pathways (PubMed:24933610, PubMed:27746309,
CC       PubMed:29378087). Promotes the accumulation of ginsenosides
CC       (PubMed:24933610). {ECO:0000250|UniProtKB:O14230,
CC       ECO:0000269|PubMed:24933610, ECO:0000269|PubMed:27746309,
CC       ECO:0000303|PubMed:29378087}.
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:0000250|UniProtKB:P14324};
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:0000250|UniProtKB:P14324};
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   -!- ACTIVITY REGULATION: Stimulated by methyl jasmonate (MeJA).
CC       {ECO:0000269|Ref.1}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC       farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC       diphosphate: step 1/1. {ECO:0000250|UniProtKB:Q12051}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC       geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC       diphosphate: step 1/1. {ECO:0000250|UniProtKB:Q12051}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14324}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14324}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in roots and seeds, and to a lower
CC       extent, in leaves and stems. {ECO:0000269|PubMed:30577538,
CC       ECO:0000269|Ref.1}.
CC   -!- DEVELOPMENTAL STAGE: Rapid decrease in roots and leaves from the leaf
CC       opened to the green fruit stage. {ECO:0000269|PubMed:30577538}.
CC   -!- INDUCTION: Induced by methyl jasmonate (MeJA) in hairy roots (Ref.1,
CC       Ref.2). Induced by A.niger mycelium-derived elicitor, thus improving
CC       ginsenosides production in adventitious roots culture
CC       (PubMed:27746309). Triggered by salicylic acid and yeast extract
CC       (Ref.4). Influenced in roots by relative humidity and rain, and in
CC       leaves by rain (PubMed:30577538). {ECO:0000269|PubMed:27746309,
CC       ECO:0000269|PubMed:30577538, ECO:0000269|Ref.1, ECO:0000269|Ref.2,
CC       ECO:0000269|Ref.4}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; DQ087959; AAY87903.1; -; mRNA.
DR   AlphaFoldDB; Q4JHN6; -.
DR   SMR; Q4JHN6; -.
DR   BRENDA; 2.5.1.10; 7895.
DR   UniPathway; UPA00259; UER00368.
DR   UniPathway; UPA00260; UER00369.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016117; P:carotenoid biosynthetic process; 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   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR   GO; GO:0001878; P:response to yeast; IEP:UniProtKB.
DR   GO; GO:0016135; P:saponin biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016104; P:triterpenoid 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   2: Evidence at transcript level;
KW   Carotenoid biosynthesis; Cytoplasm; Isoprene biosynthesis; Magnesium;
KW   Metal-binding; Protein transport; Transferase; Transport.
FT   CHAIN           1..342
FT                   /note="Farnesyl pyrophosphate synthase"
FT                   /id="PRO_0000446951"
FT   BINDING         47
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         50
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         86
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         93
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         93
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         102
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         103
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         190
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         191
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         229
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         255
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
SQ   SEQUENCE   342 AA;  39627 MW;  E29F20D2344E848C CRC64;
     MSDLKTRFLE VYSVLKSELL NDPAFEFTDD SRQWVERMLD YNVPGGKLNR GLSVIDSYKL
     LKEGKELSDD EIFLSSALGW CIEWLQAYFL VLDDIMDSSH TRRGQPCWFR LPKVGMIAVN
     DGILLRNHIP RILKKHFRQK PYYVDLLDLF NEVEFQTASG QMIDLITTLV GEKDLSKYSL
     PIHRRIVQYK TAYYSFYLPV ACALLMSGED LEKHTNVKDI LIEMGTYFQV QDDYLDCFGA
     PEVIGKIGTD IEDFKCSWLV VKALELSNEE QKKFLHENYG KDDPASVAKV KELYNTLKLQ
     DVFAEYESKS YDKLIKFIEA HPSQAVQAVL KSFLGKIYKR QK
 
 
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