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FPPS1_PARAR
ID   FPPS1_PARAR             Reviewed;         342 AA.
AC   O24241;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Farnesyl pyrophosphate synthase 1;
DE            Short=FPP synthase 1;
DE            Short=FPS 1;
DE            EC=2.5.1.10;
DE   AltName: Full=(2E,6E)-farnesyl diphosphate synthase 1;
DE   AltName: Full=Dimethylallyltranstransferase 1;
DE            EC=2.5.1.1;
DE   AltName: Full=Farnesyl diphosphate synthase 1;
DE   AltName: Full=Geranyltranstransferase 1;
GN   Name=FPS1;
OS   Parthenium argentatum (Guayule rubber plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Parthenium.
OX   NCBI_TaxID=35935;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Line 11591; TISSUE=Stem bark;
RX   PubMed=8806726; DOI=10.1006/abbi.1996.0333;
RA   Pan Z., Herickhoff L.A., Backhaus R.A.;
RT   "Cloning, characterization, and heterologous expression of cDNAs for
RT   farnesyl diphosphate synthase from the guayule rubber plant reveals that
RT   this prenyltransferase occurs in rubber particles.";
RL   Arch. Biochem. Biophys. 332:196-204(1996).
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.
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   -!- 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
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   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Rubber particles.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; X82542; CAA57892.1; -; mRNA.
DR   PIR; S71398; S71398.
DR   AlphaFoldDB; O24241; -.
DR   SMR; O24241; -.
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:0006695; P:cholesterol 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   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   Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm;
KW   Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW   Metal-binding; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism; Transferase.
FT   CHAIN           1..342
FT                   /note="Farnesyl pyrophosphate synthase 1"
FT                   /id="PRO_0000123959"
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;  39367 MW;  D49AA182B74ED6EA CRC64;
     MSSDLKSRFL QVYDTLKSEL INDPAFEFDD DSRQWVEKML DYNVPGGKLN RGLSVIDSYQ
     LLKGGELTDN EIFLAAALGW CIEWLQAYFL VLDDIMDESH TRRGQPCWFR LPKVGMIAAN
     DGIILRNNVP RILKKHFRGK PYYVDLLDLF NEVEFQTASG QMIDLITTLV GEKDLSKYSL
     SIHRRIVQYK TAYYSFYLPV ACALLMFGED LEKHEEVKNV LVEMGTYFQV QDDYLDCFGA
     PEVIGKIGTD IEDFKCSWLV VKALELSNEE QKKILHENYG KKDPSSVAKV KELYHTLNLQ
     GVFEDYENTS YKKLITSIEG HPSKAVQAVL KSFLGKIYKR QK
 
 
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