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CRTE_PANAN
ID   CRTE_PANAN              Reviewed;         302 AA.
AC   P21684;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Geranylgeranyl diphosphate synthase;
DE            Short=GGPP synthase;
DE            EC=2.5.1.29;
DE   AltName: Full=Farnesyltranstransferase;
GN   Name=crtE;
OS   Pantoea ananas (Erwinia uredovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=553;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 19321 / DSM 30080 / NCPPB 800 / NRRL B-14773 / 20D3;
RX   PubMed=2254247; DOI=10.1128/jb.172.12.6704-6712.1990;
RA   Misawa N., Nakagawa M., Kobayashi K., Yamano S., Izawa Y., Nakamura K.,
RA   Harashima K.;
RT   "Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by
RT   functional analysis of gene products expressed in Escherichia coli.";
RL   J. Bacteriol. 172:6704-6712(1990).
CC   -!- FUNCTION: Catalyzes the condensation of farnesyl diphosphate (FPP) and
CC       isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate
CC       (GGPP) needed for biosynthesis of carotenoids and diterpenes.
CC       {ECO:0000305|PubMed:2254247}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC         (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC         Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
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; geranylgeranyl diphosphate
CC       biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC       isopentenyl diphosphate: step 1/1.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; D90087; BAA14124.1; -; Genomic_DNA.
DR   PIR; A37802; A37802.
DR   AlphaFoldDB; P21684; -.
DR   SMR; P21684; -.
DR   UniPathway; UPA00389; UER00564.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; ISS:UniProtKB.
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:0033386; P:geranylgeranyl diphosphate biosynthetic process; IDA:UniProtKB.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
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   3: Inferred from homology;
KW   Carotenoid biosynthesis; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Transferase.
FT   CHAIN           1..302
FT                   /note="Geranylgeranyl diphosphate synthase"
FT                   /id="PRO_0000123993"
FT   BINDING         53
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         56
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         87
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         94
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         94
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         100
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         100
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         105
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         189
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  32583 MW;  CADB04699D2EBA4A CRC64;
     MTVCAKKHVH LTRDAAEQLL ADIDRRLDQL LPVEGERDVV GAAMREGALA PGKRIRPMLL
     LLTARDLGCA VSHDGLLDLA CAVEMVHAAS LILDDMPCMD DAKLRRGRPT IHSHYGEHVA
     ILAAVALLSK AFGVIADADG LTPLAKNRAV SELSNAIGMQ GLVQGQFKDL SEGDKPRSAE
     AILMTNHFKT STLFCASMQM ASIVANASSE ARDCLHRFSL DLGQAFQLLD DLTDGMTDTG
     KDSNQDAGKS TLVNLLGPRA VEERLRQHLQ LASEHLSAAC QHGHATQHFI QAWFDKKLAA
     VS
 
 
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