CRTE_PSEVU
ID CRTE_PSEVU Reviewed; 307 AA.
AC P22873;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Geranylgeranyl diphosphate synthase;
DE Short=GGPP synthase;
DE EC=2.5.1.29;
DE AltName: Full=Farnesyltranstransferase;
GN Name=crtE;
OS Pseudescherichia vulneris (Escherichia vulneris).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pseudescherichia.
OX NCBI_TaxID=566;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 39368 / Eho10;
RX PubMed=2263648; DOI=10.1073/pnas.87.24.9975;
RA Armstrong G.A., Alberti M., Hearst J.E.;
RT "Conserved enzymes mediate the early reactions of carotenoid biosynthesis
RT in nonphotosynthetic and photosynthetic prokaryotes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9975-9979(1990).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1495965; DOI=10.1073/pnas.89.15.6761;
RA Math S.K., Hearst J.E., Poulter C.D.;
RT "The crtE gene in Erwinia herbicola encodes geranylgeranyl diphosphate
RT synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6761-6764(1992).
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:0000269|PubMed:1495965}.
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 Evidence={ECO:0000269|PubMed:1495965};
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; M38424; AAA24819.1; -; Genomic_DNA.
DR EMBL; M87280; AAA64977.1; -; Genomic_DNA.
DR PIR; C39273; C39273.
DR AlphaFoldDB; P22873; -.
DR SMR; P22873; -.
DR BioCyc; MetaCyc:MON-18246; -.
DR UniPathway; UPA00389; UER00564.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IDA: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 1: Evidence at protein level;
KW Carotenoid biosynthesis; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Transferase.
FT CHAIN 1..307
FT /note="Geranylgeranyl diphosphate synthase"
FT /id="PRO_0000123992"
FT BINDING 52
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 55
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:Q12051"
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 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 104
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 188
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250"
SQ SEQUENCE 307 AA; 33242 MW; 6A534C6194CE9F59 CRC64;
MVSGSKAGVS PHREIEVMRQ SIDDHLAGLL PETDSQDIVS LAMREGVMAP GKRIRPLLML
LAARDLRYQG SMPTLLDLAC AVELTHTASL MLDDMPCMDN AELRRGQPTT HKKFGESVAI
LASVGLLSKA FGLIAATGDL PGERRAQAVN ELSTAVGVQG LVLGQFRDLN DAALDRTPDA
ILSTNHLKTG ILFSAMLQIV AIASASSPST RETLHAFALD FGQAFQLLDD LRDDHPETGK
DRNKDAGKST LVNRLGADAA RQKLREHIDS ADKHLTFACP QGGAIRQFMH LWFGHHLADW
SPVMKIA
