CRTE_RHOCB
ID CRTE_RHOCB Reviewed; 289 AA.
AC P17060; D5AP77;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Geranylgeranyl diphosphate synthase;
DE Short=GGPP synthase;
DE EC=2.5.1.29;
DE AltName: Full=Farnesyltranstransferase;
GN Name=crtE; OrderedLocusNames=RCAP_rcc00684;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2747617; DOI=10.1007/bf00334364;
RA Armstrong G.A., Alberti M., Leach F., Hearst J.E.;
RT "Nucleotide sequence, organization, and nature of the protein products of
RT the carotenoid biosynthesis gene cluster of Rhodobacter capsulatus.";
RL Mol. Gen. Genet. 216:254-268(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
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:0000250}.
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; X52291; CAA36538.1; -; Genomic_DNA.
DR EMBL; Z11165; CAA77545.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84449.1; -; Genomic_DNA.
DR PIR; S04407; S04407.
DR RefSeq; WP_013066428.1; NC_014034.1.
DR AlphaFoldDB; P17060; -.
DR SMR; P17060; -.
DR STRING; 272942.RCAP_rcc00684; -.
DR EnsemblBacteria; ADE84449; ADE84449; RCAP_rcc00684.
DR GeneID; 31489630; -.
DR KEGG; rcp:RCAP_rcc00684; -.
DR eggNOG; COG0142; Bacteria.
DR HOGENOM; CLU_014015_0_1_5; -.
DR OMA; HCASLVH; -.
DR OrthoDB; 1861068at2; -.
DR BioCyc; MetaCyc:MON-14935; -.
DR UniPathway; UPA00389; UER00564.
DR Proteomes; UP000002361; Chromosome.
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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
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; Chlorophyll biosynthesis; Isoprene biosynthesis;
KW Magnesium; Metal-binding; Photosynthesis; Reference proteome; Transferase.
FT CHAIN 1..289
FT /note="Geranylgeranyl diphosphate synthase"
FT /id="PRO_0000123994"
FT BINDING 43
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 73
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 91
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 170
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250"
SQ SEQUENCE 289 AA; 30044 MW; CF483A26ECA9C859 CRC64;
MSLDKRIESA LVKALSPEAL GESPPLLAAA LPYGVFPGGA RIRPTILVSV ALACGDDCPA
VTDAAAVALE LMHCASLVHD DLPAFDNADI RRGKPSLHKA YNEPLAVLAG DSLLIRGFEV
LADVGAVNPD RALKLISKLG QLSGARGGIC AGQAWESESK VDLAAYHQAK TGALFIAATQ
MGAIAAGYEA EPWFDLGMRI GSAFQIADDL KDALMSAEAM GKPAGQDIAN ERPNAVKTMG
IEGARKHLQD VLAGAIASIP SCPGEAKLAQ MVQLYAHKIM DIPASAERG
