ISPA_BRADU
ID ISPA_BRADU Reviewed; 332 AA.
AC Q45220;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable farnesyl diphosphate synthase;
DE Short=FPP synthase;
DE EC=2.5.1.10;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE AltName: Full=Geranyltranstransferase;
GN Name=fppS; OrderedLocusNames=blr2148;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=16349113; DOI=10.1128/aem.59.12.4136-4142.1993;
RA Tully R.E., Keister D.L.;
RT "Cloning and mutagenesis of a cytochrome P-450 locus from Bradyrhizobium
RT japonicum that is expressed anaerobically and symbiotically.";
RL Appl. Environ. Microbiol. 59:4136-4142(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=9655913; DOI=10.1016/s0167-4781(98)00069-4;
RA Tully R.E., van Berkum P., Lovins K.W., Keister D.L.;
RT "Identification and sequencing of a cytochrome P450 gene cluster from
RT Bradyrhizobium japonicum.";
RL Biochim. Biophys. Acta 1398:243-255(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC47413.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U12678; AAC28894.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC47413.1; ALT_INIT; Genomic_DNA.
DR PIR; I40213; I40213.
DR RefSeq; NP_768788.1; NC_004463.1.
DR RefSeq; WP_028144010.1; NZ_CP011360.1.
DR AlphaFoldDB; Q45220; -.
DR SMR; Q45220; -.
DR STRING; 224911.27350402; -.
DR EnsemblBacteria; BAC47413; BAC47413; BAC47413.
DR GeneID; 64021897; -.
DR KEGG; bja:blr2148; -.
DR PATRIC; fig|224911.44.peg.1664; -.
DR eggNOG; COG0142; Bacteria.
DR HOGENOM; CLU_014015_0_0_5; -.
DR InParanoid; Q45220; -.
DR OMA; CEGQALD; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; 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 Cytoplasm; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..332
FT /note="Probable farnesyl diphosphate synthase"
FT /id="PRO_0000123987"
FT BINDING 75
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 78
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 107
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 125
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 208
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 34639 MW; 47644FAF0220CE4C CRC64;
MQTGSTPHDD RAGVSANGIL GAQARGASGR LLPEIWMQDG AKRVEEALAR LLCAEDDGET
ELMAAMRYAT LHGGKRTRAL LCLAAGALAD TPAHMLDDVG AAIEMMHACT LVHDDLPAMD
DDVLRRGLPT VHVKFGEATA ILVGDALQAH AFLTLASLNA PGDSPIALVR ELAQAVSAEG
AAGGQAIDLS LVGKHVELDR IVAMHRMKSG ALVRASVRMG ALCAVGVNAA HAALYCALDH
YSACFGLALQ VIDDILDVTA DTAALGKTPG KDAAAQKPTC ASIMGLQEAR QFALDLLRDA
GEAIAPLGPR AERLAQLIQR ANAYLFKHAP RA
