FPPS_MYCBO
ID FPPS_MYCBO Reviewed; 359 AA.
AC P0A5H9; A0A1R3Y438; Q50727; X2BNK9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000250|UniProtKB:P9WKH1};
DE Short=E,E-FPP synthase {ECO:0000250|UniProtKB:P9WKH1};
DE Short=FPP synthase {ECO:0000250|UniProtKB:P9WKH1};
DE EC=2.5.1.10 {ECO:0000250|UniProtKB:P9WKH1};
GN OrderedLocusNames=BQ2027_MB3431C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Catalyzes the condensation of isopentenyl pyrophosphate (IPP)
CC with geranyl diphosphate (GPP) to yield (2E,6E)-farnesyl diphosphate
CC (E,E-FPP). May be used for squalene and possibly sterol biosynthesis.
CC {ECO:0000250|UniProtKB:P9WKH1}.
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 Evidence={ECO:0000250|UniProtKB:P9WKH1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WKH1};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P9WKH1};
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate. {ECO:0000250|UniProtKB:P9WKH1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WKH1}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; LT708304; SIU02060.1; -; Genomic_DNA.
DR RefSeq; NP_857072.1; NC_002945.3.
DR RefSeq; WP_003417957.1; NC_002945.4.
DR AlphaFoldDB; P0A5H9; -.
DR SMR; P0A5H9; -.
DR EnsemblBacteria; SIU02060; SIU02060; BQ2027_MB3431C.
DR PATRIC; fig|233413.5.peg.3766; -.
DR OMA; ISYEHRD; -.
DR Proteomes; UP000001419; 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:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
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; Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Transferase.
FT CHAIN 1..359
FT /note="(2E,6E)-farnesyl diphosphate synthase"
FT /id="PRO_0000123969"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 112..116
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:P9WKH1"
FT MOTIF 242..246
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:P9WKH1"
FT BINDING 73
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 76
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 105
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 121
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 201
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
SQ SEQUENCE 359 AA; 38852 MW; F59F229B19432E6E CRC64;
MRGTDEKYGL PPQPDSDRMT RRTLPVLGLA HELITPTLRQ MADRLDPHMR PVVSYHLGWS
DERGRPVNNN CGKAIRPALV FVAAEAAGAD PHSAIPGAVS VELVHNFSLV HDDLMDRDEH
RRHRPTVWAL WGDAMALLAG DAMLSLAHEV LLDCDSPHVG AALRAISEAT RELIRGQAAD
TAFESRTDVA LDECLKMAEG KTAALMAASA EVGALLAGAP RSVREALVAY GRHIGLAFQL
VDDLLGIWGR PEITGKPVYS DLRSRKKTLP VTWTVAHGGS AGRRLAAWLV DETGSQTASD
DELAAVAELI ECGGGRRWAS AEARRHVTQG IDMVARIGIP DRPAAELQDL AHYIVDRQA
