ZFPP_MYCTO
ID ZFPP_MYCTO Reviewed; 262 AA.
AC P9WFF4; L0T8K3; O53434;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=(2Z,6E)-farnesyl diphosphate synthase;
DE EC=2.5.1.68;
DE AltName: Full=Short-chain Z-isoprenyl diphosphate synthase;
DE AltName: Full=Z-FPP synthase;
DE Short=Z-FPPS;
DE AltName: Full=Z-Polyprenyl diphosphate synthase;
DE AltName: Full=Z-isoprenyl diphosphate synthase;
GN OrderedLocusNames=MT1118;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the condensation of only one isopentenyl
CC pyrophosphate (IPP) unit in the cis configuration to E-geranyl
CC diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl
CC diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl
CC diphosphate, which has a central role in the biosynthesis of the
CC mycobacterial cell wall (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2Z,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:23300,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:162247; EC=2.5.1.68;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. Z-FPP synthase
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000516; AAK45374.1; -; Genomic_DNA.
DR PIR; D70895; D70895.
DR RefSeq; WP_003906511.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WFF4; -.
DR SMR; P9WFF4; -.
DR EnsemblBacteria; AAK45374; AAK45374; MT1118.
DR KEGG; mtc:MT1118; -.
DR PATRIC; fig|83331.31.peg.1203; -.
DR HOGENOM; CLU_038505_2_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0033850; F:Z-farnesyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR CDD; cd00475; Cis_IPPS; 1.
DR Gene3D; 3.40.1180.10; -; 1.
DR HAMAP; MF_01139; ISPT; 1.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR018520; UPP_synth-like_CS.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Magnesium; Membrane; Metal-binding; Transferase.
FT CHAIN 1..262
FT /note="(2Z,6E)-farnesyl diphosphate synthase"
FT /id="PRO_0000428548"
FT ACT_SITE 40
FT /evidence="ECO:0000250"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 41..44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217..219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Important for determining product length"
FT /evidence="ECO:0000250"
SQ SEQUENCE 262 AA; 29410 MW; 2D6745748FE22518 CRC64;
MEIIPPRLKE PLYRLYELRL RQGLAASKSD LPRHIAVLCD GNRRWARSAG YDDVSYGYRM
GAAKIAEMLR WCHEAGIELA TVYLLSTENL QRDPDELAAL IEIITDVVEE ICAPANHWSV
RTVGDLGLIG EEPARRLRGA VESTPEVASF HVNVAVGYGG RREIVDAVRA LLSKELANGA
TAEELVDAVT VEGISENLYT SGQPDPDLVI RTSGEQRLSG FLLWQSAYSE MWFTEAHWPA
FRHVDFLRAL RDYSARHRSY GR
