ID   ZFPP_MYCBO              Reviewed;         262 AA.
AC   Q7U0P8; A0A1R3XXC4; X2BH82;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Short-chain Z-isoprenyl diphosphate synthase;
DE            EC=2.5.1.68;
DE   AltName: Full=(2Z,6E)-farnesyl diphosphate synthase;
DE   AltName: Full=Z-FPP synthase;
DE   AltName: Full=Z-isoprenyl diphosphate synthase;
GN   OrderedLocusNames=BQ2027_MB1115;
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: Generates Z-farnesyl diphosphate (Z-FPP) from isopentenyl
CC       pyrophosphate (IPP). Z-FPP is the precursor of decaprenyl diphosphate,
CC       which has a central role in the biosynthesis of the mycobacterial cell
CC       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   -!- PATHWAY: Phospholipid metabolism; decaprenyl phosphate biosynthesis.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. Z-FPP synthase
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT708304; SIT99714.1; -; Genomic_DNA.
DR   RefSeq; NP_854770.1; NC_002945.3.
DR   RefSeq; WP_003903314.1; NC_002945.4.
DR   AlphaFoldDB; Q7U0P8; -.
DR   SMR; Q7U0P8; -.
DR   BindingDB; Q7U0P8; -.
DR   EnsemblBacteria; SIT99714; SIT99714; BQ2027_MB1115.
DR   PATRIC; fig|233413.5.peg.1217; -.
DR   OMA; TKGQPDP; -.
DR   UniPathway; UPA00772; -.
DR   Proteomes; UP000001419; Chromosome.
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   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 shape; Cell wall biogenesis/degradation; Magnesium; Metal-binding;
KW   Peptidoglycan synthesis; Transferase.
FT   CHAIN           1..262
FT                   /note="Short-chain Z-isoprenyl diphosphate synthase"
FT                   /id="PRO_0000123746"
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"
SQ   SEQUENCE   262 AA;  29479 MW;  2D6745753FE22518 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 RDYSARHRRY GR