ZFPP_MYCLE
ID ZFPP_MYCLE Reviewed; 262 AA.
AC Q9CB36;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=ML2467;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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}.
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DR EMBL; AL583925; CAC31984.1; -; Genomic_DNA.
DR PIR; H87217; H87217.
DR RefSeq; NP_302598.1; NC_002677.1.
DR RefSeq; WP_010908917.1; NC_002677.1.
DR AlphaFoldDB; Q9CB36; -.
DR SMR; Q9CB36; -.
DR STRING; 272631.ML2467; -.
DR PRIDE; Q9CB36; -.
DR EnsemblBacteria; CAC31984; CAC31984; CAC31984.
DR KEGG; mle:ML2467; -.
DR PATRIC; fig|272631.5.peg.4736; -.
DR Leproma; ML2467; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_2_0_11; -.
DR OMA; TKGQPDP; -.
DR UniPathway; UPA00772; -.
DR Proteomes; UP000000806; 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; Reference proteome; Transferase.
FT CHAIN 1..262
FT /note="Short-chain Z-isoprenyl diphosphate synthase"
FT /id="PRO_0000123747"
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; 29528 MW; A14987A17CC2BE65 CRC64;
MEIIPPRLKE PLYALYELRL RQGLTASESR LPRHIAVLCD GNRRWARDAG YDDVSYGYRM
GAAKIAEMLR WCQEAGIEMT TVYLLSTENL QRDPDELAAL IEIITDVVEE ICAPANRWSV
RTVGDLELLG EEPACRLRGA VESTPGVAPF HVNVAVGYGG RREIVGAVRA LLGKELANGA
TAEELVEAVT VEGIARNLYT SGQPDPDLVI RTSGEQRLSG FLLWQSAYSE MWFTETHWPA
FRRVDFLRAL RDYSMRHRRY GK
