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ISPT1_TROW8
ID   ISPT1_TROW8             Reviewed;         258 AA.
AC   Q83HR7;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Isoprenyl transferase 1 {ECO:0000255|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01139};
GN   Name=uppS1 {ECO:0000255|HAMAP-Rule:MF_01139}; OrderedLocusNames=TW440;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
CC   -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC       with allylic pyrophosphates generating different type of terpenoids.
CC       {ECO:0000255|HAMAP-Rule:MF_01139}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01139};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01139};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01139}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01139}.
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DR   EMBL; BX251411; CAD67109.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q83HR7; -.
DR   SMR; Q83HR7; -.
DR   KEGG; tws:TW440; -.
DR   HOGENOM; CLU_038505_2_0_11; -.
DR   OMA; TKGQPDP; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
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   Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..258
FT                   /note="Isoprenyl transferase 1"
FT                   /id="PRO_0000123707"
FT   ACT_SITE        39
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        88
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         40..43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         85..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         213..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   258 AA;  29283 MW;  E580BF370CA02E11 CRC64;
     MGGKMLRSVS ELIYKVYARY LLGQINLNNL PGHVALIVDG NRRWARKEKR DRISDGHRAG
     AGKAVDFLHW CDELDINIVT LYLLSNDNLK NRNRQELNDL VQVICNLIAQ VSKRWKVNHV
     GSCENLPELL GNSLEGVKSS TKTNRYSERS MTVNLAIGYS GRAEITEAVR KIVNTYPIGD
     LPEKITEEVI SANLYTGGLS DPDLIIRTSG EQRLSDFMPW QSTHSEFYFL EALGPDLRKV
     DFLRAIRDFS IRRRSFGA
 
 
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