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