ID   ISPT_STRMU              Reviewed;         249 AA.
AC   Q8DSJ7;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Isoprenyl transferase {ECO:0000255|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01139};
GN   Name=uppS {ECO:0000255|HAMAP-Rule:MF_01139}; OrderedLocusNames=SMU_1786;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59413.1; -; Genomic_DNA.
DR   RefSeq; NP_722107.1; NC_004350.2.
DR   RefSeq; WP_002263518.1; NC_004350.2.
DR   AlphaFoldDB; Q8DSJ7; -.
DR   SMR; Q8DSJ7; -.
DR   STRING; 210007.SMU_1786; -.
DR   PRIDE; Q8DSJ7; -.
DR   EnsemblBacteria; AAN59413; AAN59413; SMU_1786.
DR   GeneID; 66818836; -.
DR   KEGG; smu:SMU_1786; -.
DR   PATRIC; fig|210007.7.peg.1594; -.
DR   eggNOG; COG0020; Bacteria.
DR   HOGENOM; CLU_038505_1_1_9; -.
DR   OMA; PRTEGHK; -.
DR   PhylomeDB; Q8DSJ7; -.
DR   Proteomes; UP000002512; Chromosome.
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; Reference proteome; Transferase.
FT   CHAIN           1..249
FT                   /note="Isoprenyl transferase"
FT                   /id="PRO_0000123689"
FT   ACT_SITE        25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        73
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         25
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         26..29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         70..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         203..205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   249 AA;  28524 MW;  6E578309FF2237CA CRC64;
     MFTLRRKKQD IKLSKIPAHI GIIMDGNGRW AKKRMKPRVF GHKAGMDALQ DVTIAASELG
     VKILTVYAFS TENWARPQEE VKFIMNLPVE FFDKYVPKLH KNNVRILVIG DKEELPAATL
     DALERARELT KHNSGLILNF ALNYGGRAEI VDAVKLIAQD VLDARFNPGD ITEGLIADYL
     MTSNLPYLYR DPDLIIRTSG ELRLSNFLPW QAAYSELYFT DTLWPDFDKK ALYLAIEEFN
     HRHRRFGGV