ID   ISPT_CLOTE              Reviewed;         255 AA.
AC   Q895K8;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=CTC_01265;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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; AE015927; AAO35832.1; -; Genomic_DNA.
DR   RefSeq; WP_011099494.1; NC_004557.1.
DR   AlphaFoldDB; Q895K8; -.
DR   SMR; Q895K8; -.
DR   STRING; 212717.CTC_01265; -.
DR   EnsemblBacteria; AAO35832; AAO35832; CTC_01265.
DR   GeneID; 64179054; -.
DR   KEGG; ctc:CTC_01265; -.
DR   HOGENOM; CLU_038505_1_1_9; -.
DR   OMA; PRTEGHK; -.
DR   OrthoDB; 1630604at2; -.
DR   Proteomes; UP000001412; 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..255
FT                   /note="Isoprenyl transferase"
FT                   /id="PRO_0000123600"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        83
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         35
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         36..39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         48
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         80..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         209..211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   255 AA;  29820 MW;  5D611CBEE1F90464 CRC64;
     MWNIFKNKSG QSHKVKDKFQ LDLDNIPKHI AIIMDGNGRW AKERKLPRSL GHKAGVETIR
     DIVKECNNIG VRYLTLYAFS TENWKRPKEE INALMELLVN YLRKEVAELH QNNVVVNTIG
     DVSKLPKACE DELMKAYNKT KNNTGLVLNL ALNYGGRDEI IRAIKLMYKD IEKKGLDIEN
     VNEDLLKNYL YTKGMPDPDL IIRPSGEQRI SNFLLWQCAY SEFWYSNIKW PDFKKHHLHK
     AIKDYQNRNR RFGGV