ID   ISPT_TREDE              Reviewed;         227 AA.
AC   Q73K76;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=TDE_2344;
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA   Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA   Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA   Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12862.1; -; Genomic_DNA.
DR   RefSeq; NP_972943.1; NC_002967.9.
DR   RefSeq; WP_002675801.1; NC_002967.9.
DR   AlphaFoldDB; Q73K76; -.
DR   SMR; Q73K76; -.
DR   STRING; 243275.TDE_2344; -.
DR   EnsemblBacteria; AAS12862; AAS12862; TDE_2344.
DR   GeneID; 2739439; -.
DR   KEGG; tde:TDE_2344; -.
DR   PATRIC; fig|243275.7.peg.2212; -.
DR   eggNOG; COG0020; Bacteria.
DR   HOGENOM; CLU_038505_1_1_12; -.
DR   OMA; PRTEGHK; -.
DR   OrthoDB; 1630604at2; -.
DR   Proteomes; UP000008212; 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..227
FT                   /note="Isoprenyl transferase"
FT                   /id="PRO_0000123705"
FT   ACT_SITE        13
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        61
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         14..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         26
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         58..60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         181..183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   227 AA;  25879 MW;  1702F80788DDBF26 CRC64;
     MSDELKHIAI VMDGNGRWAK KRGLPRSMGH KEGLNTVKRI TKAVSDLGIP YITLYIFSTE
     NWKRTEAEVG FLMGLIKQHL KAELKFYADN NIRIEHIGNL SGLPQDIQDE INSVRDKTSA
     YTGTAIVLGI NYGAHDEILR AIKKLNSDEL ASINEESFSL KLDTGKIPPV DLLIRTGGEK
     RLSNFLLWQS AYAELYFTDT LWPDWTVENL YEAIEDYKKR NRRYGNA