ID   ISPT_BIFLO              Reviewed;         264 AA.
AC   Q8G7Y3;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=BL0101;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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; AE014295; AAN23966.1; -; Genomic_DNA.
DR   RefSeq; NP_695330.1; NC_004307.2.
DR   AlphaFoldDB; Q8G7Y3; -.
DR   SMR; Q8G7Y3; -.
DR   STRING; 206672.BL0101; -.
DR   EnsemblBacteria; AAN23966; AAN23966; BL0101.
DR   KEGG; blo:BL0101; -.
DR   PATRIC; fig|206672.9.peg.108; -.
DR   HOGENOM; CLU_038505_1_2_11; -.
DR   OMA; PRTEGHK; -.
DR   PhylomeDB; Q8G7Y3; -.
DR   Proteomes; UP000000439; 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..264
FT                   /note="Isoprenyl transferase"
FT                   /id="PRO_0000123574"
FT   ACT_SITE        43
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         43
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         44..47
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         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         88..90
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         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         217..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   264 AA;  30244 MW;  AECEAC1C9E1366C7 CRC64;
     MSMAFENVDY TSLDIPAAPF SDPARIPDFP KNKVPRHIGV IMDGNGRWAK QRGMVRTNGH
     QAAEPVVFDT IAGAIEAGVR YLSLYTFSTE NWKRSPQEVR FLMGFSREII HRRVEQMDEW
     GVRVRWSGRR PKLWKSVIDE LEAAEERTKN NKVIDVVFCI NYGGRAEIAD ACAAIAREVR
     DGKISGDRVT EKMIADHLYN PDIPDCDLVI RTSGEQRTSN FLPWEAAYAE LDFVPELFPD
     CGRDVLWRSI DHYIHRDRRF GGVK