ID   ISPT_CLOAB              Reviewed;         257 AA.
AC   Q97I62;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=CA_C1791;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79756.1; -; Genomic_DNA.
DR   PIR; A97121; A97121.
DR   RefSeq; NP_348416.1; NC_003030.1.
DR   RefSeq; WP_010965097.1; NC_003030.1.
DR   AlphaFoldDB; Q97I62; -.
DR   SMR; Q97I62; -.
DR   STRING; 272562.CA_C1791; -.
DR   EnsemblBacteria; AAK79756; AAK79756; CA_C1791.
DR   GeneID; 44998285; -.
DR   KEGG; cac:CA_C1791; -.
DR   PATRIC; fig|272562.8.peg.1997; -.
DR   eggNOG; COG0020; Bacteria.
DR   HOGENOM; CLU_038505_1_1_9; -.
DR   OMA; PRTEGHK; -.
DR   OrthoDB; 1630604at2; -.
DR   Proteomes; UP000000814; 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..257
FT                   /note="Isoprenyl transferase"
FT                   /id="PRO_0000123598"
FT   ACT_SITE        33
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        81
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         33
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         34..37
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         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         78..80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         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         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         210..212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   257 AA;  29507 MW;  449592C5E9BC2353 CRC64;
     MLNFIRSDKD KGKGNDNDIN FSNIPKHIAI IMDGNGRWAK KRNLPRTMGH KAGGEALKRI
     VRECSDIGVK YLTVYGFSTE NWIRPKEEVN AIMRLIVEFL KREFNELNKN NVIINPIGNI
     LGLPEACITA LNDAKNKTKN NTGLMLNLAL NYGGRDEILN AVKNIFASYE ENKISKDEIF
     NLSDEEFSSY LYTGCIPDPD IIIRPSGEKR LSNFLLWQCA YSEFWYSNIN WPDFSIEDLH
     TAIKDYQNRD RRFGGVK