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ISPT1_BRADU
ID   ISPT1_BRADU             Reviewed;         246 AA.
AC   Q89W41;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Isoprenyl transferase 1 {ECO:0000255|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01139};
GN   Name=uppS1 {ECO:0000255|HAMAP-Rule:MF_01139}; OrderedLocusNames=blr0852;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(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; BA000040; BAC46117.1; -; Genomic_DNA.
DR   RefSeq; NP_767492.1; NC_004463.1.
DR   RefSeq; WP_011083674.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89W41; -.
DR   SMR; Q89W41; -.
DR   STRING; 224911.27349102; -.
DR   EnsemblBacteria; BAC46117; BAC46117; BAC46117.
DR   GeneID; 64020715; -.
DR   KEGG; bja:blr0852; -.
DR   PATRIC; fig|224911.44.peg.234; -.
DR   eggNOG; COG0020; Bacteria.
DR   HOGENOM; CLU_038505_1_1_5; -.
DR   InParanoid; Q89W41; -.
DR   OMA; TKGQPDP; -.
DR   PhylomeDB; Q89W41; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR   GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
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..246
FT                   /note="Isoprenyl transferase 1"
FT                   /id="PRO_0000123579"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        67
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         20..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         64..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         186..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         199
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   246 AA;  27095 MW;  686294270C0552FB CRC64;
     MQSDMTSRSE KLHVGIIMDG NGRWATRRGL SRLRGHEAGV ETIRRIVEAA PKQGIGTLTL
     YAFSTDNWRR PKAEVAALMT LLRFYLANEV QSLVKNGVRL TVIGRRDRLP DGIANAIARA
     EAATAHGSTL HLRIAVDYSA RDAILNAAAK AAALTSLTRE AFSQLVTGEA GLRDVDLIIR
     TSGEKRLSDF LLWEGAYAEL HFTERMWPEF DAGDLAEALA AFHGRERRFG GLQAIMPEEV
     PSLSRV
 
 
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