ID   ISPT_NEIMA              Reviewed;         248 AA.
AC   Q9JX35; A1INU3;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=NMA0081;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM07400.1; -; Genomic_DNA.
DR   PIR; H81999; H81999.
DR   RefSeq; WP_002246768.1; NC_003116.1.
DR   AlphaFoldDB; Q9JX35; -.
DR   SMR; Q9JX35; -.
DR   EnsemblBacteria; CAM07400; CAM07400; NMA0081.
DR   KEGG; nma:NMA0081; -.
DR   HOGENOM; CLU_038505_1_1_4; -.
DR   OMA; PRTEGHK; -.
DR   BioCyc; NMEN122587:NMA_RS00430-MON; -.
DR   Proteomes; UP000000626; 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; Transferase.
FT   CHAIN           1..248
FT                   /note="Isoprenyl transferase"
FT                   /id="PRO_0000123643"
FT   ACT_SITE        23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        71
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         24..27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         28
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         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         68..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         191..193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   248 AA;  28371 MW;  EAF88B705D3F32C8 CRC64;
     MKSSTQAVLE HTAIPKHIAV IMDGNGRWAK KRFLPRIMGH KRGLDALENM VKHCAKLGVQ
     YLTVFAFSTE NWRRPEDEVS FLMGLFLQAL QKQVRRLHEN NMRLKILGSR ERFNRQILKG
     IEEAEALTAN NTGLTLSIAA DYGGRWDILQ AANKLIAEGV SEITEDTLAK YLMLGDAPEP
     DLFIRTGGET RISNFLLWQM AYAELYFTDI LWPDFDGKAL DDAVASFQKR ERRFGRTSEQ
     LPIEQQRN