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Database: UniProt
Entry: A0A0B6TXJ9_9CORY
LinkDB: A0A0B6TXJ9_9CORY
Original site: A0A0B6TXJ9_9CORY 
ID   A0A0B6TXJ9_9CORY        Unreviewed;       252 AA.
AC   A0A0B6TXJ9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN   Name=uppS2 {ECO:0000313|EMBL:AJK69416.1};
GN   ORFNames=B840_09115 {ECO:0000313|EMBL:AJK69416.1};
OS   Corynebacterium marinum DSM 44953.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1224162 {ECO:0000313|EMBL:AJK69416.1, ECO:0000313|Proteomes:UP000031928};
RN   [1] {ECO:0000313|EMBL:AJK69416.1, ECO:0000313|Proteomes:UP000031928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44953 {ECO:0000313|EMBL:AJK69416.1,
RC   ECO:0000313|Proteomes:UP000031928};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of Corynebacterium marinum DSM 44953.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC       with allylic pyrophosphates generating different type of terpenoids.
CC       {ECO:0000256|HAMAP-Rule:MF_01139}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01139};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01139};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01139}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01139}.
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DR   EMBL; CP007790; AJK69416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B6TXJ9; -.
DR   STRING; 1224162.B840_09115; -.
DR   KEGG; cmq:B840_09115; -.
DR   HOGENOM; CLU_038505_1_2_11; -.
DR   OrthoDB; 4191603at2; -.
DR   Proteomes; UP000031928; 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; Decaprenyl diphosphate synthase-like; 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   NCBIfam; TIGR00055; uppS; 1.
DR   PANTHER; PTHR10291:SF0; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE 2; 1.
DR   PANTHER; PTHR10291; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE FAMILY MEMBER; 1.
DR   Pfam; PF01255; Prenyltransf; 1.
DR   SUPFAM; SSF64005; Undecaprenyl diphosphate synthase; 1.
DR   PROSITE; PS01066; UPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031928};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01139}.
FT   ACT_SITE        30
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   ACT_SITE        78
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         30
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         31..34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         75..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         204..206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   252 AA;  28939 MW;  447433B757DEEBB5 CRC64;
     MVCVNDNAAA LTPPDIPAQF IPRHIALVMD GNGRWAQERG LKRTEGHKRG EAVLMDVVDA
     CLALGVPYLS AYAFSTENWR RSTDEVRFLM GFNRDVLRRQ RDVLNEKGVR VRWVGRRPRL
     WRTVIKELET AEELTRDNTR MTLAMCVNYG GRAELVDAAR EVARRAAAGQ LRPEQITERT
     FAQFLDEPDM PDVDLFLRPS GEKRTSNFLP WHSAYAEMVY QEKLFPDFTP QDLFDAVLEY
     ASRDRRFGGT KS
//
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