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
//