ID A0A0W7W748_9MICO Unreviewed; 261 AA.
AC A0A0W7W748;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN ORFNames=AUL38_13305 {ECO:0000313|EMBL:KUF06394.1};
OS Leucobacter sp. G161.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF06394.1, ECO:0000313|Proteomes:UP000053012};
RN [1] {ECO:0000313|EMBL:KUF06394.1, ECO:0000313|Proteomes:UP000053012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G161 {ECO:0000313|EMBL:KUF06394.1,
RC ECO:0000313|Proteomes:UP000053012};
RA Ge S., Dong X.;
RT "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT effective chromium reducer.";
RL Submitted (DEC-2015) 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. Z-FPP synthase
CC subfamily. {ECO:0000256|ARBA:ARBA00038453}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01139}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF06394.1}.
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DR EMBL; LOHP01000069; KUF06394.1; -; Genomic_DNA.
DR RefSeq; WP_059062517.1; NZ_LOHP01000069.1.
DR AlphaFoldDB; A0A0W7W748; -.
DR STRING; 663704.AUL38_13305; -.
DR OrthoDB; 4191603at2; -.
DR Proteomes; UP000053012; Unassembled WGS sequence.
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:SF43; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE COMPLEX SUBUNIT DHDDS; 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:UP000053012};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01139}.
FT ACT_SITE 39
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT ACT_SITE 88
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 40..43
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 85..87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 216..218
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ SEQUENCE 261 AA; 29127 MW; 3E98E821E183C4FB CRC64;
MSSQPTPQRT GLLYRLYQRR LRREIVEAQV PHHVAIIVDG NRRWAKQRLQ ERAAFGHRAG
ARKVPEFLGW CETAGVKVVT LYLLSADNLN ARASDELTDL FGIIGELATE LSRNPDWRVQ
HVGSCDGLDP ELAAALGAAE ERTRGNTGLH VNLAVGYGGR SEIAAAVRSV IEAHQEAGGT
LDTLAETLTP DKIGEHLWTR GQADPDLVIR TSGEQRISDF MIWQSAHSEF YFVEALYPDL
REVDFLRALR DYSSRQRRLG G
//