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Database: UniProt
Entry: A0A0W7W748_9MICO
LinkDB: A0A0W7W748_9MICO
Original site: A0A0W7W748_9MICO 
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
//
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