ISPT_STRFR
ID ISPT_STRFR Reviewed; 259 AA.
AC P20182;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 95.
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};
OS Streptomyces fradiae (Streptomyces roseoflavus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1906;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn4556;
RX PubMed=2155856; DOI=10.1016/0378-1119(90)90107-3;
RA Siemieniak D.R., Slightom J.L., Chung S.T.;
RT "Nucleotide sequence of Streptomyces fradiae transposable element Tn4556: a
RT class-II transposon related to Tn3.";
RL Gene 86:1-9(1990).
RN [2]
RP CONCEPTUAL TRANSLATION.
RX PubMed=8091860; DOI=10.1002/yea.320100006;
RA Wolfe K.H., Lohan A.J.E.;
RT "Sequence around the centromere of Saccharomyces cerevisiae chromosome II:
RT similarity of CEN2 to CEN4.";
RL Yeast 10:S41-S46(1994).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M29297; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M29297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
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..259
FT /note="Isoprenyl transferase"
FT /id="PRO_0000123688"
FT ACT_SITE 33
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT ACT_SITE 82
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 34..37
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 79..81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ SEQUENCE 259 AA; 29130 MW; 9B9D32BA9336BFEC CRC64;
MRTADLFYAL YARRLRRQTA AGPLPKHIGL IMDGNRRWAR QMGMANPSIG HRYGAEHVES
VLSWCETAGI KHVTVFVCST ENLQRRGDTE VSFLMQVIEQ VVAVHLARPD ARWQVRIAGT
LDXPCADSTA HALKEAVEAT RRCTTGSQVT LAIGYGGRQE VIDAVRELLH EQAAAGTTLE
DLAASLTMDD ITRHLYTAGQ PDPDLVIRTS GEQRMSNFLL WQSAYSELYF CEAYWPAFRE
IDFLRALRSY AARQRRYGA
