ISPT_ENTFA
ID ISPT_ENTFA Reviewed; 271 AA.
AC Q831K9;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
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}; OrderedLocusNames=EF_2495;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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}.
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DR EMBL; AE016830; AAO82211.1; -; Genomic_DNA.
DR RefSeq; NP_816141.1; NC_004668.1.
DR RefSeq; WP_002362225.1; NZ_KE136528.1.
DR PDB; 6LOI; X-ray; 2.50 A; A/B/C/D/E/F=1-271.
DR PDBsum; 6LOI; -.
DR AlphaFoldDB; Q831K9; -.
DR SMR; Q831K9; -.
DR STRING; 226185.EF_2495; -.
DR EnsemblBacteria; AAO82211; AAO82211; EF_2495.
DR KEGG; efa:EF2495; -.
DR PATRIC; fig|226185.45.peg.1053; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_1_1_9; -.
DR OMA; PRTEGHK; -.
DR Proteomes; UP000001415; 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; -; 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 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..271
FT /note="Isoprenyl transferase"
FT /id="PRO_0000123612"
FT ACT_SITE 35
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT ACT_SITE 83
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 36..39
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 80..82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 84
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 207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 213..215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 48..69
FT /evidence="ECO:0007829|PDB:6LOI"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:6LOI"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:6LOI"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:6LOI"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:6LOI"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 156..172
FT /evidence="ECO:0007829|PDB:6LOI"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:6LOI"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:6LOI"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:6LOI"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:6LOI"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6LOI"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:6LOI"
SQ SEQUENCE 271 AA; 31005 MW; E91C5240ABE3979E CRC64;
MLRFFPQKNK YVEEASQYAF DKEGQIPQHI AIIMDGNGRW AQNRRLPRIA GHKEGMDTVK
KITKHASHLG VKVLTLYAFS TENWKRPTDE VNFLMQLPVD FFDTFVPELI KENVKVNVMG
YQEFLPSHTQ DAVKRAIEQT KDNTGMVLNF ALNYGARAEL LTAMKQIAAE VSEKAYTADE
ITEETIADHL MTGFLPTELR DPELLIRTSG EERISNFLLW QIAYSELFFT KALWPDFSGD
TLETAIASFQ NRNRRFGGLK ETTETEGSDP Q
