ISPT_HELPY
ID ISPT_HELPY Reviewed; 234 AA.
AC P55984;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Isoprenyl transferase;
DE EC=2.5.1.-;
GN Name=uppS; OrderedLocusNames=HP_1221;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 4-233, AND SUBUNIT.
RX PubMed=18382620; DOI=10.1155/2008/841312;
RA Kuo C.J., Guo R.T., Lu I.L., Liu H.G., Wu S.Y., Ko T.P., Wang A.H.,
RA Liang P.H.;
RT "Structure-based inhibitors exhibit differential activities against
RT Helicobacter pylori and Escherichia coli undecaprenyl pyrophosphate
RT synthases.";
RL J. Biomed. Biotechnol. 2008:841312-841312(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RA Guo R.T., Kuo C.J., Chen C.L., Ko T.P., Liang P.H., Wang A.H.-J.;
RT "Biochemical characterization, crystal structure, and inhibitors of
RT Helicobacter pylori undecaprenyl pyrophosphate synthase.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC with allylic pyrophosphates generating different type of terpenoids.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18382620, ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; AE000511; AAD08263.1; -; Genomic_DNA.
DR PIR; E64672; E64672.
DR RefSeq; NP_208013.1; NC_000915.1.
DR RefSeq; WP_000370674.1; NC_018939.1.
DR PDB; 2D2R; X-ray; 1.88 A; A/B=2-233.
DR PDB; 2DTN; X-ray; 2.50 A; A/B=2-233.
DR PDBsum; 2D2R; -.
DR PDBsum; 2DTN; -.
DR AlphaFoldDB; P55984; -.
DR SMR; P55984; -.
DR IntAct; P55984; 2.
DR STRING; 85962.C694_06305; -.
DR PaxDb; P55984; -.
DR EnsemblBacteria; AAD08263; AAD08263; HP_1221.
DR KEGG; hpy:HP_1221; -.
DR PATRIC; fig|85962.47.peg.1309; -.
DR eggNOG; COG0020; Bacteria.
DR OMA; PRTEGHK; -.
DR PhylomeDB; P55984; -.
DR BRENDA; 2.5.1.31; 2604.
DR EvolutionaryTrace; P55984; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR GO; GO:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
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..234
FT /note="Isoprenyl transferase"
FT /id="PRO_0000123623"
FT ACT_SITE 13
FT /evidence="ECO:0000250"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 14..17
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 58..60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2D2R"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:2D2R"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2D2R"
FT HELIX 26..45
FT /evidence="ECO:0007829|PDB:2D2R"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2D2R"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2D2R"
FT HELIX 69..89
FT /evidence="ECO:0007829|PDB:2D2R"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2D2R"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2D2R"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:2D2R"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:2D2R"
FT HELIX 134..147
FT /evidence="ECO:0007829|PDB:2D2R"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2D2R"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:2D2R"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:2D2R"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2D2R"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2DTN"
FT TURN 192..197
FT /evidence="ECO:0007829|PDB:2D2R"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:2D2R"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2D2R"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:2D2R"
SQ SEQUENCE 234 AA; 27455 MW; F3C84720F9E4EB96 CRC64;
MDNTLKHLAI IMDGNGRWAK LKNKARAYGH KKGVKTLKDI TIWCANHKLE CLTLYAFSTE
NWKRPKSEVD FLMKMLKKYL KDERSTYLNN NIRFRAIGDL EGFSKELRDT ILQLENDTRH
FKDFTQVLAL NYGSKNELSR AFKSLLESPP SHINLLESLE NEISNRLDTH DLPEVDLLLR
TGGEMRLSNF LLWQSSYAEL FFTPILWPDF TPKDLENIIS DFYKRVRKFG ELKC
