PYRE_HELPY
ID PYRE_HELPY Reviewed; 201 AA.
AC P56162;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01208};
DE Short=OPRT {ECO:0000255|HAMAP-Rule:MF_01208};
DE Short=OPRTase {ECO:0000255|HAMAP-Rule:MF_01208};
DE EC=2.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01208};
GN Name=pyrE {ECO:0000255|HAMAP-Rule:MF_01208}; OrderedLocusNames=HP_1257;
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 CRYSTALLIZATION.
RX PubMed=12872993;
RA Kim M.-K., Song H.-E., Kim Y.S., Rho S.-H., Im Y.J., Lee J.H., Kang G.B.,
RA Eom S.H.;
RT "Crystallization and preliminary X-ray crystallographic analysis of orotate
RT phosphoribosyltransferase from Helicobacter pylori.";
RL Mol. Cells 15:361-363(2003).
CC -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-
CC phosphoribose 1-diphosphate to orotate, leading to the formation of
CC orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01208};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01208};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000511; AAD08303.1; -; Genomic_DNA.
DR PIR; A64677; A64677.
DR RefSeq; NP_208049.1; NC_000915.1.
DR RefSeq; WP_000351558.1; NC_018939.1.
DR PDB; 4PAW; X-ray; 2.23 A; A/B=1-201.
DR PDBsum; 4PAW; -.
DR AlphaFoldDB; P56162; -.
DR SMR; P56162; -.
DR IntAct; P56162; 3.
DR STRING; 85962.C694_06495; -.
DR PaxDb; P56162; -.
DR EnsemblBacteria; AAD08303; AAD08303; HP_1257.
DR KEGG; hpy:HP_1257; -.
DR PATRIC; fig|85962.47.peg.1349; -.
DR eggNOG; COG0461; Bacteria.
DR OMA; YFQCAKV; -.
DR PhylomeDB; P56162; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0006222; P:UMP biosynthetic process; IBA:GO_Central.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01208; PyrE; 1.
DR InterPro; IPR023031; OPRT.
DR InterPro; IPR006273; Orotate_PRibTrfase_bac.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01367; pyrE_Therm; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Magnesium; Pyrimidine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..201
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000110701"
FT BINDING 113..121
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 117
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 145
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:4PAW"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:4PAW"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:4PAW"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:4PAW"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:4PAW"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:4PAW"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:4PAW"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:4PAW"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:4PAW"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4PAW"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:4PAW"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:4PAW"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:4PAW"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4PAW"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:4PAW"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4PAW"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4PAW"
SQ SEQUENCE 201 AA; 21903 MW; 9FD8A1DE81787837 CRC64;
MDIKACYQNA KALLEGHFLL SSGFHSNYYL QSAKVLEDPK LAEQLALELA KQIQEAHLNI
ECVCSPAIGG ILAGYELARA LGVRFIFTER VDNTMALRRG FEVKKNEKIL VCEDIITTGK
SAMECAKVLE EKGAQIVAFG ALANRGICKR AHSHLKAQEG ACLPSHLPLF ALEDFVFDMH
KPSSCPLCAT SVAIKPGSRG N
