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PYRE_PSESM
ID   PYRE_PSESM              Reviewed;         213 AA.
AC   Q88BD7;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=PSPTO_0080;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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}.
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DR   EMBL; AE016853; AAO53634.1; -; Genomic_DNA.
DR   RefSeq; NP_789939.1; NC_004578.1.
DR   RefSeq; WP_007246510.1; NC_004578.1.
DR   AlphaFoldDB; Q88BD7; -.
DR   SMR; Q88BD7; -.
DR   STRING; 223283.PSPTO_0080; -.
DR   EnsemblBacteria; AAO53634; AAO53634; PSPTO_0080.
DR   GeneID; 1181688; -.
DR   KEGG; pst:PSPTO_0080; -.
DR   PATRIC; fig|223283.9.peg.84; -.
DR   eggNOG; COG0461; Bacteria.
DR   HOGENOM; CLU_074878_0_1_6; -.
DR   OMA; MKAYQRQ; -.
DR   OrthoDB; 1280396at2; -.
DR   PhylomeDB; Q88BD7; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR004467; Or_phspho_trans_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR00336; pyrE; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Magnesium; Pyrimidine biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..213
FT                   /note="Orotate phosphoribosyltransferase"
FT                   /id="PRO_0000110726"
FT   BINDING         26
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         34..35
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         72..73
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         99
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         100
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         103
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         105
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         124..132
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         128
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         156
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
SQ   SEQUENCE   213 AA;  23170 MW;  980BDD8EE17B9111 CRC64;
     MQAYQRDFIR FAIDRGVLRF GEFTLKSGRT SPYFFNAGLF NTGSALAQLG RFYAAAVVES
     GIRFDVLFGP AYKGIPLASA TAVALAEHHD RDLPWCFNRK EAKAHGEGGS LVGSPLAGNV
     LIIDDVITAG TAIREVMQII KDQDATAAGV LIALNRQERG NGELSAIQEV ERDFGIPVVS
     IVSLNQVLEF LADDEQLKQH LPAVEAYRAQ YGI
 
 
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