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PYRE_XANC5
ID   PYRE_XANC5              Reviewed;         219 AA.
AC   Q3BNB6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=XCV4016;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ25747.1; -; Genomic_DNA.
DR   RefSeq; WP_011348851.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BNB6; -.
DR   SMR; Q3BNB6; -.
DR   STRING; 456327.BJD11_02535; -.
DR   EnsemblBacteria; CAJ25747; CAJ25747; XCV4016.
DR   KEGG; xcv:XCV4016; -.
DR   eggNOG; COG0461; Bacteria.
DR   HOGENOM; CLU_074878_0_1_6; -.
DR   OMA; MKAYQRQ; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000007069; 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; Transferase.
FT   CHAIN           1..219
FT                   /note="Orotate phosphoribosyltransferase"
FT                   /id="PRO_1000066324"
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         98
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         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                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         102
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         104
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   219 AA;  22858 MW;  5F31CE9F17C25B7D CRC64;
     MTDHRTRFLQ LALDADALRF GEFTLKSGRL SPYFFNAGRF DSGAKTAQLA QCYADAIDAA
     GLDFDLLFGP AYKGIPLATA LACAYAGRGR DLPLAFNRKE AKDHGEGGTL IGAPLAGRKV
     LIVDDVITAG TAIREALAII RAAGGMPSGI VVALDRQEIA SDQDRRSAAQ AVAAEAGIPV
     IAVANLGDLL AFAAGNADLV GFQEPLLAYR GRYGTDTTG
 
 
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