ID   PYRE_BARQU              Reviewed;         192 AA.
AC   Q6G086;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=BQ04240;
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897700; CAF25923.1; -; Genomic_DNA.
DR   RefSeq; WP_011179212.1; NC_005955.1.
DR   AlphaFoldDB; Q6G086; -.
DR   SMR; Q6G086; -.
DR   STRING; 283165.BQ04240; -.
DR   EnsemblBacteria; CAF25923; CAF25923; BQ04240.
DR   KEGG; bqu:BQ04240; -.
DR   eggNOG; COG0461; Bacteria.
DR   HOGENOM; CLU_074878_3_0_5; -.
DR   OMA; YFQCAKV; -.
DR   OrthoDB; 1280396at2; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000000597; 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   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
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   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01367; pyrE_Therm; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Magnesium; Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..192
FT                   /note="Orotate phosphoribosyltransferase"
FT                   /id="PRO_1000066208"
FT   BINDING         116..124
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         120
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         148
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
SQ   SEQUENCE   192 AA;  20825 MW;  14A0FEB16D1332D1 CRC64;
     MNTQDVIDIF KQADAILEGH FILTSGRHSA IYMQKAQVFM HADLTEKLCR GLAEKIKRSI
     KEKIDYVVGP AIGGLIPSYE TSRHLGIPSL WVERVNGIFE LRRFKIKNGA RVVIVEDIVT
     TGLSIRETVE ALVAAGADVV ASACILDRSG GKVDVGVPLI ALAEYEIVSY ASDALPTELA
     LLPAVKPGSR NI