(data stored in ACNUC9435 zone)

SWISSPROT: PYRE_CLOD6

ID   PYRE_CLOD6              Reviewed;         194 AA.
AC   Q18CS5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 77.
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=CD630_01870;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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}.
DR   EMBL; AM180355; CAJ67009.1; -; Genomic_DNA.
DR   RefSeq; WP_003420885.1; NZ_CP010905.2.
DR   RefSeq; YP_001086657.1; NC_009089.1.
DR   SMR; Q18CS5; -.
DR   STRING; 272563.CD630_01870; -.
DR   EnsemblBacteria; CAJ67009; CAJ67009; CD630_01870.
DR   GeneID; 4915023; -.
DR   KEGG; cdf:CD630_01870; -.
DR   KEGG; pdc:CDIF630_00308; -.
DR   PATRIC; fig|272563.120.peg.202; -.
DR   eggNOG; ENOG4107XPQ; Bacteria.
DR   eggNOG; COG0461; LUCA.
DR   HOGENOM; HOG000059806; -.
DR   KO; K00762; -.
DR   OMA; YFQCAKV; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000001978; 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:0009116; P:nucleoside metabolic process; IEA:InterPro.
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.
PE   3: Inferred from homology;
DR   PRODOM; Q18CS5.
DR   SWISS-2DPAGE; Q18CS5.
KW   Glycosyltransferase; Magnesium; Pyrimidine biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..194
FT                   /note="Orotate phosphoribosyltransferase"
FT                   /id="PRO_1000138782"
FT   REGION          114..122
FT                   /note="5-phosphoribose 1-diphosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         118
FT                   /note="Orotate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         146
FT                   /note="Orotate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
SQ   SEQUENCE   194 AA;  21301 MW;  6318597262803BBF CRC64;
     MSKVDVVDIL KKSDALLEGH FLLSSGKHSN RYVQCAKVLR FPEYAAEVLS TVVEQIKDLD
     IDLVVGPAMG GVIVSYELGR QLGKEAVFTE RKDNTMELRR GFEVKKGAKI IIAEDVVTTG
     KSTMETKRVL EALGGEVVGV ACIADRTNHD IGMPIYSAIK LDIQVYESDE CPLCKEGKLP
     VVKPGSREFK ELGM
//

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