ID   D6JGV5_ECOLX            Unreviewed;       213 AA.
AC   D6JGV5;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   16-OCT-2013, entry version 18.
DE   RecName: Full=Orotate phosphoribosyltransferase;
DE            Short=OPRT;
DE            Short=OPRTase;
DE            EC=2.4.2.10;
GN   Name=pyrE; ORFNames=ECEG_04150;
OS   Escherichia coli B354.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=550677;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B354;
RG   The Broad Institute Genome Sequencing Platform, The Broad Institute
RG   Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S.,
RA   Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.I.,
RA   Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA   Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J.,
RA   Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Escherichia coli B354.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from
CC       5-phosphoribose 1-diphosphate to orotate, leading to the formation
CC       of orotidine monophosphate (OMP) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate
CC       + 5-phospho-alpha-D-ribose 1-diphosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from orotate: step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. PyrE subfamily.
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DR   EMBL; GG749337; EFF11216.2; -; Genomic_DNA.
DR   ProteinModelPortal; D6JGV5; -.
DR   SMR; D6JGV5; 1-213.
DR   EnsemblBacteria; EFF11216; EFF11216; ECEG_04150.
DR   PATRIC; 35881307; VBIEscCol143929_4216.
DR   OMA; DRMEKLP; -.
DR   UniPathway; UPA00070; UER00119.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01208; PyrE; 1; -.
DR   InterPro; IPR023031; OPRT.
DR   InterPro; IPR004467; Or_phspho_trans_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   TIGRFAMs; TIGR00336; pyrE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Magnesium; Pyrimidine biosynthesis; Transferase.
FT   REGION       34     35       Orotate binding (By similarity).
FT   REGION       72     73       5-phosphoribose 1-diphosphate binding (By
FT                                similarity).
FT   REGION      124    132       5-phosphoribose 1-diphosphate binding (By
FT                                similarity).
FT   BINDING      26     26       5-phosphoribose 1-diphosphate (By
FT                                similarity).
FT   BINDING      99     99       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner (By similarity).
FT   BINDING     100    100       5-phosphoribose 1-diphosphate (By
FT                                similarity).
FT   BINDING     103    103       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner (By similarity).
FT   BINDING     105    105       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner (By similarity).
FT   BINDING     128    128       Orotate (By similarity).
FT   BINDING     156    156       Orotate (By similarity).
SQ   SEQUENCE   213 AA;  23567 MW;  F618A6D0A119B9D4 CRC64;
     MKPYQRQFIE FALSKQVLKF GEFTLKSGRK SPYFFNAGLF NTGRDLALLG RFYAEALVDS
     GIEFDLLFGP AYKGIPIATT TAVALAEHHD LDLPYCFNRK EAKDHGEGGN LVGSALQGRV
     MLVDDVITAG TAIRESMEII QANGATLAGV LISLDRQERG RGEISAIQEV ERDYNCKVIS
     IITLKDLIAY LEEKPEMAEH LAAVKAYREE FGV
//