ID PYRE_SHIDS Reviewed; 213 AA.
AC Q329L4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 01-MAY-2013, entry version 66.
DE RecName: Full=Orotate phosphoribosyltransferase;
DE Short=OPRT;
DE Short=OPRTase;
DE EC=2.4.2.10;
GN Name=pyrE; OrderedLocusNames=SDY_4073;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB63991.1; -; Genomic_DNA.
DR RefSeq; YP_405482.1; NC_007606.1.
DR ProteinModelPortal; Q329L4; -.
DR SMR; Q329L4; 1-213.
DR STRING; 300267.SDY_4073; -.
DR EnsemblBacteria; ABB63991; ABB63991; SDY_4073.
DR GeneID; 3795845; -.
DR KEGG; sdy:SDY_4073; -.
DR PATRIC; 18698873; VBIShiDys99784_4792.
DR eggNOG; COG0461; -.
DR HOGENOM; HOG000037974; -.
DR KO; K00762; -.
DR OMA; MKAYQRQ; -.
DR ProtClustDB; PRK00455; -.
DR BioCyc; SDYS300267:GJEW-4069-MONOMER; -.
DR UniPathway; UPA00070; UER00119.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA: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.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 3: Inferred from homology;
KW Complete proteome; Glycosyltransferase; Magnesium;
KW Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1 213 Orotate phosphoribosyltransferase.
FT /FTId=PRO_1000066296.
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; 23495 MW; F618A6D0A2AF59D4 CRC64;
MKPYQRQFIE FALSKQVLKF GEFTLKSGRK SPYFFNAGLF NTGRDLALLG RFYAEALVDS
GIEFDLLFGP AYKGIPIATT TAVALAEHHD LDLPYCFNRK EAKDHGEGGN LVGSALQGRV
MLVDDVITAG TAIRESMEII QANGATLAGV LISLDRQERG RGEISAIQEV ERDYNCKVIS
IITLKDLIAY LEGKPEMAEH LAAVKAYREE FGV
//
