ID PYRE_ECOLI Reviewed; 213 AA. AC P0A7E3; P00495; Q2M7V6; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 30-NOV-2010, entry version 54. DE RecName: Full=Orotate phosphoribosyltransferase; DE Short=OPRT; DE Short=OPRTase; DE EC=2.4.2.10; GN Name=pyrE; OrderedLocusNames=b3642, JW3617; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND RP SUBUNIT. RC STRAIN=K12; RX MEDLINE=83287414; PubMed=6349999; RX DOI=10.1111/j.1432-1033.1983.tb07641.x; RA Poulsen P., Jensen K.F., Valentin-Hansen P., Carlsson P., RA Lundberg L.G.; RT "Nucleotide sequence of the Escherichia coli pyrE gene and of the DNA RT in front of the protein-coding region."; RL Eur. J. Biochem. 135:223-229(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=85003588; PubMed=6207018; RA Poulsen P., Bonekamp F., Jensen K.F.; RT "Structure of the Escherichia coli pyrE operon and control of pyrE RT expression by a UTP modulated intercistronic attentuation."; RL EMBO J. 3:1783-1790(1984). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=93315143; PubMed=7686882; DOI=10.1006/geno.1993.1230; RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.; RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli RT genome: organizational symmetry around the origin of replication."; RL Genomics 16:551-561(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH DIPHOSPHATE RP ANALOG, FUNCTION, ENZYME REGULATION, AND SUBUNIT. RX MEDLINE=96183498; PubMed=8620002; DOI=10.1021/bi952226y; RA Henriksen A., Aghajari N., Jensen K.F., Gajhede M.; RT "A flexible loop at the dimer interface is a part of the active site RT of the adjacent monomer of Escherichia coli orotate RT phosphoribosyltransferase."; RL Biochemistry 35:3803-3809(1996). 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 -!- ENZYME REGULATION: Inhibited by sulfate and phosphate ions. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 1/2. CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC P0A6B7:iscS; NbExp=1; IntAct=EBI-1133376, EBI-550055; CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. PyrE subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X00781; CAA25358.1; -; Genomic_DNA. DR EMBL; V01578; CAA24899.1; -; Genomic_DNA. DR EMBL; L10328; AAA61995.1; -; Genomic_DNA. DR EMBL; U00096; AAC76666.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77650.1; -; Genomic_DNA. DR PIR; D65165; XJEC. DR RefSeq; AP_004149.1; AC_000091.1. DR RefSeq; NP_418099.1; NC_000913.2. DR PDB; 1ORO; X-ray; 2.40 A; A/B=1-213. DR PDBsum; 1ORO; -. DR ProteinModelPortal; P0A7E3; -. DR SMR; P0A7E3; 1-213. DR IntAct; P0A7E3; 1. DR STRING; P0A7E3; -. DR ECO2DBASE; D023.3; 6TH EDITION. DR EnsemblBacteria; EBESCT00000001508; EBESCP00000001508; EBESCG00000001254. DR EnsemblBacteria; EBESCT00000017906; EBESCP00000017197; EBESCG00000016962. DR GeneID; 948157; -. DR GenomeReviews; AP009048_GR; JW3617. DR GenomeReviews; U00096_GR; b3642. DR KEGG; ecj:JW3617; -. DR KEGG; eco:b3642; -. DR EchoBASE; EB0801; -. DR EcoGene; EG10808; pyrE. DR eggNOG; COG0461; -. DR HOGENOM; HBG404341; -. DR OMA; FAFNRKE; -. DR ProtClustDB; PRK00455; -. DR BioCyc; EcoCyc:OROPRIBTRANS-MONOMER; -. DR BioCyc; MetaCyc:OROPRIBTRANS-MONOMER; -. DR Genevestigator; P0A7E3; -. DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki. DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoliWiki. DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IDA:EcoliWiki. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IMP:EcoliWiki. DR HAMAP; MF_01208; PyrE; 1; -. DR InterPro; IPR004467; Or_phspho_trans_clade-1. DR InterPro; IPR023031; Orotate_PribosylTferase. DR InterPro; IPR000836; PRibTrfase. DR Pfam; PF00156; Pribosyltran; 1. DR TIGRFAMs; TIGR00336; pyrE; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Glycosyltransferase; Magnesium; Pyrimidine biosynthesis; Transferase. FT INIT_MET 1 1 Removed. FT CHAIN 2 213 Orotate phosphoribosyltransferase. FT /FTId=PRO_0000110694. FT REGION 34 35 Orotate binding (By similarity). FT REGION 72 73 5-phosphoribose 1-diphosphate binding. 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. FT BINDING 100 100 5-phosphoribose 1-diphosphate. FT BINDING 103 103 5-phosphoribose 1-diphosphate; shared FT with dimeric partner. 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). FT CONFLICT 133 133 Missing (in Ref. 1 and 2). FT HELIX 3 14 FT STRAND 17 24 FT STRAND 30 35 FT HELIX 37 39 FT HELIX 43 60 FT STRAND 65 69 FT TURN 71 73 FT HELIX 74 89 FT STRAND 94 98 FT STRAND 104 107 FT STRAND 111 114 FT STRAND 118 123 FT HELIX 130 133 FT HELIX 134 142 FT STRAND 146 155 FT STRAND 161 164 FT HELIX 166 174 FT STRAND 177 183 FT HELIX 184 191 FT HELIX 195 197 FT HELIX 198 211 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 //