(data stored in ACNUC7421 zone)

SWISSPROT: PYRE_EDWI9

ID   PYRE_EDWI9              Reviewed;         213 AA.
AC   C5B9D0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 52.
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};
GN   OrderedLocusNames=NT01EI_0050;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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). {ECO:0000255|HAMAP-
CC       Rule:MF_01208}.
CC   -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate
CC       + 5-phospho-alpha-D-ribose 1-diphosphate. {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
CC       pathway; UMP from orotate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_01208}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. PyrE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01208}.
DR   EMBL; CP001600; ACR67310.1; -; Genomic_DNA.
DR   RefSeq; WP_015869534.1; NC_012779.2.
DR   ProteinModelPortal; C5B9D0; -.
DR   SMR; C5B9D0; -.
DR   STRING; 634503.NT01EI_0050; -.
DR   EnsemblBacteria; ACR67310; ACR67310; NT01EI_0050.
DR   GeneID; 7959769; -.
DR   KEGG; eic:NT01EI_0050; -.
DR   PATRIC; fig|634503.3.peg.43; -.
DR   eggNOG; ENOG4107QP2; Bacteria.
DR   eggNOG; COG0461; LUCA.
DR   HOGENOM; HOG000037974; -.
DR   KO; K00762; -.
DR   OMA; MKAYQRQ; -.
DR   OrthoDB; POG091H034Q; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   HAMAP; MF_01208; PyrE; 1.
DR   InterPro; IPR023031; OPRT.
DR   InterPro; IPR004467; Or_phspho_trans_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR00336; pyrE; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B9D0.
DR   SWISS-2DPAGE; C5B9D0.
KW   Complete proteome; Glycosyltransferase; Magnesium;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    213       Orotate phosphoribosyltransferase.
FT                                /FTId=PRO_1000213859.
FT   REGION       34     35       Orotate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   REGION       72     73       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01208}.
FT   REGION      124    132       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01208}.
FT   BINDING      26     26       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01208}.
FT   BINDING      99     99       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     100    100       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01208}.
FT   BINDING     103    103       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     105    105       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     128    128       Orotate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     156    156       Orotate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
SQ   SEQUENCE   213 AA;  23323 MW;  223AACAE0B2FF9AA CRC64;
     MKAYQRRFIE FALGKQVLKF GEFTLKSGRT SPYFFNAGLF NTGRDLALLG RFYAEALVES
     GIAFDVLFGP AYKGIPIATT TAVALAEHHD RDMPYCFNRK EAKDHGEGGT LVGSALAGRV
     MLVDDVITAG TAIRESMSII QANGAALAGV LISLDRQERG RGELSAIQEV ERDYGCRVIS
     IITLGDLIHY LEEQPEMAQH LAAVKAYRAR YGV
//

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