(data stored in ACNUC7421 zone)

SWISSPROT: PYRE_POLNA

ID   PYRE_POLNA              Reviewed;         237 AA.
AC   A1VIL5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   11-DEC-2019, entry version 75.
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=Pnap_0168;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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; CP000529; ABM35493.1; -; Genomic_DNA.
DR   SMR; A1VIL5; -.
DR   STRING; 365044.Pnap_0168; -.
DR   EnsemblBacteria; ABM35493; ABM35493; Pnap_0168.
DR   KEGG; pna:Pnap_0168; -.
DR   eggNOG; ENOG4107QP2; Bacteria.
DR   eggNOG; COG0461; LUCA.
DR   HOGENOM; HOG000037974; -.
DR   KO; K00762; -.
DR   OMA; MKAYQRQ; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000000644; 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   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 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; A1VIL5.
DR   SWISS-2DPAGE; A1VIL5.
KW   Glycosyltransferase; Magnesium; Pyrimidine biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..237
FT                   /note="Orotate phosphoribosyltransferase"
FT                   /id="PRO_1000066266"
FT   REGION          37..38
FT                   /note="Orotate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   REGION          79..80
FT                   /note="5-phosphoribose 1-diphosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   REGION          130..138
FT                   /note="5-phosphoribose 1-diphosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         29
FT                   /note="5-phosphoribose 1-diphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         105
FT                   /note="5-phosphoribose 1-diphosphate; shared with dimeric
FT                   partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         106
FT                   /note="5-phosphoribose 1-diphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         109
FT                   /note="5-phosphoribose 1-diphosphate; shared with dimeric
FT                   partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         111
FT                   /note="5-phosphoribose 1-diphosphate; shared with dimeric
FT                   partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         134
FT                   /note="Orotate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         162
FT                   /note="Orotate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
SQ   SEQUENCE   237 AA;  25654 MW;  1B359D8C1592DA9F CRC64;
     MPAEGSLAQE FVQFAVESGV LRFGQFKTKA GRMSPYFFNA GLFDDGAKLG RLAQFYARQL
     LAEEQRSGLA FDMIFGPAYK GIPLAAAVAI ELARLGRNLP FAYNRKEAKD HGEGGTLVGA
     KLQGRVLIVD DVMSAGTAVR ESIALIQAAG ATPHAVAIAL DRQEKATENG LDVEHSAVQY
     VTRQLGLQVC AIARLSDLLQ YLSEKSDSPS GGETLDGQRL KDHYQSVLAY RERYGVN
//

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