(data stored in ACNUC7421 zone)

SWISSPROT: PYRE_SINFN

ID   PYRE_SINFN              Reviewed;         232 AA.
AC   C3MF81;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
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=NGR_c01150;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP23918.1; -; Genomic_DNA.
DR   RefSeq; WP_012706703.1; NC_012587.1.
DR   RefSeq; YP_002824671.1; NC_012587.1.
DR   ProteinModelPortal; C3MF81; -.
DR   SMR; C3MF81; -.
DR   STRING; 394.NGR_c01150; -.
DR   EnsemblBacteria; ACP23918; ACP23918; NGR_c01150.
DR   GeneID; 7790694; -.
DR   KEGG; rhi:NGR_c01150; -.
DR   PATRIC; fig|394.7.peg.2913; -.
DR   eggNOG; ENOG4107SW0; Bacteria.
DR   eggNOG; COG0461; LUCA.
DR   HOGENOM; HOG000037975; -.
DR   KO; K00762; -.
DR   OMA; HAAWVSE; -.
DR   OrthoDB; POG091H034Q; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000001054; 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.
PE   3: Inferred from homology;
DR   PRODOM; C3MF81.
DR   SWISS-2DPAGE; C3MF81.
KW   Complete proteome; Glycosyltransferase; Magnesium;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    232       Orotate phosphoribosyltransferase.
FT                                /FTId=PRO_1000164689.
FT   REGION      133    141       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01208}.
FT   BINDING     107    107       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     108    108       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01208}.
FT   BINDING     111    111       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     113    113       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     137    137       Orotate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01208}.
SQ   SEQUENCE   232 AA;  25418 MW;  494B083CAC39E687 CRC64;
     MFSNAFTDKT VMAELVAKML WEIKAVHFRA DEPYKLSSGM ASPVYIDCRK LISYPRIRSA
     VMDFAAATIL RDAGFEQFDV VAGGETAGIP FAAMLAERLG LPMIYVRKAP KGHGRNAQIE
     GHMPEGARVL VIEDLTTAGG SMFKFIDAIR AAGGIVEHGI ALFYYDIFPE ARGNMKSKGV
     DLHYIATWRN VLAVAREQAL FDEKTLNEVE AFLNAPLAWS ERNGGVGTLA AQ
//

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