(data stored in SCRATCH zone)

SWISSPROT: PYRE_PSEU2

ID   PYRE_PSEU2              Reviewed;         213 AA.
AC   Q4ZZY3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   11-DEC-2019, entry version 100.
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=Psyr_0216;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35289.1; -; Genomic_DNA.
DR   RefSeq; WP_003403990.1; NC_007005.1.
DR   RefSeq; YP_233327.1; NC_007005.1.
DR   SMR; Q4ZZY3; -.
DR   STRING; 205918.Psyr_0216; -.
DR   EnsemblBacteria; AAY35289; AAY35289; Psyr_0216.
DR   GeneID; 3365692; -.
DR   KEGG; psb:Psyr_0216; -.
DR   PATRIC; fig|205918.7.peg.213; -.
DR   eggNOG; ENOG4107QP2; Bacteria.
DR   eggNOG; COG0461; LUCA.
DR   HOGENOM; HOG000037974; -.
DR   KO; K00762; -.
DR   OMA; MKAYQRQ; -.
DR   BioCyc; PSYR205918:G1G4J-217-MONOMER; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000000426; 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; Q4ZZY3.
DR   SWISS-2DPAGE; Q4ZZY3.
KW   Glycosyltransferase; Magnesium; Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..213
FT                   /note="Orotate phosphoribosyltransferase"
FT                   /id="PRO_1000066278"
FT   REGION          34..35
FT                   /note="Orotate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   REGION          72..73
FT                   /note="5-phosphoribose 1-diphosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   REGION          124..132
FT                   /note="5-phosphoribose 1-diphosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         26
FT                   /note="5-phosphoribose 1-diphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         99
FT                   /note="5-phosphoribose 1-diphosphate; shared with dimeric
FT                   partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         100
FT                   /note="5-phosphoribose 1-diphosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         103
FT                   /note="5-phosphoribose 1-diphosphate; shared with dimeric
FT                   partner"
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         128
FT                   /note="Orotate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT   BINDING         156
FT                   /note="Orotate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
SQ   SEQUENCE   213 AA;  23037 MW;  7DEAF71F434ABFFA CRC64;
     MQAYQRDFIR FAIDRGVLRF GEFTLKSGRT SPYFFNAGLF NTGSALAQLG RFYAAAVVES
     GIAFDVLFGP AYKGIPLASA TAVALAEHHD RDLPWCFNRK EAKAHGEGGS LVGSPLAGNV
     LIIDDVITAG TAIREVMQII KDQDATAAGV LIALNRQERG NGELSAIQEV ERDFGIPVVS
     IVSLNQVLEF LADDPQLKQH LPAVEAYRAQ FGI
//

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