(data stored in SCRATCH zone)

SWISSPROT: E6V1E6_VARPE

ID   E6V1E6_VARPE            Unreviewed;       227 AA.
AC   E6V1E6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 57.
DE   RecName: Full=Orotate phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS00615437};
DE            Short=OPRT {ECO:0000256|HAMAP-Rule:MF_01208};
DE            Short=OPRTase {ECO:0000256|HAMAP-Rule:MF_01208};
DE            EC=2.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS00345661};
GN   Name=pyrE {ECO:0000256|HAMAP-Rule:MF_01208};
GN   OrderedLocusNames=Varpa_0288 {ECO:0000313|EMBL:ADU34510.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34510.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34510.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34510.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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:0000256|HAMAP-
CC       Rule:MF_01208, ECO:0000256|SAAS:SAAS01081938}.
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:0000256|HAMAP-
CC         Rule:MF_01208, ECO:0000256|SAAS:SAAS01118317};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01208};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from orotate: step 1/2. {ECO:0000256|HAMAP-
CC       Rule:MF_01208, ECO:0000256|SAAS:SAAS00015801}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01208,
CC       ECO:0000256|SAAS:SAAS00216311}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. PyrE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000256|SAAS:SAAS00541116}.
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DR   EMBL; CP002417; ADU34510.1; -; Genomic_DNA.
DR   RefSeq; WP_013538756.1; NC_014931.1.
DR   STRING; 595537.Varpa_0288; -.
DR   EnsemblBacteria; ADU34510; ADU34510; Varpa_0288.
DR   GeneID; 29715293; -.
DR   KEGG; vpe:Varpa_0288; -.
DR   eggNOG; ENOG4107QP2; Bacteria.
DR   eggNOG; COG0461; LUCA.
DR   HOGENOM; HOG000037974; -.
DR   KO; K00762; -.
DR   OMA; MKAYQRQ; -.
DR   OrthoDB; 1280396at2; -.
DR   BioCyc; VPAR595537:G1GQO-290-MONOMER; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000008917; 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   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; E6V1E6.
DR   SWISS-2DPAGE; E6V1E6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00423761, ECO:0000313|EMBL:ADU34510.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01208};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00423725};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000256|SAAS:SAAS00423769, ECO:0000313|EMBL:ADU34510.1}.
FT   DOMAIN       47    167       Pribosyltran. {ECO:0000259|Pfam:PF00156}.
FT   REGION       41     42       Orotate binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01208}.
FT   REGION       79     80       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   REGION      130    138       5-phosphoribose 1-diphosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   BINDING      33     33       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   BINDING     105    105       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     106    106       5-phosphoribose 1-diphosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   BINDING     109    109       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     111    111       5-phosphoribose 1-diphosphate; shared
FT                                with dimeric partner. {ECO:0000256|HAMAP-
FT                                Rule:MF_01208}.
FT   BINDING     134    134       Orotate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01208}.
FT   BINDING     162    162       Orotate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01208}.
SQ   SEQUENCE   227 AA;  24196 MW;  949942DCB8F540EA CRC64;
     MAVDGEKSSA VAQDFVQFAR DAGVLRFGEF KTKAGRMSPY FFNSGLFDDG AKIARLAGFY
     ADRLIESGLE FDMIFGPAYK GIPLGATVAA ELARRGRNYP FAYNRKEAKA HGEGGNLVGA
     PLQGRVLIVD DVMSAGTAVR ESIAAIQAAG ATPHAVAIAL DRQEKATENG VDVDHSAVQY
     VRNQLGLSVI AIATLDDLLS YLSGDAAADL GAHRERVLAY RTRYGAH
//

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