ID PYRE_RHOS1 Reviewed; 232 AA.
AC A3PH80;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 01-MAY-2013, entry version 45.
DE RecName: Full=Orotate phosphoribosyltransferase;
DE Short=OPRT;
DE Short=OPRTase;
DE EC=2.4.2.10;
GN Name=pyrE; OrderedLocusNames=Rsph17029_0580;
OS Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=349101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17029 / ATH 2.4.9;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Richardson P., Mackenzie C., Choudhary M.,
RA Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC
RT 17029.";
RL Submitted (FEB-2007) 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) (By similarity).
CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate
CC + 5-phospho-alpha-D-ribose 1-diphosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; UMP from orotate: step 1/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. PyrE subfamily.
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DR EMBL; CP000577; ABN75696.1; -; Genomic_DNA.
DR RefSeq; YP_001042468.1; NC_009049.1.
DR ProteinModelPortal; A3PH80; -.
DR STRING; 349101.Rsph17029_0580; -.
DR EnsemblBacteria; ABN75696; ABN75696; Rsph17029_0580.
DR GeneID; 4895354; -.
DR KEGG; rsh:Rsph17029_0580; -.
DR PATRIC; 23168807; VBIRhoSph114483_0720.
DR eggNOG; COG0461; -.
DR HOGENOM; HOG000037975; -.
DR KO; K00762; -.
DR OMA; RNARIEG; -.
DR ProtClustDB; PRK00455; -.
DR BioCyc; RSPH349101:GHC8-1724-MONOMER; -.
DR UniPathway; UPA00070; UER00119.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01208; PyrE; 1; -.
DR InterPro; IPR023031; OPRT.
DR InterPro; IPR000836; PRibTrfase_dom.
DR Pfam; PF00156; Pribosyltran; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Glycosyltransferase; Magnesium;
KW Pyrimidine biosynthesis; Transferase.
FT CHAIN 1 232 Orotate phosphoribosyltransferase.
FT /FTId=PRO_1000066286.
FT REGION 133 141 5-phosphoribose 1-diphosphate binding (By
FT similarity).
FT BINDING 107 107 5-phosphoribose 1-diphosphate; shared
FT with dimeric partner (By similarity).
FT BINDING 108 108 5-phosphoribose 1-diphosphate (By
FT similarity).
FT BINDING 111 111 5-phosphoribose 1-diphosphate; shared
FT with dimeric partner (By similarity).
FT BINDING 137 137 Orotate (By similarity).
SQ SEQUENCE 232 AA; 25574 MW; 8511D572D9AC277A CRC64;
MIPTSFPPRE EIARLTARML LEIEAVHFRP QEPFTLASGL PSPTYIDCRK LISYPRIRST
LMDFMAVTLL RDAGFEAFDN IAGGETAGIP FAALVAERLG LPMTYVRKKP KGYGRNARIE
GVMTEGQRVL LVEDLTTDGG SKLSFVDAIR ETGASCAHTA VIFYYGIFPE TIGRLQAHGV
TLHHLCTWWD VLAEARASGA FDAGTLAEVE SFLSNPRDWQ DARKPADPTK SL
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