PYRE_STAES
ID PYRE_STAES Reviewed; 203 AA.
AC Q8CSW7;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=SE_0881;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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}.
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DR EMBL; AE015929; AAO04478.1; -; Genomic_DNA.
DR RefSeq; NP_764436.1; NC_004461.1.
DR RefSeq; WP_001830179.1; NZ_WBME01000063.1.
DR AlphaFoldDB; Q8CSW7; -.
DR SMR; Q8CSW7; -.
DR STRING; 176280.SE_0881; -.
DR EnsemblBacteria; AAO04478; AAO04478; SE_0881.
DR GeneID; 50018981; -.
DR KEGG; sep:SE_0881; -.
DR PATRIC; fig|176280.10.peg.853; -.
DR eggNOG; COG0461; Bacteria.
DR HOGENOM; CLU_074878_1_1_9; -.
DR OMA; ENPFTWA; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000001411; 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 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;
KW Glycosyltransferase; Magnesium; Pyrimidine biosynthesis; Transferase.
FT CHAIN 1..203
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000110742"
FT BINDING 94
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 98
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 100
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 120..128
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 124
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
SQ SEQUENCE 203 AA; 22140 MW; 04DE28263151A4C7 CRC64;
MAKNIAKALL DIEAVSLSPN DLFTWSSGIK SPIYCDNRIT LGYPEVRNAI RDGLIQLIKE
HFSNVEIISG TATAGIPHAA YISEKLELPM NYVRSKSKSH GKQNQIEGAK SENKNVVVVE
DLISTGGSSI TAVEALEEAG ANVLGVVAIF TYGLAKADKT FNKAHIPFYT LSDYNELIEV
AKDEGKISLN DIQTLVDWRD NLS
