PYRE_ENTFO
ID PYRE_ENTFO Reviewed; 210 AA.
AC F2MMN7; O07657;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 53.
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=OG1RF_11423;
OS Enterococcus faecalis (strain ATCC 47077 / OG1RF).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=474186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47077 / OG1RF;
RX PubMed=18611278; DOI=10.1186/gb-2008-9-7-r110;
RA Bourgogne A., Garsin D.A., Qin X., Singh K.V., Sillanpaa J.,
RA Yerrapragada S., Ding Y., Dugan-Rocha S., Buhay C., Shen H., Chen G.,
RA Williams G., Muzny D., Maadani A., Fox K.A., Gioia J., Chen L., Shang Y.,
RA Arias C.A., Nallapareddy S.R., Zhao M., Prakash V.P., Chowdhury S.,
RA Jiang H., Gibbs R.A., Murray B.E., Highlander S.K., Weinstock G.M.;
RT "Large scale variation in Enterococcus faecalis illustrated by the genome
RT analysis of strain OG1RF.";
RL Genome Biol. 9:R110.1-R110.16(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-138.
RC STRAIN=ATCC 47077 / OG1RF;
RX PubMed=7592480; DOI=10.1128/jb.177.23.6866-6873.1995;
RA Li X., Weinstock G.M., Murray B.E.;
RT "Generation of auxotrophic mutants of Enterococcus faecalis.";
RL J. Bacteriol. 177:6866-6873(1995).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEA94110.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP002621; AEA94110.1; ALT_INIT; Genomic_DNA.
DR EMBL; U24682; AAB61216.1; -; Genomic_DNA.
DR RefSeq; WP_002357418.1; NZ_CP025020.1.
DR AlphaFoldDB; F2MMN7; -.
DR SMR; F2MMN7; -.
DR GeneID; 60894008; -.
DR KEGG; efi:OG1RF_11423; -.
DR HOGENOM; CLU_074878_1_1_9; -.
DR UniPathway; UPA00070; UER00119.
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..210
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000412179"
FT BINDING 97
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 101
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 103
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 123..131
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 127
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
SQ SEQUENCE 210 AA; 22869 MW; 8269D5C8C27D633A CRC64;
MTKVAKKIAK DLLDIEAVFL NPNEPFTWAS GIKSPIYCDN RITMSYPAVR KEIAEGLAAK
IKETFPEVEV IAGTATAGIP HAAWVADILG LPMVYIRSKA KDHGKGNQIE GRISEGQKMV
VIEDLISTGG SVLEAAEAAE REGATVLGVA AIFTYELPKG TANFADKQMT LLTLTNYSTL
IDAALEANYI EEKDVTLLQE WKKDPENWGK
