PYRE_THET2
ID PYRE_THET2 Reviewed; 183 AA.
AC P61498; O08047; O08276; Q60016;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=TT_C1380;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8787418; DOI=10.1128/aem.62.6.2191-2194.1996;
RA Yamagishi A., Tanimoto T., Suzuki T., Oshima T.;
RT "Pyrimidine biosynthesis genes (pyrE and pyrF) of an extreme thermophile,
RT Thermus thermophilus.";
RL Appl. Environ. Microbiol. 62:2191-2194(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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 ECO:0000269|PubMed:8787418}.
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, ECO:0000269|PubMed:8787418};
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; D83330; BAA11886.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS81722.1; -; Genomic_DNA.
DR RefSeq; WP_011173763.1; NC_005835.1.
DR AlphaFoldDB; P61498; -.
DR SMR; P61498; -.
DR STRING; 262724.TT_C1380; -.
DR EnsemblBacteria; AAS81722; AAS81722; TT_C1380.
DR KEGG; tth:TT_C1380; -.
DR eggNOG; COG0461; Bacteria.
DR HOGENOM; CLU_074878_3_0_0; -.
DR OMA; YFQCAKV; -.
DR OrthoDB; 1280396at2; -.
DR UniPathway; UPA00070; UER00119.
DR Proteomes; UP000000592; 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:0019856; P:pyrimidine nucleobase biosynthetic 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; IPR006273; Orotate_PRibTrfase_bac.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01367; pyrE_Therm; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Magnesium; Pyrimidine biosynthesis; Transferase.
FT CHAIN 1..183
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000110760"
FT BINDING 21
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 88
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 112..120
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 116
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
FT BINDING 144
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208"
SQ SEQUENCE 183 AA; 19442 MW; DDD3BB0235AEB9ED CRC64;
MDVLELYRRT GALLEGHFLL RSGMHSPFFL QSAALLQHPL YAEAVGEALG KLFEDEKVDF
VIAPAIGGVV LSFVVAKALG ARALFAEKDG RGGMLIRKGL TVNPGDRFLA VEDVVTTGES
VRKAIRAAEA RGGVLVGVGA IVDRSGGRAA FGVPFRALLA LEVPQYPEEA CPLCREGVPL
EEV
