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Database: UniProt
Entry: H6Q7N9_PYROT
LinkDB: H6Q7N9_PYROT
Original site: H6Q7N9_PYROT 
ID   H6Q7N9_PYROT            Unreviewed;       192 AA.
AC   H6Q7N9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Orotate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011971, ECO:0000256|HAMAP-Rule:MF_01208};
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|ARBA:ARBA00011971, ECO:0000256|HAMAP-Rule:MF_01208};
GN   Name=pyrE {ECO:0000256|HAMAP-Rule:MF_01208};
GN   OrderedLocusNames=Pogu_0442 {ECO:0000313|EMBL:AFA38469.1};
OS   Pyrobaculum oguniense (strain DSM 13380 / JCM 10595 / TE7).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=698757 {ECO:0000313|EMBL:AFA38469.1, ECO:0000313|Proteomes:UP000009062};
RN   [1] {ECO:0000313|EMBL:AFA38469.1, ECO:0000313|Proteomes:UP000009062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13380 / JCM 10595 / TE7
RC   {ECO:0000313|Proteomes:UP000009062};
RX   PubMed=23407329; DOI=10.4056/sigs.2645906;
RA   Bernick D.L., Karplus K., Lui L.M., Coker J.K., Murphy J.N., Chan P.P.,
RA   Cozen A.E., Lowe T.M.;
RT   "Complete genome sequence of Pyrobaculum oguniense.";
RL   Stand. Genomic Sci. 6:336-345(2012).
RN   [2] {ECO:0000313|Proteomes:UP000009062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13380 / JCM 10595 / TE7
RC   {ECO:0000313|Proteomes:UP000009062};
RA   Bernick D.L., Karplus K., Lui L.M., Coker J.K.C., Murphy J.N., Cozen A.E.,
RA   Chan P.P., Lowe T.M.;
RT   "Complete genome sequence of Pyrobaculum oguniense.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01208};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01208};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 1/2. {ECO:0000256|ARBA:ARBA00004889,
CC       ECO:0000256|HAMAP-Rule:MF_01208}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01208}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrE subfamily. {ECO:0000256|HAMAP-Rule:MF_01208}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01208}.
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DR   EMBL; CP003316; AFA38469.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6Q7N9; -.
DR   STRING; 698757.Pogu_0442; -.
DR   KEGG; pog:Pogu_0442; -.
DR   eggNOG; arCOG00029; Archaea.
DR   HOGENOM; CLU_074878_2_0_2; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000009062; 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   NCBIfam; TIGR00336; pyrE; 1.
DR   PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01208,
KW   ECO:0000313|EMBL:AFA38469.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01208};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01208};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01208, ECO:0000313|EMBL:AFA38469.1}.
FT   DOMAIN          53..146
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   BINDING         85
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:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         89
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:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         91
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:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         111..119
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:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         115
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         143
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ   SEQUENCE   192 AA;  20805 MW;  9886B4F82ADC6612 CRC64;
     MIQRLLEVGV VKFGDFVLSS GLKSPFYIDL RAVLGHPDLF QWVVSQYLST LSKLEYDVIL
     GVATGGIPYA SVLGYLLQRP FGYVRPEAKG HGVGRQIEGA EVAGKRAVVV DDVLTTGKSV
     LGAISAVGEA GGRVTAVVVF LDREQCGAEA VRRAGAGVYS VYKMRELLEA LRPHIGEGQY
     RSAVEYLSQW RC
//
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