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Database: UniProt
Entry: A0A101XK91_9CREN
LinkDB: A0A101XK91_9CREN
Original site: A0A101XK91_9CREN 
ID   A0A101XK91_9CREN        Unreviewed;       175 AA.
AC   A0A101XK91;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ORFNames=AT710_01495 {ECO:0000313|EMBL:KUO92984.1};
OS   Thermocladium sp. ECH_B.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermocladium.
OX   NCBI_TaxID=1714261 {ECO:0000313|EMBL:KUO92984.1, ECO:0000313|Proteomes:UP000054381};
RN   [1] {ECO:0000313|EMBL:KUO92984.1, ECO:0000313|Proteomes:UP000054381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA   Inskeep W.P.;
RT   "The distribution, diversity and function of predominant Thermoproteales in
RT   high-temperature environments of Yellowstone National Park.";
RL   Submitted (DEC-2015) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUO92984.1}.
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DR   EMBL; LOBW01000006; KUO92984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101XK91; -.
DR   STRING; 1714261.AT710_01495; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000054381; Unassembled WGS sequence.
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   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}; Transferase {ECO:0000256|HAMAP-Rule:MF_01208}.
FT   DOMAIN          42..149
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   BINDING         88
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                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         92
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         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:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         114..122
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         118
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
FT   BINDING         146
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01208"
SQ   SEQUENCE   175 AA;  19497 MW;  DF781A50AA036F78 CRC64;
     MNRKELMKLL KEYGVIQFGK FKLSSGKESD YYIDMRRALS VPVIYREIIE AMTQLVSDVD
     LVAGIESGGV PWAAMLAYRL GMGMIYVRKQ PKEHGTSRSV EGIYSSNQRV LVIDDVMTTG
     SSIMRGIELI QAAGLRVIQA MVIVDRSGGS VNLKVPLHYV LRAEEILNEL NGTNK
//
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