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Database: UniProt
Entry: Q2UEQ7_ASPOR
LinkDB: Q2UEQ7_ASPOR
Original site: Q2UEQ7_ASPOR 
ID   Q2UEQ7_ASPOR            Unreviewed;       249 AA.
AC   Q2UEQ7;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Orotate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00014769};
DE            EC=2.4.2.10 {ECO:0000256|ARBA:ARBA00011971};
GN   ORFNames=AO090026000521 {ECO:0000313|EMBL:BAE59958.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE59958.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE59958.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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|ARBA:ARBA00003769}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001431};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 1/2. {ECO:0000256|ARBA:ARBA00004889}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrE subfamily. {ECO:0000256|ARBA:ARBA00006340}.
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DR   EMBL; AP007159; BAE59958.1; -; Genomic_DNA.
DR   RefSeq; XP_001821960.1; XM_001821908.2.
DR   AlphaFoldDB; Q2UEQ7; -.
DR   STRING; 510516.Q2UEQ7; -.
DR   EnsemblFungi; BAE59958; BAE59958; AO090026000521.
DR   GeneID; 5993988; -.
DR   KEGG; aor:AO090026000521; -.
DR   VEuPathDB; FungiDB:AO090026000521; -.
DR   HOGENOM; CLU_074878_0_0_1; -.
DR   OMA; SPFFMNA; -.
DR   OrthoDB; 276022at2759; -.
DR   UniPathway; UPA00070; UER00119.
DR   Proteomes; UP000006564; Chromosome 3.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
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; PTHR46683; OROTATE PHOSPHORIBOSYLTRANSFERASE 1-RELATED; 1.
DR   PANTHER; PTHR46683:SF1; OROTATE PHOSPHORIBOSYLTRANSFERASE 1-RELATED; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT   DOMAIN          85..192
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   249 AA;  26541 MW;  4EFD666608D73ADB CRC64;
     MSAATIPAPA AEQDYKETLL PLLMKNNVLS FGSFILKSGR ESPYFFTSSL LHTAPLLRAT
     SAAYASVLSA PPFVTVAADG TTTPNFDIIF GPAYKGIPVC ASVLNELAVR DSLSASAKGT
     WDNVSYSFNR KEAKDHGEGG NIVGAPLKGK RVVIVDDVIT AGTAIREAVS IIQKEGGIVT
     GIVVLLDREE RVSDAEPKSA IGVAQRDLGE NIPIRAVIGL HDLIEKLGDK IGESEIQRLK
     DYRARYGAE
//
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