ID   PYRF_ASPOR              Reviewed;         277 AA.
AC   O13416; O74652; Q2TZF8;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE            EC=4.1.1.23;
DE   AltName: Full=OMP decarboxylase;
DE            Short=OMPDCase;
DE            Short=OMPdecase;
DE   AltName: Full=Uridine 5'-monophosphate synthase;
DE            Short=UMP synthase;
GN   Name=pyrG; ORFNames=AO090011000868;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TK3;
RA   Doumas A., Vandenbroek P.J.M., Affolter M., Monod M.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KBN616;
RA   Kitamoto N., Yoshino S.;
RT   "Nucleotide sequence of the pyrG gene from a shoyu koji mold, Aspergillus
RT   oryzae KBN616.";
RL   Nihon Shoyu Kenkyujo Zasshi 25:21-26(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
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.R., 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC         Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10110};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. {ECO:0000305}.
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DR   EMBL; Y13811; CAA74139.1; -; Genomic_DNA.
DR   EMBL; AB017705; BAA33760.1; -; Genomic_DNA.
DR   EMBL; AP007171; BAE65307.1; -; Genomic_DNA.
DR   RefSeq; XP_001826440.1; XM_001826388.2.
DR   AlphaFoldDB; O13416; -.
DR   SMR; O13416; -.
DR   STRING; 510516.O13416; -.
DR   EnsemblFungi; BAE65307; BAE65307; AO090011000868.
DR   GeneID; 5998543; -.
DR   KEGG; aor:AO090011000868; -.
DR   VEuPathDB; FungiDB:AO090011000868; -.
DR   HOGENOM; CLU_030821_0_0_1; -.
DR   OMA; CLIKTHI; -.
DR   OrthoDB; 922at2759; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000006564; Chromosome 7.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04725; OMP_decarboxylase_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR01740; pyrF; 1.
DR   PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..277
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134644"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   VARIANT         260
FT                   /note="K -> N (in strain: KBN616)"
SQ   SEQUENCE   277 AA;  30282 MW;  C6F2EE037B112977 CRC64;
     MSSKSQLTYS ARASKHPNAL VKKLFEVAEA KKTNVTVSAD VTTTKELLDL ADRLGPYIAV
     IKTHIDILSD FSEETITGLK ALAEKHNFLI FEDRKFIDIG NTVQKQYHGG TLRISEWAHI
     INCSILPGEG IVEALAQTAS AEDFPYGSER GLLILAEMTS KGSLATGQYT TSSVDYARKY
     KKFVMGFVST RHLGEVQSEV SSPSEEEDFV VFTTGVNLSS KGDKLGQQYQ TPESAVGRGA
     DFIIAGRGIY AAPDPVEAAK QYQKEGWDAY LKRVGAQ
//