PYRF_ASPOR
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 03-AUG-2022, entry version 117.
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; KNFVMGF; -.
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 Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01740; pyrF; 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