ID   PYRF_ASPNG              Reviewed;         277 AA.
AC   P07817; Q9HGS5;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   27-MAR-2024, entry version 109.
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; Synonyms=pyrA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=L112;
RX   PubMed=3357784; DOI=10.1093/nar/16.5.2339;
RA   Wilson L.J., Ward M., Carmona C.;
RT   "Sequence of the Aspergillus niger pyrG gene.";
RL   Nucleic Acids Res. 16:2339-2339(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RA   van den Hombergh J.P.T.W., de Vries R.P., de Zwart P.J.I.,
RA   van de Vondervoort L.H., de Graaff L.H., Visser J.;
RT   "The pyrA gene from Aspergillus niger: characterization of gene and
RT   mutants; targeting to homologous locus and use of disruption strains in
RT   locus-specific integration.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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; X06626; CAA29838.1; -; Genomic_DNA.
DR   EMBL; X96734; CAA65508.2; -; Genomic_DNA.
DR   PIR; S03652; DCASON.
DR   AlphaFoldDB; P07817; -.
DR   SMR; P07817; -.
DR   BindingDB; P07817; -.
DR   PaxDb; 5061-CADANGAP00009614; -.
DR   VEuPathDB; FungiDB:An12g03570; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1103304; -.
DR   VEuPathDB; FungiDB:ATCC64974_38430; -.
DR   VEuPathDB; FungiDB:M747DRAFT_241590; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   UniPathway; UPA00070; UER00120.
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:InterPro.
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.
FT   CHAIN           1..277
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134643"
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         73
FT                   /note="D -> N (in strain: CBS 120.49 / N400)"
FT   VARIANT         109
FT                   /note="R -> G (in strain: CBS 120.49 / N400)"
FT   VARIANT         145
FT                   /note="S -> A (in strain: CBS 120.49 / N400)"
FT   VARIANT         192
FT                   /note="S -> A (in strain: CBS 120.49 / N400)"
FT   VARIANT         233
FT                   /note="A -> G (in strain: CBS 120.49 / N400)"
SQ   SEQUENCE   277 AA;  30196 MW;  02F30DAF5D9DA808 CRC64;
     MSSKSQLTYT ARASKHPNAL AKRLFEIAEA KKTNVTVSAD VTTTKELLDL ADRLGPYIAV
     IKTHIDILSD FSDETIEGLK ALAQKHNFLI FEDRKFIDIG NTVQKQYHRG TLRISEWAHI
     INCSILPGEG IVEALAQTAS APDFSYGPER GLLILAEMTS KGSLATGQYT TSSVDYARKY
     KNFVMGFVST RSLGEVQSEV SSPSDEEDFV VFTTGVNISS KGDKLGQQYQ TPASAIGRGA
     DFIIAGRGIY AAPDPVQAAQ QYQKEGWEAY LARVGGN
//