ID   PYRF_SORMK              Reviewed;         396 AA.
AC   P78748; D1ZSM5; F7W814;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   03-MAY-2023, entry version 104.
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=URA3; ORFNames=SMAC_07225;
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RA   Nowrousian M., Kueck U.;
RT   "Isolation and cloning of the Sordaria macrospora ura3 gene and its
RT   heterologous expression in Aspergillus niger.";
RL   Fungal Genet. Newsl. 45:34-37(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA   Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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; Z70291; CAA94305.1; -; Genomic_DNA.
DR   EMBL; CABT02000042; CCC13658.1; -; Genomic_DNA.
DR   RefSeq; XP_003344657.1; XM_003344609.1.
DR   AlphaFoldDB; P78748; -.
DR   SMR; P78748; -.
DR   STRING; 771870.P78748; -.
DR   GeneID; 10801959; -.
DR   KEGG; smp:SMAC_07225; -.
DR   VEuPathDB; FungiDB:SMAC_07225; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   HOGENOM; CLU_030821_1_1_1; -.
DR   InParanoid; P78748; -.
DR   OMA; CLIKTHI; -.
DR   OrthoDB; 922at2759; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
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   PANTHER; PTHR32119; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR32119:SF2; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 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..396
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134685"
FT   ACT_SITE        105
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         68..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         103..112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        45
FT                   /note="A -> D (in Ref. 1; CAA94305)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  43764 MW;  0AF26D344BBC7888 CRC64;
     MSTTQQPHWS LQKSFAERVE SSSHPLTSYL FRLMEVKQSN LCLSADVEHA RELLALADKI
     GPSIVVLKTH YDLITGWDYH PHTGTGAKLA ALARKHGFLI FEDRKFVDIG STVQKQYTAG
     TARIVEWAHI TNADIHAGEA MVSAMAQAAQ KWRERIPYEV KTSVSVGTPV ADQFADEEAE
     DQVDELRKIV PRENSTSKEK DTDGRKGSIV SITTVTQTYE PADSPRLAKT ISEGDEAVFP
     GIEEAPLDRG LLILAQMSSK GCLMDGKYTW ECVKAARKNK DFVMGYVAQQ NLNGITKEDL
     APGYEDGETS TEEEAQADNF IHMTPGCKLP PPGEEAPQGD GLGQQYNTPD NLVNIKGTDI
     AIVGRGIITA SDPPAEAERY RRKAWKAYQD RRERLA
//