ID   PYRF_HYPJE              Reviewed;         381 AA.
AC   P21594;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 92.
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;
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX   PubMed=2263502; DOI=10.1093/nar/18.23.7183;
RA   Berges T., Perrot M., Barreau C.;
RT   "Nucleotide sequences of the Trichoderma reesei ura3 (OMPdecase) and ura5
RT   (OPRTase) genes.";
RL   Nucleic Acids Res. 18:7183-7183(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX   PubMed=1913875; DOI=10.1007/bf00309596;
RA   Berges T., Barreau C.;
RT   "Isolation of uridine auxotrophs from Trichoderma reesei and efficient
RT   transformation with the cloned ura3 and ura5 genes.";
RL   Curr. Genet. 19:359-365(1991).
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; X55880; CAA39365.1; -; Genomic_DNA.
DR   PIR; S14132; S14132.
DR   AlphaFoldDB; P21594; -.
DR   SMR; P21594; -.
DR   PRIDE; P21594; -.
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   Gene3D; 3.20.20.70; -; 2.
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   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT   CHAIN           1..381
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134688"
FT   REGION          311..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         99..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  41176 MW;  C57FE146442983B9 CRC64;
     MAPHPTLKAT FAARSETATH PLTAYLFKLM DLKASNLCLS ADVPTARELL YLADKIGPSI
     VVLKTHYDMV SGWTSHPETG TGAQLASLAR KHGFLIFEDR KFGDIGHTVE LQYTGGSARI
     IDWAHIVNVN MVPGKASVAS LAQGAKRWLE RYPCEVKTSV TVGTPTMDSF DDDADSRDAE
     PAGAVNGMGS IGVLDKPIYS NRSGDGRKGS IVSITTVTQQ YESVSSPRLT KAIAEGDESL
     FPGIEEAPLS RGLLILAQMS SQGNFMNKEY TQASVEAARE HKDFVMGFIS QETLNTEPDD
     AFIHMTPGCQ LPPEDEDQQT NGSVGGDGQG QQYNTPHKLI GIAGSDIAIV GRGILKASDP
     VEEAERYRSA AWKAYTERLL R