ID   PYRF_HYPAT              Reviewed;         379 AA.
AC   Q12709;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=pyr4;
OS   Hypocrea atroviridis (Trichoderma atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=63577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 36042 / 2440A / CBS 391.92;
RX   PubMed=8088543; DOI=10.1016/0378-1119(94)90057-4;
RA   Heidenreich E.J., Kubicek C.P.;
RT   "Sequence of the pyr4 gene encoding orotidine-5'-phosphate decarboxylase
RT   from the biocontrol fungus Trichoderma harzianum.";
RL   Gene 147:151-152(1994).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U05192; AAA51865.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12709; -.
DR   SMR; Q12709; -.
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; -; 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   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT   CHAIN           1..379
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134687"
FT   REGION          165..198
FT                   /note="Disordered"
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         331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  41259 MW;  33B6C02043BD1E38 CRC64;
     MASHPTLKTT FAARSEATTH PLTSYLLRLM DLKASNLCLS ADVPTARELL YLADKIGPSI
     VVLKTHYDMV SGWDFHPDTG TGAKLASLAR KHGFLIFEDR KFGDIGHTVE LQYTSGSARI
     IDWAHIVNVN MVPGKASVAS LAQGARRWLE RYPCEVKTSV TVGTPTMDQF DDAEDAKDDE
     PATVNDNGSN MMEKPIYAGR NGDGRKGSIV SITTVTQQYE SAASPRLGKT IAEGDESLFP
     GIEEAPLNRG LLILAQMSSE GNFMTGEYTQ ACVEAAREHK DFVMGFISQE ALNTQADDDF
     IHMTPGCQLP PEDEDQQTNG KVGGDGQGQQ YNTAHKIIGI AGSDIAIVGR GILKASDPVE
     EAERYRSAAW KAYTERLLR