ID   PYRF_HAPCH              Reviewed;         376 AA.
AC   P14017;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-NOV-2023, entry version 97.
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   Hapsidospora chrysogena (Acremonium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Hapsidospora.
OX   NCBI_TaxID=5044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11550 / CBS 779.69 / DSM 880 / IMI 49137;
RX   PubMed=2587233; DOI=10.1093/nar/17.21.8874;
RA   Vian A., Penalva M.A.;
RT   "Nucleotide sequence of the Cephalosporium acremonium pyr4 gene.";
RL   Nucleic Acids Res. 17:8874-8874(1989).
RN   [2]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=2140299; DOI=10.1007/bf00312613;
RA   Vian A., Penalva M.A.;
RT   "Cloning of the pyr4 gene encoding orotidine-5'-phosphate decarboxylase in
RT   Cephalosporium acremonium.";
RL   Curr. Genet. 17:223-227(1990).
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; X15937; CAA34063.1; -; Genomic_DNA.
DR   PIR; S06746; DCCEOC.
DR   AlphaFoldDB; P14017; -.
DR   SMR; P14017; -.
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; 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; 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.
FT   CHAIN           1..376
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134655"
FT   REGION          160..208
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         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  41128 MW;  462A23AD21814FA7 CRC64;
     MAPHPTLKST YSTRAETVTH PLSAYLYKLM DLKASNLCLS ADVANARELL HVADKVGPSI
     VVLKTHYDMV AGWDFTPETG TGARLAKLAR KHGFLIFEDR KFGDIGNTVE LQYTQGAARI
     IEWAHIVNVN MVPGKASVTS LANAAAKWLE RLPYEVKTSV TVGTPRNTDE DDDDEDDGNA
     GEMERSHTFG LNGNNGVPIK ESSDGRKGSI VSVTTVTQQY ESAHSPRLTK TIAEEGDMLL
     AGLEEPPLNR GLLILAQMSS AGNFMNAEYT QACVEAAREH KDFVMGFVSQ EALNSQPDDD
     FIHMTPGCQL PPEHEEDAEL RGDGKGQQYN TPEKLIGVCG ADIVIVGRGI LKAGDLQHEA
     ERYRSAAWKA YTERVR
//