ID   PYRF_NEUCR              Reviewed;         397 AA.
AC   P05035; Q7RV44;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   24-JAN-2024, entry version 149.
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=pyr-4; ORFNames=B23H20.130, NCU03488;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3019837; DOI=10.1016/0378-1119(86)90007-7;
RA   Newbury S.F., Glazebrook J.A., Radford A.;
RT   "Sequence analysis of the pyr-4 (orotidine 5'-P decarboxylase) gene of
RT   Neurospora crassa.";
RL   Gene 43:51-58(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2959843; DOI=10.1007/bf00329672;
RA   Glazebrook J.A., Mitchell K., Radford A.;
RT   "Molecular genetic analysis of the pyr-4 gene of Neurospora crassa.";
RL   Mol. Gen. Genet. 209:399-402(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; M13448; AAA33611.1; -; Genomic_DNA.
DR   EMBL; X05993; CAA29411.1; -; Genomic_DNA.
DR   EMBL; AL669988; CAD21085.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA26639.1; -; Genomic_DNA.
DR   PIR; A24398; DCNCOP.
DR   RefSeq; XP_955875.1; XM_950782.3.
DR   AlphaFoldDB; P05035; -.
DR   SMR; P05035; -.
DR   STRING; 367110.P05035; -.
DR   PaxDb; 5141-EFNCRP00000002693; -.
DR   EnsemblFungi; EAA26639; EAA26639; NCU03488.
DR   GeneID; 3872022; -.
DR   KEGG; ncr:NCU03488; -.
DR   VEuPathDB; FungiDB:NCU03488; -.
DR   HOGENOM; CLU_030821_1_1_1; -.
DR   InParanoid; P05035; -.
DR   OMA; CLIKTHI; -.
DR   OrthoDB; 922at2759; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
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..397
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134665"
FT   ACT_SITE        107
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105..114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  43903 MW;  C9A39CDA33A3FCD9 CRC64;
     MSTSQETQPH WSLKQSFAER VESSTHPLTS YLFRLMEVKQ SNLCLSADVE HARDLLALAD
     KVGPSIVVLK THYDLITGWD YHPHTGTGAK LAALARKHGF LIFEDRKFVD IGSTVQKQYT
     AGTARIVEWA HITNADIHAG EAMVSAMAQA AQKWRERIPY EVKTSVSVGT PVADQFADEE
     AEDQVEELRK VVTRETSTTT KDTDGRKSSI VSITTVTQTY EPADSPRLVK TISEDDEMVF
     PGIEEAPLDR GLLILAQMSS KGCLMDGKYT WECVKAARKN KGFVMGYVAQ QNLNGITKEA
     LAPSYEDGES TTEEEAQADN FIHMTPGCKL PPPGEEAPQG DGLGQQYNTP DNLVNIKGTD
     IAIVGRGIIT AADPPAEAER YRRKAWKAYQ DRRERLA
//