ID   PYRF_DEBHA              Reviewed;         267 AA.
AC   Q6BY69; Q96VQ4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 102.
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; OrderedLocusNames=DEHA2A11968g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MTCC 234;
RX   PubMed=11571754; DOI=10.1002/yea.774;
RA   Bansal P.K., Sharma P., Mondal A.K.;
RT   "A minisatellite sequence in the upstream region of DURA3 gene from
RT   halotolerant yeast Debaryomyces hansenii.";
RL   Yeast 18:1301-1307(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; AY033329; AAK54442.1; -; Genomic_DNA.
DR   EMBL; CR382133; CAG84825.1; -; Genomic_DNA.
DR   RefSeq; XP_456850.1; XM_456850.1.
DR   AlphaFoldDB; Q6BY69; -.
DR   SMR; Q6BY69; -.
DR   STRING; 284592.Q6BY69; -.
DR   GeneID; 2899491; -.
DR   KEGG; dha:DEHA2A11968g; -.
DR   VEuPathDB; FungiDB:DEHA2A11968g; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   HOGENOM; CLU_030821_0_0_1; -.
DR   InParanoid; Q6BY69; -.
DR   OMA; CLIKTHI; -.
DR   OrthoDB; 922at2759; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000000599; Chromosome A.
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   NCBIfam; TIGR01740; pyrF; 1.
DR   PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 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..267
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134658"
FT   ACT_SITE        94
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         60..62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         92..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        3..4
FT                   /note="KT -> NK (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28
FT                   /note="N -> S (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="E -> D (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="E -> D (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="F -> Y (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75..76
FT                   /note="VV -> II (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141..143
FT                   /note="SSK -> VSS (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167..168
FT                   /note="EK -> GL (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="T -> S (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200
FT                   /note="V -> I (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="Q -> E (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="T -> S (in Ref. 1; AAK54442)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   267 AA;  29320 MW;  D999613C57D2BEE0 CRC64;
     MVKTQTYTER ASAHPSPVAQ RLFKLMDNKK TNLCASVDVK STEEFLTLIE KLGPYICLVK
     THIDIIDDFS YEGTVVPLLA LAKKHNFMIF EDRKFADIGN TVKSQYSGGV YKIAQWSDIT
     NAHGITGSGI VKGLKEAAQE SSKEPRGLLM LAELSSKGSL AYGEYTEKTI EIAKSDKEFV
     IGFIAQRDMG GTDEGFDWIV MTPGVGLDDK GDGLGQQYRT VDQVVTTGTD IIIVGRGLFG
     QGRDPTVEGK RYRDAGWNAY LKKTGSL
//