ID   PYRF_MYCLB              Reviewed;         282 AA.
AC   B8ZUL5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01215};
DE            EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01215};
DE   AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01215};
DE            Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01215};
DE            Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01215};
GN   Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01215};
GN   OrderedLocusNames=MLBr00537;
OS   Mycobacterium leprae (strain Br4923).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=561304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br4923;
RX   PubMed=19881526; DOI=10.1038/ng.477;
RA   Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA   Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA   Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA   Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA   Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA   Rougemont J., Brennan P.J., Cole S.T.;
RT   "Comparative genomic and phylogeographic analysis of Mycobacterium
RT   leprae.";
RL   Nat. Genet. 41:1282-1289(2009).
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|HAMAP-Rule:MF_01215};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01215}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01215}.
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DR   EMBL; FM211192; CAR70630.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8ZUL5; -.
DR   SMR; B8ZUL5; -.
DR   KEGG; mlb:MLBr00537; -.
DR   HOGENOM; CLU_060704_0_0_11; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000006900; Chromosome.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01215; OMPdecase_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR011995; OMPdecase_type-2.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR02127; pyrF_sub2; 1.
DR   PANTHER; PTHR43375; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43375:SF1; 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..282
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_1000213893"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   282 AA;  28678 MW;  89DE23C44B227BA5 CRC64;
     MTGFGARLVE ATSRRGQLCL GIDPHPELLR AWDLPTTADG LAAFCDICVE AFSGFAIVKP
     QVAFFEAYGA AGFAVLEYTI AALRSVGVLV LADAKRGDIG STMAAYAAAW AGNSPLAADA
     VTASPYLGFG SLRPLLEVAA AHDRGVFVLA STSNLEGATV QRATFDGRIV AQLIVDQAAF
     VNREMNRSFH RSEPGCLGYV GVVVGATVFG APDVSALGGP VLVPGVGAQG GHPEALGGLG
     GAAPGQLLPA VSRAVLRAGP GVSELRAAGE QMRDAVAYLA AV
//