PYRF_MYCUA
ID PYRF_MYCUA Reviewed; 278 AA.
AC A0PPJ3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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}; OrderedLocusNames=MUL_1785;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL04262.1; -; Genomic_DNA.
DR RefSeq; WP_011739882.1; NC_008611.1.
DR AlphaFoldDB; A0PPJ3; -.
DR SMR; A0PPJ3; -.
DR STRING; 362242.MUL_1785; -.
DR EnsemblBacteria; ABL04262; ABL04262; MUL_1785.
DR KEGG; mul:MUL_1785; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_060704_0_0_11; -.
DR OMA; QSAFFER; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000000765; 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 Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR43375; PTHR43375; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR02127; pyrF_sub2; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1..278
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_1000066480"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ SEQUENCE 278 AA; 27827 MW; 36F53EE88E6D794F CRC64;
MTGFGARLAE AKAHRGPLCL GIDPHPELLR AWDLPATADG LAAFCDICVA AFAGFAVVKP
QVAFFEAYGA AGFAVLEGTM AALRANGVLV LADAKRGDIG STMAAYAAAW AGDSPLAADA
VTVSPFLGFG SLRPLLEVAT ANDRGVFVLA ATSNPEGATI QRADADGRTV AQLIVDQVGL
FNSEVGEVTG SEPGSVGVVV GATVLNPPDV SGLGGPVLVP GVGVQGGRPE ALGGLGGAAP
QQLLPAVSRE VLRAGPSISE VRAAAERMLD SVAYLSAV
