ID   PYRF_DEHM1              Reviewed;         270 AA.
AC   Q3ZAI1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=DET0013;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS   (Dehalococcoides ethenogenes (strain 195)).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA   Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA   Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA   Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA   Zinder S.H., Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(2005).
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; CP000027; AAW39163.1; -; Genomic_DNA.
DR   RefSeq; WP_010935823.1; NC_002936.3.
DR   AlphaFoldDB; Q3ZAI1; -.
DR   SMR; Q3ZAI1; -.
DR   STRING; 243164.DET0013; -.
DR   EnsemblBacteria; AAW39163; AAW39163; DET0013.
DR   KEGG; det:DET0013; -.
DR   PATRIC; fig|243164.10.peg.12; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_1_0_0; -.
DR   OMA; QSAFFER; -.
DR   OrthoDB; 1181405at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000008289; 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; 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.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..270
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_1000066470"
FT   ACT_SITE        89
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   270 AA;  29786 MW;  33EFBCC7B816224F CRC64;
     MKFLEKLKQA GNSHNSLLCV GLDPDPKLMP VGMTALEFNR EIIAATAPFV CGYKINLAFY
     EALGKQGWEI LSETCKLIPP ELLSIADAKR GDIGNTSKAY ARAVFDELGC DGVTASPYLG
     YDSLEPFIEY QDKGIFILCR TSNQGSADFQ MLKTEYLGQK RFLYEVVADK SLQWNRYENI
     GLVVGATQQE ELKKLRLSYP KMPFLIPGIG AQGGDLKATV ENGTNQSGQL ALICASRGIL
     YARSGSEFAQ GAAEAAKQMR DAINHYRKRF