ID   PYRF_ALBFT              Reviewed;         287 AA.
AC   Q21RX7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Rfer_3776;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000267; ABD71476.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q21RX7; -.
DR   SMR; Q21RX7; -.
DR   STRING; 338969.Rfer_3776; -.
DR   EnsemblBacteria; ABD71476; ABD71476; Rfer_3776.
DR   KEGG; rfr:Rfer_3776; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_1_0_4; -.
DR   OMA; QSAFFER; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000008332; 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; Reference proteome.
FT   CHAIN           1..287
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_1000066486"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   287 AA;  30777 MW;  C38048531FF45DE3 CRC64;
     MTFLDMLRAA ERQNGSMLCV GLDPEPTRFP AHYSGDVSKI YDFCAAIVDA TADLVMAFKP
     QIAYFAAHRA EPQLERLIAH MRRAAPHVPV ILDAKRGDIG STAEQYAKEA FERYGADAVT
     LSPFMGFDSL QPYLRYHGKG AFLLCRTSNP GGDDLQSQRL ASVEGTPLLY EHIARLAQGP
     WNLNGQLGLV VGATYPAELE RVRALAPTLP LLIPGVGAQG GDCAATVRAA WRAAPGTSGE
     ALDTLAPIIV NSSRAILYAS SGADFAQAAR REALATRDLL QAARQPA