ID   PYRF_METRJ              Reviewed;         230 AA.
AC   B1M7M3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE            EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200};
DE   AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE            Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200};
DE            Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200};
GN   Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200};
GN   OrderedLocusNames=Mrad2831_1753;
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS   NBRC 15690 / NCIMB 10815 / 0-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC   0-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC       (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-
CC       Rule:MF_01200}.
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_01200};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01200}.
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DR   EMBL; CP001001; ACB23748.1; -; Genomic_DNA.
DR   RefSeq; WP_012318735.1; NC_010505.1.
DR   AlphaFoldDB; B1M7M3; -.
DR   SMR; B1M7M3; -.
DR   STRING; 426355.Mrad2831_1753; -.
DR   KEGG; mrd:Mrad2831_1753; -.
DR   PATRIC; fig|426355.14.peg.1801; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_067069_1_0_5; -.
DR   OrthoDB; 9806203at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000006589; 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_01200_B; OMPdecase_type1_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR047596; OMPdecase_bac.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR01740; pyrF; 1.
DR   PANTHER; PTHR32119; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR32119:SF2; 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..230
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_1000138542"
FT   ACT_SITE        67
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         65..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
SQ   SEQUENCE   230 AA;  23701 MW;  21CC0609A8A2C687 CRC64;
     MTEIADPRDR LIVALDLPSV QAAEALIDRI GDAATFYKIG YQLGYAGGLA LAERLAARGL
     KVFLDLKLHD IGNTVEEGVR SASGSGATFL TVHAYPQTMR AAVRGRGAGL RILAVTVLTS
     YDDADAAEAG YGLPVAELVA KRAAQAAEIG IDGLVCSAAE AGSVRRIVGP DRLIVTPGIR
     PAGAEAGDQK RVMTPGDARR AGIDHVVVGR PITGAADPRA VAQAIVADLA
//