ID   PYRF_METC4              Reviewed;         232 AA.
AC   B7KUF7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=Mchl_1799;
OS   Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS   extorquens).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=440085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT   CM4.";
RL   Submitted (DEC-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; CP001298; ACK82662.1; -; Genomic_DNA.
DR   RefSeq; WP_015950449.1; NC_011757.1.
DR   AlphaFoldDB; B7KUF7; -.
DR   SMR; B7KUF7; -.
DR   KEGG; mch:Mchl_1799; -.
DR   HOGENOM; CLU_067069_1_0_5; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000002385; 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..232
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_1000164575"
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   232 AA;  24165 MW;  99C9DF502DF6BD89 CRC64;
     MPESADPRDR LIVALDLPDV EAAERLVARI GDAVTFYKIG YRLAYAGGLD FAARLAKSGK
     KTFLDLKLHD IGNTVEEGVR SASALGATFL TVHAYPQTMR AAVRGRGSGL KILAVTVLTS
     YDDADAAEAG YALPVADLVA RRAEQAAEIG IDGIVCSAAE AGAVRHRIGP SGLIVTPGIR
     PAGAEAGDQK RVMTPGQARA AGIDHVVVGR PITGADDPRA VAQRIVAEME DA
//