ID   PYRF_MOOTA              Reviewed;         252 AA.
AC   Q2RK39;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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}; OrderedLocusNames=Moth_0883;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC19200.1; -; Genomic_DNA.
DR   RefSeq; YP_429743.1; NC_007644.1.
DR   AlphaFoldDB; Q2RK39; -.
DR   SMR; Q2RK39; -.
DR   STRING; 264732.Moth_0883; -.
DR   EnsemblBacteria; ABC19200; ABC19200; Moth_0883.
DR   KEGG; mta:Moth_0883; -.
DR   PATRIC; fig|264732.11.peg.948; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_067069_1_0_9; -.
DR   OMA; NFKIFLD; -.
DR   UniPathway; UPA00070; UER00120.
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_01200_B; OMPdecase_type1_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR01740; pyrF; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT   CHAIN           1..252
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000241877"
FT   ACT_SITE        75
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         73..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
SQ   SEQUENCE   252 AA;  26861 MW;  4E497F88E7685D51 CRC64;
     MPTLMYLQEM IRMHAKDKII VALDVPDLAA GEKLVDRLSP YAGMFKVGLE FFTAAGPAAV
     RMVKERGGRV FADLKFHDIP NTVAGAARAL VRLGVDMLNV HAAGGKAMLQ AAAAAVREEA
     AALNRPAPVI IAVTVLTSLD REALRCEVGI EREVEEQVAR WALLAREAGL DGVVASPREI
     RAIREACGPE FVIVTPGVRP AGSDRGDQRR VMTPAEALRE GASYLVIGRP ITAAPDPVAA
     ARAIAAEIEM VK