ID   PYRF_THET2              Reviewed;         257 AA.
AC   P96076;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE            EC=4.1.1.23;
DE   AltName: Full=OMP decarboxylase;
DE            Short=OMPDCase;
DE            Short=OMPdecase;
GN   Name=pyrF; OrderedLocusNames=TT_C1381;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-257.
RX   PubMed=8787418; DOI=10.1128/aem.62.6.2191-2194.1996;
RA   Yamagishi A., Tanimoto T., Suzuki T., Oshima T.;
RT   "Pyrimidine biosynthesis genes (pyrE and pyrF) of an extreme thermophile,
RT   Thermus thermophilus.";
RL   Appl. Environ. Microbiol. 62:2191-2194(1996).
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE017221; AAS81723.1; -; Genomic_DNA.
DR   EMBL; D83330; BAA11885.1; -; Genomic_DNA.
DR   RefSeq; WP_011173764.1; NZ_CP133179.1.
DR   AlphaFoldDB; P96076; -.
DR   SMR; P96076; -.
DR   KEGG; tth:TT_C1381; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_0_0_0; -.
DR   OrthoDB; 9808470at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000000592; 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_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   NCBIfam; TIGR02127; pyrF_sub2; 1.
DR   PANTHER; PTHR43375; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43375:SF1; 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..257
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134635"
FT   ACT_SITE        86
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   257 AA;  27436 MW;  806D562484B9F3EA CRC64;
     MDFLEALSRP PLVLGVDPRP TLHGPEPLAH IRRYTLELLE ALAPRLAAAK FQLAFFEALG
     PEGTALLWEL ASASRVMGLP VIFDGKRGDI GSTAEAYARA YLEAFPGSAL TVNPYLGLDA
     LKPFFQAASR TGGGVFVLAK TSNPGSGFLQ DLLVEGKPLY LHLAEALERE GERYREGPWS
     RVGMVVGATY PEAVARVRER APHAPLLLPG VGAQGGRPLK GEGLLFAASR ALYYPGGRPD
     LKAALEAAEA LLKALVE
//