PYRF_THET2
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 25-MAY-2022, entry version 114.
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; Deinococcus-Thermus; 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; NC_005835.1.
DR AlphaFoldDB; P96076; -.
DR SMR; P96076; -.
DR STRING; 262724.TT_C1381; -.
DR EnsemblBacteria; AAS81723; AAS81723; TT_C1381.
DR KEGG; tth:TT_C1381; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_060704_0_0_0; -.
DR OMA; QSAFFER; -.
DR OrthoDB; 1181405at2; -.
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 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.
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
