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 29-MAY-2013, entry version 82.
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 HB27 / ATCC BAA-163 / DSM 7039).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB27 / ATCC BAA-163 / DSM 7039;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T.,
RA Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R.,
RA Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R.,
RA Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus
RT thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-257.
RX PubMed=8787418;
RA Yamagishi A., Tanimoto T., Suzuki T., Oshima T.;
RT "Pyrimidine biosynthesis genes (pyrE and pyrF) of an extreme
RT thermophile, Thermus thermophilus.";
RL Appl. Environ. Microbiol. 62:2191-2194(1996).
CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2).
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; UMP from orotate: step 2/2.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2
CC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AE017221; AAS81723.1; -; Genomic_DNA.
DR EMBL; D83330; BAA11885.1; -; Genomic_DNA.
DR RefSeq; YP_005350.1; NC_005835.1.
DR ProteinModelPortal; P96076; -.
DR STRING; 262724.TTC1381; -.
DR EnsemblBacteria; AAS81723; AAS81723; TT_C1381.
DR GeneID; 2774890; -.
DR KEGG; tth:TTC1381; -.
DR PATRIC; 23953175; VBITheThe54392_1374.
DR eggNOG; COG0284; -.
DR KO; K01591; -.
DR OMA; AHIRRYT; -.
DR ProtClustDB; CLSK738813; -.
DR BioCyc; TTHE262724:GCAT-1398-MONOMER; -.
DR UniPathway; UPA00070; UER00120.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:HAMAP.
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 Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; RibP_bind_barrel; 1.
DR TIGRFAMs; TIGR02127; pyrF_sub2; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1 257 Orotidine 5'-phosphate decarboxylase.
FT /FTId=PRO_0000134635.
FT ACT_SITE 86 86 Proton donor (By similarity).
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
//
