ID PYRF_BRASB Reviewed; 243 AA.
AC A5E8J8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 39.
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=BBta_0195;
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=288000;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S.,
RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L.,
RA Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P.,
RA Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A.,
RA Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic
RT bradyrhizobia.";
RL Science 316:1307-1312(2007).
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-
CC monophosphate (OMP) to uridine 5'-monophosphate (UMP) (By
CC similarity).
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 -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1
CC subfamily.
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DR EMBL; CP000494; ABQ32492.1; -; Genomic_DNA.
DR RefSeq; YP_001236398.1; NC_009485.1.
DR ProteinModelPortal; A5E8J8; -.
DR STRING; 288000.BBta_0195; -.
DR EnsemblBacteria; ABQ32492; ABQ32492; BBta_0195.
DR GeneID; 5150940; -.
DR KEGG; bbt:BBta_0195; -.
DR PATRIC; 21201390; VBIBraSp29847_0399.
DR eggNOG; COG0284; -.
DR HOGENOM; HOG000226070; -.
DR KO; K01591; -.
DR OMA; NFKIFLD; -.
DR ProtClustDB; PRK00230; -.
DR BioCyc; BSP288000:GJBR-188-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_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 Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; RibP_bind_barrel; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1 243 Orotidine 5'-phosphate decarboxylase.
FT /FTId=PRO_1000065895.
FT REGION 65 74 Substrate binding (By similarity).
FT ACT_SITE 67 67 Proton donor (By similarity).
FT BINDING 16 16 Substrate (By similarity).
FT BINDING 38 38 Substrate (By similarity).
FT BINDING 120 120 Substrate (By similarity).
FT BINDING 181 181 Substrate (By similarity).
FT BINDING 190 190 Substrate (By similarity).
FT BINDING 210 210 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 211 211 Substrate (By similarity).
SQ SEQUENCE 243 AA; 25201 MW; 895A0F455256A1FE CRC64;
MPTEIAPRDR LIVALDLPGV AEAEAMITRL GDAVTFYKIG MELTYAGGLG LAERLAADGK
QVFMDLKLHD IPNTVERATR QIARLGARFL TVHGFSQSMT AALAGAAGSP LELLAVTVMT
SYDDADLAAA GYAMGVKELV ARRAVQAKQI GIHGLILSPE ETQLVRPLVG PDMQLVTPGI
RPAGSDVGDQ KRIMTPALAI AGGADRLVVG RPVTGAADPA AAAESIVADI ASALALVGKT
NRT
//
