ID PYRF_XANC5 Reviewed; 243 AA.
AC Q3BMA4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 01-MAY-2013, entry version 54.
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=XCV4378;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O.,
RA Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A.,
RA Bonas U., Bartels D., Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant
RT pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed
RT by the complete genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ26109.1; -; Genomic_DNA.
DR RefSeq; YP_366109.1; NC_007508.1.
DR ProteinModelPortal; Q3BMA4; -.
DR STRING; 316273.XCV4378; -.
DR EnsemblBacteria; CAJ26109; CAJ26109; XCV4378.
DR GeneID; 3732791; -.
DR KEGG; xcv:XCV4378; -.
DR PATRIC; 24098436; VBIXanCam71633_4678.
DR eggNOG; COG0284; -.
DR HOGENOM; HOG000226070; -.
DR KO; K01591; -.
DR OMA; NFKIFLD; -.
DR ProtClustDB; PRK00230; -.
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_0000241931.
FT REGION 69 78 Substrate binding (By similarity).
FT ACT_SITE 71 71 Proton donor (By similarity).
FT BINDING 19 19 Substrate (By similarity).
FT BINDING 41 41 Substrate (By similarity).
FT BINDING 124 124 Substrate (By similarity).
FT BINDING 185 185 Substrate (By similarity).
FT BINDING 194 194 Substrate (By similarity).
FT BINDING 214 214 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 215 215 Substrate (By similarity).
SQ SEQUENCE 243 AA; 25692 MW; E49BC68570A372B1 CRC64;
MSRAPLPLAA HERLIFALDV PGHDEAIAWV DRLGDSVSFY KIGMELLASG EYFHVLDALA
KRDKRVFVDL KFFDIPATVA GTIRRLAQWP VSYCTVHGWH AGMLQAAAEA NHGDMRLLAV
TVLTSMGRPD LAAMGIDREP VDVVVERALA AQAAGIDGVI ASGQEAGPIR RATGPDFSIV
CPGIRPGGPV GDDQQRTVGV AQAFTDGADA IVVGRPIRQA SDPAAAATAI QDEIRAALPQ
NGN
//
