ID A4XVS0_PSEMY Unreviewed; 245 AA.
AC A4XVS0;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 47.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMP decarboxylase;
GN Name=pyrF; OrderedLocusNames=Pmen_2681;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C.,
RA Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Hersman L., Dubois J., Maurice P.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000680; ABP85436.1; -; Genomic_DNA.
DR RefSeq; YP_001188168.1; NC_009439.1.
DR ProteinModelPortal; A4XVS0; -.
DR STRING; 399739.Pmen_2681; -.
DR EnsemblBacteria; ABP85436; ABP85436; Pmen_2681.
DR GeneID; 5107832; -.
DR KEGG; pmy:Pmen_2681; -.
DR PATRIC; 19911908; VBIPseMen131592_2708.
DR eggNOG; COG0284; -.
DR HOGENOM; HOG000226071; -.
DR KO; K01591; -.
DR OMA; NFKIFLD; -.
DR ProtClustDB; PRK00230; -.
DR BioCyc; PMEN399739:GHR6-2761-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 REGION 74 83 Substrate binding (By similarity).
FT ACT_SITE 76 76 Proton donor (By similarity).
FT BINDING 25 25 Substrate (By similarity).
FT BINDING 47 47 Substrate (By similarity).
FT BINDING 134 134 Substrate (By similarity).
FT BINDING 194 194 Substrate (By similarity).
FT BINDING 203 203 Substrate (By similarity).
FT BINDING 223 223 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 224 224 Substrate (By similarity).
SQ SEQUENCE 245 AA; 25907 MW; ABEB7F8C329D25B2 CRC64;
MRGVFVLSET RLMPACQTPI IVALDFPSRD AALALADRLD PALCRVKVGK ELFTRSGPQV
VEALQAKGFE LFLDLKFHDI PNTTAMAVKA AAELGVWMVN VHCSGGLRMM AACRNELDKL
TGAKPLLIGV TVLTSMEQQD LAGIGLDVPP QEQVLRLAGL AADAGLDGLV CSAQEAQALK
VAQPRLQLVT PGIRPAGSNA DDQKRILTPR QALEAGSDYL VIGRPISQAA DPAQALAAVV
AELRA
//
