ID PYRF_ECOLC Reviewed; 245 AA.
AC B1ITH3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 01-MAY-2013, entry version 37.
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=EcolC_2345;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) 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; CP000946; ACA77980.1; -; Genomic_DNA.
DR RefSeq; YP_001725307.1; NC_010468.1.
DR ProteinModelPortal; B1ITH3; -.
DR SMR; B1ITH3; 12-243.
DR STRING; 481805.EcolC_2345; -.
DR EnsemblBacteria; ACA77980; ACA77980; EcolC_2345.
DR GeneID; 6066877; -.
DR KEGG; ecl:EcolC_2345; -.
DR PATRIC; 18227562; VBIEscCol82905_2504.
DR eggNOG; COG0284; -.
DR HOGENOM; HOG000226071; -.
DR KO; K01591; -.
DR OMA; NFKIFLD; -.
DR ProtClustDB; PRK00230; -.
DR BioCyc; ECOL481805:GI3G-2391-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 1 245 Orotidine 5'-phosphate decarboxylase.
FT /FTId=PRO_1000085490.
FT REGION 71 80 Substrate binding (By similarity).
FT ACT_SITE 73 73 Proton donor (By similarity).
FT BINDING 22 22 Substrate (By similarity).
FT BINDING 44 44 Substrate (By similarity).
FT BINDING 131 131 Substrate (By similarity).
FT BINDING 192 192 Substrate (By similarity).
FT BINDING 201 201 Substrate (By similarity).
FT BINDING 221 221 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 222 222 Substrate (By similarity).
SQ SEQUENCE 245 AA; 26366 MW; F2E53689CFB1D90D CRC64;
MTLTASSSSR AVTNSPVVVA LDYHNRDDAL SFVDKIDPRD CRLKVGKEMF TLFGPQFVRE
LQQRGFDIFL DLKFHDIPNT AAHAVAAAAD LGVWMVNVHA SGGARMMTAA REALVPFGKD
APLLIAVTVL TSMEASDLVD LGMTLSPADY AERLAALTQK CGLDGVVCSA QEAVRFKQVF
GQEFKLVTPG IRPQGSEAGD QRRIMTPEQA LSAGVDYMVI GRPVTQSVDP AQTLKAINAS
LQRSA
//
