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Database: UniProt
Entry: B1ITH3
LinkDB: B1ITH3
Original site: B1ITH3 
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   14-MAY-2014, entry version 41.
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; RPITQSA; -.
DR   OrthoDB; EOG6N6815; -.
DR   BioCyc; ECOL481805:GI3G-2391-MONOMER; -.
DR   UniPathway; UPA00070; UER00120.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-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; SSF51366; 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
//
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