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Database: UniProt/TrEMBL
Entry: E1SJL1_PANVC
LinkDB: E1SJL1_PANVC
Original site: E1SJL1_PANVC 
ID   E1SJL1_PANVC            Unreviewed;       347 AA.
AC   E1SJL1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   19-FEB-2014, entry version 23.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=Pvag_0865;
OS   Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Pantoea.
OX   NCBI_TaxID=712898;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C9-1;
RX   PubMed=20952567; DOI=10.1128/JB.01122-10;
RA   Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA   Stockwell V.O., Frey J.E., Duffy B.;
RT   "The genome sequence of the biocontrol agent Pantoea vagans strain C9-
RT   1.";
RL   J. Bacteriol. 192:6486-6487(2010).
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC       aspartate.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the DHOase family. Type 1 subfamily.
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DR   EMBL; CP002206; ADO09062.1; -; Genomic_DNA.
DR   RefSeq; YP_003930511.1; NC_014562.1.
DR   ProteinModelPortal; E1SJL1; -.
DR   EnsemblBacteria; ADO09062; ADO09062; Pvag_0865.
DR   GeneID; 9789385; -.
DR   KEGG; pva:Pvag_0865; -.
DR   PATRIC; 42417784; VBIPanVag152020_1009.
DR   HOGENOM; HOG000256259; -.
DR   KO; K01465; -.
DR   OMA; YAEAFEQ; -.
DR   BioCyc; PVAG712898:GHQ2-865-MONOMER; -.
DR   UniPathway; UPA00070; UER00117.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00219; PyrC_type1; 1.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR004721; DHOdimr.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF001237; DHOdimr; 1.
DR   TIGRFAMs; TIGR00856; pyrC_dimer; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW   Zinc.
FT   METAL        17     17       Zinc 1 (By similarity).
FT   METAL        19     19       Zinc 1 (By similarity).
FT   METAL       103    103       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL       103    103       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       140    140       Zinc 2 (By similarity).
FT   METAL       178    178       Zinc 2 (By similarity).
FT   METAL       251    251       Zinc 1 (By similarity).
FT   MOD_RES     103    103       N6-carboxylysine (By similarity).
SQ   SEQUENCE   347 AA;  38287 MW;  023173F430A60583 CRC64;
     MTAQPQQLTL RRPDDWHIHL RDDEMLKTVL PYTSAVNGRA IVMPNLVPPV TSVAAGEAYR
     DRILAALPAD HAFTPLMTCY LTDSLDPDEL ERGFTAGLFT AAKLYPAHAT TNSSHGVTNI
     ASIARVLDRM QTLGMPLLIH GEVTDAHIDI FDREARFIET VMVPLRSQFP ALKVVMEHIT
     TQDAAEYVAD AGETLGATIT PQHLMFNRNH MLVGGIRPHL YCLPILKRNV HQEALRKVVA
     SGNPRFFLGT DTAPHLRHLK EASCGCAGVF NAPTSLPAYA TVFEELNALE HFEAFCSENG
     PRFYGLPLNE GTITLVREPW QVPESIALGS HSLVPFLAGE TLNWRIA
//
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