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Database: UniProt/TrEMBL
Entry: C8TPD2_ECO26
LinkDB: C8TPD2_ECO26
Original site: C8TPD2_ECO26 
ID   C8TPD2_ECO26            Unreviewed;       348 AA.
AC   C8TPD2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   11-JUN-2014, entry version 31.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=ECO26_1395;
OS   Escherichia coli O26:H11 (strain 11368 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=573235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11368 / EHEC;
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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; AP010953; BAI24696.1; -; Genomic_DNA.
DR   RefSeq; YP_003228436.1; NC_013361.1.
DR   STRING; 573235.ECO26_1395; -.
DR   MEROPS; M38.A02; -.
DR   EnsemblBacteria; BAI24696; BAI24696; ECO26_1395.
DR   GeneID; 8480868; -.
DR   KEGG; eoj:ECO26_1395; -.
DR   PATRIC; 18398339; VBIEscCol24965_1427.
DR   eggNOG; COG0418; -.
DR   HOGENOM; HOG000256259; -.
DR   KO; K01465; -.
DR   OrthoDB; EOG6TFCMH; -.
DR   BioCyc; ECOL573235:GCY7-1435-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; PS00482; DIHYDROOROTASE_1; 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){EA6}.
FT   METAL        19     19       Zinc 1 (By similarity){EA6}.
FT   METAL       103    103       Zinc 1; via carbamate group (By
FT                                similarity){EA6}.
FT   METAL       103    103       Zinc 2; via carbamate group (By
FT                                similarity){EA6}.
FT   METAL       140    140       Zinc 2 (By similarity){EA6}.
FT   METAL       178    178       Zinc 2 (By similarity){EA6}.
FT   METAL       251    251       Zinc 1 (By similarity){EA6}.
FT   MOD_RES     103    103       N6-carboxylysine (By similarity){EA6}.
SQ   SEQUENCE   348 AA;  38807 MW;  13357FD24172C1F1 CRC64;
     MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR
     QRILDAVPAG HNFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSI
     DAIMPVLERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT
     TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA
     SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG
     PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVHWSVKQ
//
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