ID C8TPD2_ECO26 Unreviewed; 348 AA.
AC C8TPD2;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 25.
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 ProtClustDB; PRK05451; -.
DR UniPathway; UPA00070; UER00117.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA: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).
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 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
//
