ID   PYRC_ENTS8              Reviewed;         348 AA.
AC   A7MG30;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 12.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=ESA_02286;
OS   Enterobacter sakazakii (strain ATCC BAA-894).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; UMP from HCO(3)(-): step 3/6.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the DHOase family. Type 1 subfamily.
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DR   EMBL; CP000783; ABU77535.1; -; Genomic_DNA.
DR   RefSeq; YP_001438371.1; -.
DR   GeneID; 5551627; -.
DR   GenomeReviews; CP000783_GR; ESA_02286.
DR   KEGG; esa:ESA_02286; -.
DR   OMA; A7MG30; IMPNLVP.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0019856; P:pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00219; -; 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   CHAIN         1    348       Dihydroorotase.
FT                                /FTId=PRO_1000024012.
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;  38591 MW;  7E2E81788657B6B2 CRC64;
     MTAQPQVLTI RRPDDWHVHL RDGDMLKTVV PYTSETYGRA IVMPNLAPPV TTVEAAIAYR
     QRILDAVPEH HAFEPLMTCY LTDTLDADEL ERGFQQGVFT AAKLYPANAT TNSSHGVTSV
     DNIMTVLERM EKLGMPLLVH GEVTHSEVDI FDREARFIET VMEPLRKRLQ GLKVVFEHIT
     TKDAADYVRE GNSLLGATIT PQHLMFNRNH MLAGGIRPHL YCLPILKRNV HQQALRELVA
     SGCERVFLGT DSAPHARHRK ETSCGCAGCF NAPSALGAYA TVFEEMNALA HFEAFASLNG
     PGFYGLPVNE GTVTLVREES VMPETIAIAD DTLVPFLAGE AVRWTVKR
//