ID   PYRC_CITK8              Reviewed;         347 AA.
AC   A8AI14;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-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=CKO_02001;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000822; ABV13127.1; -; Genomic_DNA.
DR   RefSeq; YP_001453563.1; -.
DR   GeneID; 5582931; -.
DR   GenomeReviews; CP000822_GR; CKO_02001.
DR   KEGG; cko:CKO_02001; -.
DR   OMA; A8AI14; 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    347       Dihydroorotase.
FT                                /FTId=PRO_1000024008.
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;  38731 MW;  9A1EEBF605745458 CRC64;
     MTAPSQVLKI RRPDDWHVHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVDAAIAYR
     QRILDAVPAG HDFTPLMTCY LTDTLDPDEL ERGFREGVFT AAKLYPANAT TNSSHGVTSV
     DTIMPVLERM EKLGMPLLVH GEVTHADIDI FDREARFIET VMEPLRQRLT ALKVVFEHIT
     TKDAAEYVRD GNELLAATIT PQHLMFNRNH MLVGGIRPHL YCLPILKRNV HQQALRELVA
     SGFSRAFLGT DSAPHARHRK ETSCGCAGCF NAPTALGSYA TVFEEMNALA HFEAFCSLNG
     PRFYGLSVNE TYVELVREEQ LVPESITLAD DSLVPFLGGE RVRWSVK
//