ID   PYRC_CLOD6              Reviewed;         421 AA.
AC   Q18C47;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   02-SEP-2008, entry version 22.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=CD1526;
OS   Clostridium difficile (strain 630).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K.,
RA   Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a
RT   highly mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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 2 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; AM180355; CAJ68391.1; -; Genomic_DNA.
DR   RefSeq; YP_001088027.1; -.
DR   GeneID; 4914653; -.
DR   GenomeReviews; AM180355_GR; CD1526.
DR   KEGG; cdf:CD1526; -.
DR   NMPDR; fig|1496.1.peg.3393; -.
DR   HOGENOM; Q18C47; -.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00220; -; 1.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR004722; DHOmult.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   TIGRFAMs; TIGR00857; pyrC_multi; 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    421       Dihydroorotase.
FT                                /FTId=PRO_1000024080.
FT   METAL        60     60       Zinc 1 (By similarity).
FT   METAL        62     62       Zinc 1 (By similarity).
FT   METAL       141    141       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL       141    141       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       178    178       Zinc 2 (By similarity).
FT   METAL       231    231       Zinc 2 (By similarity).
FT   METAL       304    304       Zinc 1 (By similarity).
FT   MOD_RES     141    141       N6-carboxylysine (By similarity).
SQ   SEQUENCE   421 AA;  45976 MW;  1B97667E07506FDB CRC64;
     MILIKNGRVI DPKSQRDENI DLIIKENKIY KIGKFDESDE YEKIIDASGN VVAPGLVDVH
     VHFRDPGFTY KEDIESGAKS AARGGFTTVI CMANTNPIVD NEDTFNYVKE KSKNACINVL
     QAAAITKGFE GKELVDMEAL KKAGVPGFTD DGLPLMDSNL IMEAMIKAKE LDVPLSFHEE
     DPSLVGNPGV NAGKVASELG LKGASSVAED VMVARDCMLA LKTGAKVDIQ HISSGVSVDM
     VRFAKYLGAT VVAEASPHHF TLTEEDVLEF GTNAKMNPPL RSKWDRDKII EGLNDGTIEI
     IATDHAPHSK EEKDREFIKA PSGIIGLETS LALGITNLVH KNHLSMMQLI EKMSINPAKL
     YNLNIGFIEE GAVADIVIFN PEEEWTVESF VSKADNSPFK GKSLYGKVNY TICNGEIVYN
     A
//