ID   PYRC_CALS8              Reviewed;         430 AA.
AC   A4XKT2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 15.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=Csac_1932;
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Caldicellulosiruptor.
OX   NCBI_TaxID=351627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L.,
RA   Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M.,
RA   Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W.,
RA   Richardson P.;
RT   "Genome sequence of the thermophilic hydrogen-producing bacterium
RT   Caldicellulosiruptor saccharolyticus DSM 8903.";
RL   Submitted (APR-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 2 subfamily.
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DR   EMBL; CP000679; ABP67517.1; -; Genomic_DNA.
DR   RefSeq; YP_001180708.1; -.
DR   GeneID; 5089294; -.
DR   GenomeReviews; CP000679_GR; Csac_1932.
DR   KEGG; csc:Csac_1932; -.
DR   OMA; A4XKT2; CDVHPVG.
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; FALSE_NEG.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW   Zinc.
FT   CHAIN         1    430       Dihydroorotase.
FT                                /FTId=PRO_0000325590.
FT   METAL        61     61       Zinc 1 (By similarity).
FT   METAL        63     63       Zinc 1 (By similarity).
FT   METAL       143    143       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL       143    143       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       180    180       Zinc 2 (By similarity).
FT   METAL       233    233       Zinc 2 (By similarity).
FT   METAL       306    306       Zinc 1 (By similarity).
FT   MOD_RES     143    143       N6-carboxylysine (By similarity).
SQ   SEQUENCE   430 AA;  47394 MW;  75C5C16A7ED4318E CRC64;
     MILIKNAQII NSLHDKVEKA DILIVDDKIK KIGKDIEENP EKMTIIDASG KVVMPSFTDI
     HCHLREPGFE YKEDIKSGSR SAAAGGFTTI CCMPNTNPPV DNRAMVAYIK YRAREVSPIE
     VLPVGAITKG LLGEELAEIG FMKEEGAIAI SDDGKCVMNA NLMKNALLYS RDFSIPVISH
     CEDTNLSEGG QINLGYVSTI TGLRGIPREA ESVIIARDIL LAKETKSHLH ITHVSTKESV
     RLIKMAKEWG VNVTADTCPH YISLTEEEVL GFNTNAKVNP PLRTQEDVEA LIEGLKEGVI
     DCISTDHAPH HKDEKNVEFN LAASGTIGFE TAFSVLFTYL VEKNGFDIGK IVELLNHNPR
     KIIGLSPNVL KEGEKANLVI VDLKKKWEVK EENIVSKSKN SVFLGKLLTS YVETVIYNGK
     ILKKDGVLNC
//