ID   PYRC_CORGL              Reviewed;         447 AA.
AC   Q8NQ39;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   22-JUL-2008, entry version 41.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=Cgl1611, cg1815;
OS   Corynebacterium glutamicum (Brevibacterium flavum).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RA   Nakagawa S.;
RT   "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA   Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA   Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA   McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA   Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA   Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT   and its impact on the production of L-aspartate-derived amino acids
RT   and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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; BA000036; BAB99004.1; -; Genomic_DNA.
DR   EMBL; BX927152; CAF21620.1; -; Genomic_DNA.
DR   RefSeq; NP_600825.1; -.
DR   RefSeq; YP_225896.1; -.
DR   GeneID; 1019579; -.
DR   GeneID; 3343550; -.
DR   GenomeReviews; BX927147_GR; cg1815.
DR   GenomeReviews; BA000036_GR; Cgl1611.
DR   KEGG; cgb:cg1815; -.
DR   KEGG; cgl:NCgl1549; -.
DR   HOGENOM; Q8NQ39; -.
DR   BioCyc; CGLU196627-1:CG1815-MON; -.
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   ProDom; PD000518; DHOase; 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    447       Dihydroorotase.
FT                                /FTId=PRO_0000147232.
FT   METAL        73     73       Zinc 1 (By similarity).
FT   METAL        75     75       Zinc 1 (By similarity).
FT   METAL       194    194       Zinc 2 (By similarity).
FT   METAL       247    247       Zinc 2 (By similarity).
FT   METAL       320    320       Zinc 1 (By similarity).
SQ   SEQUENCE   447 AA;  47827 MW;  5AAD2377CF5F6572 CRC64;
     MVDSNTQYPE TGALAPAPAD SLLISNVLVY GEGEPTNVFV KDGVIAAIGG THEADRTIDG
     NGGVLLPGFV DMHVHLREPG REDTETIATG SAAAAKGGFT AVFTMANTTP VMDQPVIAES
     VWFKGQNIGL CDVHPVGSIT KGLEGKELTE FGMMARSEAK VRMFSDDGKC VDDPQVMRRA
     LEYAKGMDVL IAQHAEDHRL TEGASAHEGE NAARLGLRGW PRVAEESIVV RDAIMARDYG
     NRVHICHAST EGTVELLRWA KSQGIPITAE VTPHHLTLTD ERLETYDAVN KVNPPLRESR
     DAEALKKALL DGTIDVVATD HAPHGSEDKC CEFENAKPGM LGLETSLSII VDTFVATGLA
     DWRFVARVMS ERPAEITRLP GQGRPIAEGE PANLAIVDPG KTWTASGADF ASKAENTPFE
     GQEFSAKVTH TVLRGKVTCA DGVAQNA
//