ID   PYRC_HELHP              Reviewed;         343 AA.
AC   Q7VIJ1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=HH_0614;
OS   Helicobacter hepaticus.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=32025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   MEDLINE=22709201; PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P.,
RA   Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A.,
RA   Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G.,
RA   Schauer D.B., Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium
RT   Helicobacter hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(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 1 subfamily.
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DR   EMBL; AE017125; AAP77211.1; -; Genomic_DNA.
DR   RefSeq; NP_860145.1; -.
DR   HSSP; P05020; 1J79.
DR   GeneID; 1493668; -.
DR   GenomeReviews; AE017125_GR; HH_0614.
DR   KEGG; hhe:HH0614; -.
DR   NMPDR; fig|235279.1.peg.614; -.
DR   HOGENOM; Q7VIJ1; -.
DR   OMA; Q7VIJ1; IMPNLVP.
DR   BioCyc; HHEP235279:HH_0614-MON; -.
DR   BRENDA; 3.5.2.3; 279780.
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; IPR004721; DHOdimr.
DR   InterPro; IPR002195; Dihydroorotase_CS.
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    343       Dihydroorotase.
FT                                /FTId=PRO_0000325572.
FT   METAL        14     14       Zinc 1 (By similarity).
FT   METAL        16     16       Zinc 1 (By similarity).
FT   METAL        97     97       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL        97     97       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       136    136       Zinc 2 (By similarity).
FT   METAL       170    170       Zinc 2 (By similarity).
FT   METAL       242    242       Zinc 1 (By similarity).
FT   MOD_RES      97     97       N6-carboxylysine (By similarity).
SQ   SEQUENCE   343 AA;  38495 MW;  D11C3F0BA743F204 CRC64;
     MPQTLQLTNP MDMHLHLREG EMLSAILPFS ANPFSAAVVM PNLKTPITTT AQALAYKRQI
     LSLCSTSFEP LMSIFLTPDL DKQELIRAKE AGIHILKLYP KGSTTGSEKG VKEMLCEKTL
     HIFEIAQELG FILSIHGESN GFCMEREYEF LPIFAHIAQH FPRLRIIIEH MSDRRSLELI
     EQYPNLYATL TLHHITMNLD DVLGGGINPH HFCKPMLKTK KDQQALLQAA LNAHPKVSFG
     SDSAPHLESA KLNSKGAAGI FSAPILLPAL AEVFAFHNAL DCLQTFISNR AIANYKLKHF
     PIKTITLERV ENPVPPYINT PLGHIIPLRA QTNLSWRIKE ENR
//