ID   PYRC_HELAH              Reviewed;         339 AA.
AC   Q17W17;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=Hac_1431;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H.,
RA   Morelli G., Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied
RT   a host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(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 1 subfamily.
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DR   EMBL; AM260522; CAK00159.1; -; Genomic_DNA.
DR   RefSeq; YP_665158.1; -.
DR   GeneID; 4177751; -.
DR   GenomeReviews; AM260522_GR; Hac_1431.
DR   KEGG; hac:Hac_1431; -.
DR   NMPDR; fig|382638.8.peg.1385; -.
DR   HOGENOM; Q17W17; -.
DR   OMA; Q17W17; IMPNLVP.
DR   BioCyc; HACI382638:HAC_1431-MON; -.
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    339       Dihydroorotase.
FT                                /FTId=PRO_1000024016.
FT   METAL        12     12       Zinc 1 (By similarity).
FT   METAL        14     14       Zinc 1 (By similarity).
FT   METAL        94     94       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL        94     94       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       133    133       Zinc 2 (By similarity).
FT   METAL       167    167       Zinc 2 (By similarity).
FT   METAL       239    239       Zinc 1 (By similarity).
FT   MOD_RES      94     94       N6-carboxylysine (By similarity).
SQ   SEQUENCE   339 AA;  38001 MW;  F40860B3AF155A31 CRC64;
     MEITLFDPID AHLHVREGVL LKAVLKYSSE PFSAAVIMPN LSKPLIDTQI TLEYEGEILK
     NSSNFKPLMS LYFNDGLTLE ELQHAKHQGI KFLKLYPKGM TTNAQNGTSD LLGEKTLEIL
     EDAQKLGFIL CIHAEQAGFC LDKEFLCHSV LETFAHSFPK LKIIIEHLSD WRSIALIEKH
     DNLYATLTLH HISMTLDDLL GGSLNPHCFC KPLIKTQKDQ ERLLSLALKA HPKISFGSDS
     APHVISKKHS ANIPAGIFSA PILLPALCEL FEKHNALENL QAFISDNAKK IYTLDNLPSK
     KVRLSKKPFI VPTHTLCLNE KIAILREGET LSWNIQEIA
//