ID   PYRC_BUCAP              Reviewed;         349 AA.
AC   Q8K9L2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 48.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=BUsg_322;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67876.1; -; Genomic_DNA.
DR   RefSeq; NP_660665.1; -.
DR   HSSP; P05020; 1J79.
DR   GeneID; 1005527; -.
DR   GenomeReviews; AE013218_GR; BUsg_322.
DR   KEGG; bas:BUsg322; -.
DR   HOGENOM; Q8K9L2; -.
DR   BioCyc; BAPH198804:BUSG322-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; IPR006680; Amidohydro_1.
DR   InterPro; IPR004721; DHOdimr.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   Pfam; PF01979; Amidohydro_1; 1.
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    349       Dihydroorotase.
FT                                /FTId=PRO_0000147204.
FT   METAL        17     17       Zinc 1 (By similarity).
FT   METAL        19     19       Zinc 1 (By similarity).
FT   METAL       103    103       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL       103    103       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       140    140       Zinc 2 (By similarity).
FT   METAL       178    178       Zinc 2 (By similarity).
FT   METAL       252    252       Zinc 1 (By similarity).
FT   MOD_RES     103    103       N6-carboxylysine (By similarity).
SQ   SEQUENCE   349 AA;  40557 MW;  03D6ADFD7BCE0BC5 CRC64;
     MSKFLKKIKI IKPDDWHVHL RDNEILKKVS QYTGTFYKRA IIMPNLEEPI TNCFRSISYR
     RRILNSMTPN TAFQPLMICY LTEKTSPEEL QQGFFKKIFV GAKLYPHCST TNSKYGIKNI
     NNIYHLFNIM EKIKMPLLIH GEENNLNIDI YDREAKFIEN TLKPLRKKFP ELKIILEHIT
     TEEAISYIEE CNSSYLAGTI TPHHLMLNRN NMFIDGIQPH LYCLPLLKRK KHQIALRNVI
     SSGSKNFFLG SDTAPHFHKN KINTFGCAGI FNAPSSLLCY VSVFEEMNAL QHFQSFCSEN
     GPNFYNMPIN KETITLVKKP HKILEKINIG KNIIVPFLAG KRLDWSIEK
//