ID   PYRC_HAHCH              Reviewed;         345 AA.
AC   Q2SCE3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=HCH_04992;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H.,
RA   Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H.,
RA   Park H.-S., Lee H.K., Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing
RT   an algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000155; ABC31681.1; -; Genomic_DNA.
DR   RefSeq; YP_436106.1; -.
DR   GeneID; 3842977; -.
DR   GenomeReviews; CP000155_GR; HCH_04992.
DR   KEGG; hch:HCH_04992; -.
DR   NMPDR; fig|349521.5.peg.4382; -.
DR   HOGENOM; Q2SCE3; -.
DR   OMA; Q2SCE3; IMPNLVP.
DR   BioCyc; HCHE349521:HCH_04992-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    345       Dihydroorotase.
FT                                /FTId=PRO_1000024015.
FT   METAL        13     13       Zinc 1 (By similarity).
FT   METAL        15     15       Zinc 1 (By similarity).
FT   METAL        99     99       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL        99     99       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       136    136       Zinc 2 (By similarity).
FT   METAL       174    174       Zinc 2 (By similarity).
FT   METAL       247    247       Zinc 1 (By similarity).
FT   MOD_RES      99     99       N6-carboxylysine (By similarity).
SQ   SEQUENCE   345 AA;  37661 MW;  25913E5A9141005F CRC64;
     MSDLVITRPD DWHLHLRDGD ALATTVPATA RLFSRAIVMP NLVPPVTHTA QAEAYRHRIL
     SHVPAGAAFD PLMTLYLTNN TSPEEIVAAR QSGIVYGCKL YPAGATTNSD AGVTDVANVF
     SVLEKMSDMG MPLLIHGEVV QADVDIFDRE KRFIDETLTP LTERFPNLKI VLEHITTRDA
     VEFVNQAGSN VGATITAHHL LYNRNHMLVG GIRPHFYCLP ILKRSEHQLA LRDAAASGSD
     RFFLGTDSAP HPKEKKEAAC GCAGCFTAPS ALELYAEAFD ELGALDKLEG FASLHGPTFY
     GLPINSGKVR LSKQEWTMPA SMALGDSSIV PFRAGETIRW KAELL
//