ID   PYRC_ACIAD              Reviewed;         344 AA.
AC   Q6FD29;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=ACIAD1150;
OS   Acinetobacter sp. (strain ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG68030.1; -; Genomic_DNA.
DR   RefSeq; YP_045852.1; -.
DR   GeneID; 2879564; -.
DR   GenomeReviews; CR543861_GR; ACIAD1150.
DR   KEGG; aci:ACIAD1150; -.
DR   NMPDR; fig|62977.3.peg.65; -.
DR   HOGENOM; Q6FD29; -.
DR   OMA; Q6FD29; IMPNLVP.
DR   BioCyc; ASP62977:ACIAD1150-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; IPR006992; Amidohydro_2.
DR   InterPro; IPR004721; DHOdimr.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   Pfam; PF04909; Amidohydro_2; 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    344       Dihydroorotase.
FT                                /FTId=PRO_1000024007.
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   344 AA;  38867 MW;  DE11304473479E6E CRC64;
     MDTITLLQPD DWHAHLRDGL ALKRTVPDLA QQFARAICMP NLVPPVKTVD EAEAYRERIM
     AHVPEGVHFD PRMVLYFTDH TSPSEVKKIK DSAHVNAIKL YPAGATTNSD NGVSDIRKVY
     AVIEQLEEHQ VPLLLHGEVT HHHVDIFDRE KRFLDEVLSP LLKQFPKLKL VLEHITTSEA
     AHFVLEQDRN VAATITPQHL LFNRNDMLVG GIKPHFYCLP ILKRQTHQQT LIEVATSGNP
     KFFLGTDSAP HSKNAKENAC GCAGCYSAPT AIELYAQAFD QVNKIERLEG FASHFGADFY
     GLPRNTNTIT LVKEDQIIPE QLDYLDDEKI IPLYAGKTIQ WRKV
//