ID   PYRC_IDILO              Reviewed;         344 AA.
AC   Q5QWC6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=IL0362;
OS   Idiomarina loihiensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=135577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-TR / ATCC BAA-735 / DSM 15497;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S.,
RA   Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(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.
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DR   EMBL; AE017340; AAV81205.1; -; Genomic_DNA.
DR   RefSeq; YP_154754.1; -.
DR   GeneID; 3172502; -.
DR   GenomeReviews; AE017340_GR; IL0362.
DR   KEGG; ilo:IL0362; -.
DR   NMPDR; fig|283942.3.peg.446; -.
DR   HOGENOM; Q5QWC6; -.
DR   OMA; Q5QWC6; IMPNLVP.
DR   BioCyc; ILOI283942:IL0362-MON; -.
DR   BRENDA; 3.5.2.3; 280818.
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    344       Dihydroorotase.
FT                                /FTId=PRO_1000024018.
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;  37656 MW;  0524427E85F4BD41 CRC64;
     MQSLTIPRPD DWHLHLRDGA MLQTTVPATA AVFHRAVVMP NLVPPVTTVA AAMEYRERIL
     AEIPAGMSFN PLMALYLTAD TTPAEIAEAA ANEHVIGFKL YPSGATTNSA AGVKSVEALA
     PVLAAMQEHQ VPLLVHGEVT DSDIDIFDRE RVFIERHLIP ITERFPQLKL VLEHITTADA
     VKFVENANSN VAATMTPQHL LMNRNDLLVG GIRPHNYCLP ILKRRSHQQA LQQAALSGNP
     KFFLGTDSAP HVQANKETAC GCAGCYSAPA AIELYAEFFS QHNALDKLAN FASVFGADFY
     QLPRNTETIE LVQQPWTVAE TVDTATGPMV PYWAGSDLQW KLRG
//