ID   PYRC_ARCFU              Reviewed;         403 AA.
AC   O28034;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=AF_2250;
OS   Archaeoglobus fulgidus.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=2234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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 2 subfamily.
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DR   EMBL; AE000782; AAB89007.1; -; Genomic_DNA.
DR   PIR; B69531; B69531.
DR   RefSeq; NP_071075.1; -.
DR   GeneID; 1485481; -.
DR   GenomeReviews; AE000782_GR; AF_2250.
DR   KEGG; afu:AF2250; -.
DR   NMPDR; fig|224325.1.peg.2236; -.
DR   TIGR; AF_2250; -.
DR   HOGENOM; O28034; -.
DR   OMA; O28034; YATDHAP.
DR   BioCyc; AFUL224325:AF_2250-MON; -.
DR   BRENDA; 3.5.2.3; 7576.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00220; -; 1.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR004722; DHOmult.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   ProDom; PD000518; DHOase; 1.
DR   TIGRFAMs; TIGR00857; pyrC_multi; 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    403       Dihydroorotase.
FT                                /FTId=PRO_0000147267.
FT   METAL        48     48       Zinc 1 (By similarity).
FT   METAL        50     50       Zinc 1 (By similarity).
FT   METAL       172    172       Zinc 2 (By similarity).
FT   METAL       211    211       Zinc 2 (By similarity).
FT   METAL       277    277       Zinc 1 (By similarity).
SQ   SEQUENCE   403 AA;  45559 MW;  7AF4E74CCA4624AF CRC64;
     MIRGKVFYKG EFVEAGIEVE NGRIKRIGKL VEGKEVKGVI LPAGIDVHVH LRDFAEKRKE
     TIETGTLSAL HGGICLVVDQ PNTKPPVDDA ETYFRRMGKA EKSVYVDYAL NLALTNSNHG
     KIGSIMRKIS ERYFVPAVGE VFIQHDSEDL QIDYETLSSV YKRFEGVVFT IHAEDPAYVA
     RGSPNFVFRR REAEVLAVER LVELGKFHFC HISTKDSAKE ILNSNSTYEV TPHHMLLSVE
     DYGRLGNLVN VNPPLRERED VEWLFRNFHR IDVLASDHAP HTLEDKEAGA SGFPGVETMY
     PLFVNLASKG YISFKTLVEK IASNPARIFG FKGYGEIEVG NYANFAVFDL KKVDEIRAER
     LHSKCGWTPF EGFEAVFPDK VYLRGKELLE NEMKAGNVLK KRV
//