ID   PYRC_BACCL              Reviewed;         427 AA.
AC   P46538;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2008, entry version 58.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC;
OS   Bacillus caldolyticus.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 405 / IFO 15313 / YP-T;
RX   MEDLINE=94282293; PubMed=7516791;
RA   Ghim S.Y., Nielsen P., Neuhard J.;
RT   "Molecular characterization of pyrimidine biosynthesis genes from the
RT   thermophile Bacillus caldolyticus.";
RL   Microbiology 140:479-491(1994).
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; X73308; CAA51737.1; -; Genomic_DNA.
DR   PIR; I40167; I40167.
DR   HSSP; P81006; 1GKR.
DR   MEROPS; M38.972; -.
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   Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
FT   CHAIN         1    427       Dihydroorotase.
FT                                /FTId=PRO_0000147227.
FT   METAL        60     60       Zinc 1 (By similarity).
FT   METAL        62     62       Zinc 1 (By similarity).
FT   METAL       142    142       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL       142    142       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       179    179       Zinc 2 (By similarity).
FT   METAL       232    232       Zinc 2 (By similarity).
FT   METAL       305    305       Zinc 1 (By similarity).
FT   MOD_RES     142    142       N6-carboxylysine (By similarity).
SQ   SEQUENCE   427 AA;  46048 MW;  759A2AA99F733F4E CRC64;
     MGVWLKNGMS FNKDGELMRT HIKIEHGTIA AILYEQPLEA NEDVIDVGGR LIVPGLIDLH
     VHLREPGGEA KETIETGTLA AAKGGFTTVA AMPNTNPAPD RKEQMEWLQA RIRETARVNV
     LPYAAITIGQ KGEELTDFAA LKEAGAFAFT DDGVGVQSAG MMFEAMKQAA ALDMAIVAHC
     EDDTLTNGGA VHDGEFARRY GLRGIPSVCE AVHIARDVLL AEAAGCHYHV CHISTKESVR
     VVRDAKRAGI RVTAEVTPHH LLLCDEDIPG LDANYKMNPP LRSREDRDAL IEGLLDGTID
     FIATDHAPHT AAEKAKGIEA APFGIVGLET AFPLLYTHFV KTGVFTLKQL VDWLTIKPAQ
     CFGLKAGRLA VGAPADIAVI DLETEEAIDP ETFASKGKNT PFAGWVCQGW PVMTFVGGTL
     VWEKGRA
//