ID A5I6W9_CLOBO Unreviewed; 396 AA. AC A5I6W9; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 02-OCT-2007, entry version 5. DE Dihydroorotase (EC 3.5.2.3). GN Name=pyrC; ORFNames=CBO3239; OS Clostridium botulinum A str. ATCC 3502. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=413999; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 3502; RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T., RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., RA Paul C.J., Ivens A., Wells-Bennik M.H., Davis I.J., RA Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T., RA Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., RA Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., RA Sanders M., Simmonds M., White B., Whithead S., Parkhill J.; RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum RT strain Hall A and comparative analysis of the clostridial genomes."; RL Genome Res. 17:1082-1092(2007). 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: Nucleotide biosynthesis; UMP biosynthesis; UMP from CC HCO(3)(-): step 3. CC -!- SIMILARITY: Belongs to the DHOase family. CC -!- SIMILARITY: Belongs to the DHOase family. Type 2 subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM412317; CAL84801.1; -; Genomic_DNA. DR RefSeq; YP_001255729.1; -. DR GeneID; 5187851; -. DR InterPro; IPR006680; Amidohydro_1. DR InterPro; IPR005847; DHOase. DR InterPro; IPR004722; DHOmult. DR InterPro; IPR002195; Dihydroorotase. DR Pfam; PF01979; Amidohydro_1; 1. DR ProDom; PD000518; DHOase; 1. DR TIGRFAMs; TIGR00857; pyrC_multi; 1. DR PROSITE; PS00482; DIHYDROOROTASE_1; UNKNOWN_1. DR PROSITE; PS00483; DIHYDROOROTASE_2; 1. PE 3: Inferred from homology; KW Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc. SQ SEQUENCE 396 AA; 44626 MW; BB5E0FD209158EE4 CRC64; MNELLIKNVN IIDWCQNFHG DVYIKNGIIE ELGKDLNKNC EIFDGRGLTL LPSFIDMHAH FRDPGFTYKE DILTGSRAAV KGGYTMVNLM ANTKPICSSN KEVEYVLEKG KEIGLVDIHQ CMSITKDFSG DDISHLDSID KKVKIISEDG KDVMNTRVLI EAMFKAKEKD LIVMCHSEEH DVTNLDTRLS ENLMTWRNIA LSEFTDCKVH IAHVSTKESM EYIKNAKKKG LKVTCEVAPH HIALTNKIFY RVNPPLREEE DIKVLIEAIK EDLVDCIGTD HAPHSKEDKL KGSPGISGIE TSFSTCYTKL VHNNHISLSK LSKIMSKNPA DILGVNNGEI KIGREADLVL VDTKEEYKVK SEEFHSKGKN TPMDGMYLKG RIKVTFKAGC IVYSEF //