ID A5I6W9_CLOBH Unreviewed; 396 AA. AC A5I6W9; A7G854; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 07-NOV-2018, entry version 100. DE RecName: Full=Dihydroorotase {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00853100}; DE Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00220}; DE EC=3.5.2.3 {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00964835}; GN Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00220, GN ECO:0000313|EMBL:CAL84801.1}; GN OrderedLocusNames=CBO3239 {ECO:0000313|EMBL:CAL84801.1}; OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441771 {ECO:0000313|Proteomes:UP000001986}; RN [1] {ECO:0000313|EMBL:CAL84801.1, ECO:0000313|Proteomes:UP000001986} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger] RC {ECO:0000313|Proteomes:UP000001986}; RX PubMed=17519437; DOI=10.1101/gr.6282807; RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., 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.J., 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 -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl CC aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00220, CC ECO:0000256|SAAS:SAAS00925093}. CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L- CC aspartate. {ECO:0000256|HAMAP-Rule:MF_00220, CC ECO:0000256|SAAS:SAAS00964837}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00220}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00220}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 3/3. CC {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00964833}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases CC superfamily. DHOase family. Class I DHOase subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00964840}. 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; WP_012048209.1; NC_009698.1. DR RefSeq; YP_001255729.1; NC_009495.1. DR RefSeq; YP_001388969.1; NC_009698.1. DR ProteinModelPortal; A5I6W9; -. DR GeneID; 5187851; -. DR GeneID; 5401636; -. DR KEGG; cbh:CLC_3150; -. DR KEGG; cbo:CBO3239; -. DR PATRIC; fig|413999.7.peg.3218; -. DR HOGENOM; HOG000219142; -. DR KO; K01465; -. DR OMA; FGCESIE; -. DR BioCyc; CBOT441771:G1G97-3044-MONOMER; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000001986; Chromosome. DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01317; DHOase_IIa; 1. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00220_B; PyrC_classI_B; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR004722; DHOase. DR InterPro; IPR002195; Dihydroorotase_CS. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; SSF51338; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR PROSITE; PS00482; DIHYDROOROTASE_1; 1. DR PROSITE; PS00483; DIHYDROOROTASE_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001986}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00220, KW ECO:0000256|SAAS:SAAS00470770, ECO:0000313|EMBL:CAL84801.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00220, KW ECO:0000256|SAAS:SAAS00470804}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00220, KW ECO:0000256|SAAS:SAAS01000213}; KW Reference proteome {ECO:0000313|Proteomes:UP000001986}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00964841}. FT DOMAIN 49 392 Amidohydro-rel. {ECO:0000259|Pfam: FT PF01979}. FT REGION 60 62 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00220}. FT REGION 294 295 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00220}. FT ACT_SITE 280 280 {ECO:0000256|HAMAP-Rule:MF_00220}. FT METAL 58 58 Zinc 1; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00220}. FT METAL 60 60 Zinc 1; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00220}. FT METAL 149 149 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_00220}. FT METAL 149 149 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00220}. FT METAL 176 176 Zinc 2; via pros nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00220}. FT METAL 213 213 Zinc 2; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00220}. FT METAL 280 280 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_00220}. FT BINDING 92 92 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00220}. FT BINDING 253 253 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00220}. FT BINDING 284 284 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00220}. 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 //