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 30-NOV-2016, entry version 90. DE RecName: Full=Dihydroorotase {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00329264}; DE Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00220}; DE EC=3.5.2.3 {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00329238}; 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 -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L- CC aspartate. {ECO:0000256|HAMAP-Rule:MF_00220, CC ECO:0000256|SAAS:SAAS00329237}. 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:SAAS00393543}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00220, CC ECO:0000256|SAAS:SAAS00329235}. CC -!- SIMILARITY: Belongs to the DHOase family. Type 2 subfamily. CC {ECO:0000256|SAAS:SAAS00571224}. 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; 19368567; VBICloBot22612_3218. DR HOGENOM; HOG000219142; -. DR KO; K01465; -. DR OMA; FAMANTF; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000001986; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004038; F:allantoinase activity; IBA:GO_Central. DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00220_B; PyrC_type2_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; 2. DR SUPFAM; SSF51556; SSF51556; 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 {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:SAAS00470782}; KW Reference proteome {ECO:0000313|Proteomes:UP000001986}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00460808}. FT DOMAIN 49 392 Amidohydro-rel. {ECO:0000259|Pfam: FT PF01979}. FT METAL 58 58 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_00220}. FT METAL 60 60 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_00220}. FT METAL 176 176 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00220}. FT METAL 213 213 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00220}. FT METAL 280 280 Zinc 1. {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 //