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 29-SEP-2021, entry version 111. DE RecName: Full=Dihydroorotase {ECO:0000256|HAMAP-Rule:MF_00220}; DE Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00220}; DE EC=3.5.2.3 {ECO:0000256|HAMAP-Rule:MF_00220}; 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; Eubacteriales; 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., Cerdeno-Tarraga A.M., RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A., RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., RA White B., Whithead S., Parkhill J.; RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain RT Hall A and comparative analysis of the clostridial genomes."; RL Genome Res. 17:1082-1092(2007). CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate CC to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368, ECO:0000256|HAMAP- CC Rule:MF_00220}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00220}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-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 pathway; CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000256|HAMAP- CC Rule:MF_00220}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC DHOase family. Class I DHOase subfamily. CC {ECO:0000256|ARBA:ARBA00010286, ECO:0000256|HAMAP-Rule:MF_00220}. 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 GeneID; 56881434; -. DR KEGG; cbh:CLC_3150; -. DR KEGG; cbo:CBO3239; -. DR PATRIC; fig|413999.7.peg.3218; -. DR HOGENOM; CLU_015572_1_2_9; -. DR OMA; SHYAKSY; -. 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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00220}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00220}; Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00220}; KW Reference proteome {ECO:0000313|Proteomes:UP000001986}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00220}. FT DOMAIN 49..392 FT /note="Amidohydro-rel" FT /evidence="ECO:0000259|Pfam:PF01979" FT REGION 60..62 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT REGION 294..295 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT ACT_SITE 280 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT METAL 58 FT /note="Zinc 1; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT METAL 60 FT /note="Zinc 1; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT METAL 149 FT /note="Zinc 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT METAL 149 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT METAL 176 FT /note="Zinc 2; via pros nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT METAL 213 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT METAL 280 FT /note="Zinc 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 92 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 253 FT /note="Substrate; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 284 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule: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 //