ID PYRC_BACMK Reviewed; 428 AA. AC A9VTC8; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 02-SEP-2026, entry version 99. DE RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00220}; DE Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00220}; DE EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00220}; GN Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00220}; GN OrderedLocusNames=BcerKBAB4_3715; OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=315730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBAB4; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., RA Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate CC to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate + H(+); 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:0000255|HAMAP-Rule:MF_00220}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00220}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00220}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP- CC Rule:MF_00220}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC DHOase family. Class I DHOase subfamily. {ECO:0000255|HAMAP- CC 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; CP000903; ABY44884.1; -; Genomic_DNA. DR RefSeq; WP_002088243.1; NC_010184.1. DR AlphaFoldDB; A9VTC8; -. DR SMR; A9VTC8; -. DR GeneID; 66266545; -. DR KEGG; bwe:BcerKBAB4_3715; -. DR eggNOG; COG0044; Bacteria. DR HOGENOM; CLU_015572_1_0_9; -. DR UniPathway; UPA00070; UER00117. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0004038; F:allantoinase activity; IEA:TreeGrafter. 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-UniRule. DR GO; GO:0006145; P:purine nucleobase catabolic process; IEA:TreeGrafter. DR CDD; cd01317; DHOase_IIa; 1. DR FunFam; 2.30.40.10:FF:000007; Dihydroorotase; 1. DR FunFam; 3.20.20.140:FF:000025; Dihydroorotase; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2. DR HAMAP; MF_00220_B; PyrC_classI_B; 1. DR InterPro; IPR013108; Amidohydro_3. DR InterPro; IPR004722; DHOase. DR InterPro; IPR050138; DHOase/Allantoinase_Hydrolase. DR InterPro; IPR024403; DHOase_cat. DR InterPro; IPR002195; Dihydroorotase_CS. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; NF006837; PRK09357.1-2; 1. DR NCBIfam; TIGR00857; pyrC_multi; 1. DR PANTHER; PTHR43668; ALLANTOINASE; 1. DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 1. DR Pfam; PF07969; Amidohydro_3; 1. DR Pfam; PF12890; DHOase; 1. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 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..428 FT /note="Dihydroorotase" FT /id="PRO_1000100071" FT ACT_SITE 304 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 59 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 61..63 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 93 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 178 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 277 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 304 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 308 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 322..323 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" SQ SEQUENCE 428 AA; 46487 MW; 241D4181B4761FB3 CRC64; MNYLFKNGRY MNAEGTIVAT DLLVQDGKIA KVAENITADN AEVIDVNGKL IAPGLVDVHV HLREPGGEHK ETIETGTLAA AKGGFTTICA MPNTRPVPDC KEHMEDLQKR IKEKAHVNVL PYGAITVRQA GSEMTDFETL KELGAFAFTD DGVGVQDASM MLAAMKRASK LNMAVVAHCE ENTLINKGCV HEGKFSEKHG LNGIPSVCES VHIARDILLA EAANCHYHVC HVSTKGSVRV IRDAKRAGIK VTAEVTPHHL VLCEDDIPSA DPNFKMNPPL RGKEDHAALI EGLLDGTIDM IATDHAPHTA EEKAQGIERA PFGITGFETA FPLLYTNLVK KGIITLEQLI QFLTEKPADT FGLEAGRLTE GRTADITIID LEQEEEIDPT TFLSKGKNTP FAGWKCQGWP VMTIVGGKIA WQKESALV //