AC MF_00220; DC Protein; auto c? TR HAMAP; MF_00220_B; -; 1; level=0 c? TR HAMAP; MF_00220_A; -; 1; level=0 XX Names: PyrC_classI XX ID PYRC DE RecName: Full=Dihydroorotase; DE Short=DHOase; DE EC=3.5.2.3; GN Name=pyrC; XX CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate CC to dihydroorotate. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions per subunit.; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 3/3. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC DHOase family. Class I DHOase subfamily. XX DR Pfam; PF01979; Amidohydro_1; 1; trigger=no DR NCBIfam; TIGR00857; PyrC_multi; 1; trigger=no DR PROSITE; PS00482; DIHYDROOROTASE_1; 1; trigger=no DR PROSITE; PS00483; DIHYDROOROTASE_2; 1; trigger=no XX KW Hydrolase KW Metal-binding KW Pyrimidine biosynthesis KW Zinc XX GO GO:0004151; F:dihydroorotase activity GO GO:0008270; F:zinc ion binding GO GO:0006221; P:pyrimidine nucleotide biosynthetic process XX FT From: PYRC_BACAN (Q81WF0) case FT BINDING 61..63 FT /ligand="substrate" FT Condition: H-x-R FT BINDING 322..323 FT /ligand="substrate" FT Condition: [FP]-G FT ACT_SITE 304 FT Condition: D FT BINDING 59 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: H FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: H FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: D FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: D FT BINDING 178 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: H FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: H FT BINDING 304 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: D FT BINDING 93 FT /ligand="substrate" FT Condition: N FT BINDING 277 FT /ligand="substrate" FT Condition: N FT BINDING 308 FT /ligand="substrate" FT Condition: H end case FT From: PYRC_PYRAB (Q9UXV6) case FT BINDING 59..61 FT /ligand="substrate" FT Optional; Condition: H-x-R FT BINDING 286..287 FT /ligand="substrate" FT Optional; Condition: [FPA]-G FT ACT_SITE 272 FT Condition: D FT BINDING 57 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: H FT BINDING 59 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: H FT BINDING 135 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: [KE] FT BINDING 135 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: [KE] FT BINDING 164 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: H FT BINDING 204 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: H FT BINDING 272 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Condition: D FT MOD_RES 135 FT /note="N6-carboxylysine" FT Optional; Condition: K FT BINDING 91 FT /ligand="substrate" FT Optional; Condition: N FT BINDING 276 FT /ligand="substrate" FT Optional; Condition: H end case XX case Size: 370-500; end case case Size: 380-480; end case Related: MF_00219; Template: Q81WF0; Q5SK67; O66990; Q5HGN1; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Classification into subfamilies was done according to PubMed:24332717. XX # Revision 1.41 2023/06/01 //