ID Q8FT40_COREF Unreviewed; 450 AA. AC Q8FT40; C8NP40; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 10-JUN-2026, entry version 152. 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}; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18541.1, ECO:0000313|Proteomes:UP000001409}; RN [1] {ECO:0000313|EMBL:BAC18541.1, ECO:0000313|Proteomes:UP000001409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395 RC {ECO:0000313|Proteomes:UP000001409}; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). 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 = 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:0000256|HAMAP-Rule:MF_00220}; 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 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; BA000035; BAC18541.1; -; Genomic_DNA. DR RefSeq; WP_006767731.1; NC_004369.1. DR AlphaFoldDB; Q8FT40; -. DR STRING; 196164.gene:10742152; -. DR KEGG; cef:CE1731; -. DR eggNOG; COG0044; Bacteria. DR HOGENOM; CLU_015572_1_0_11; -. DR OrthoDB; 9803027at2; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000001409; Chromosome. 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 Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1. DR HAMAP; MF_00220_B; PyrC_classI_B; 1. 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; NF006836; PRK09357.1-1; 1. DR NCBIfam; TIGR00857; pyrC_multi; 1. DR PANTHER; PTHR43668; ALLANTOINASE; 1. DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00220}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00220}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_00220}; Reference proteome {ECO:0000313|Proteomes:UP000001409}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00220}. FT DOMAIN 63..250 FT /note="Dihydroorotase catalytic" FT /evidence="ECO:0000259|Pfam:PF12890" FT ACT_SITE 320 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 75..77 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 107 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 167 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 167 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 194 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 293 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 320 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 324 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" FT BINDING 338..339 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220" SQ SEQUENCE 450 AA; 48518 MW; 56D9AACE1119A5C0 CRC64; MTVHDYPETG ALAPAAPGTL LITDVRVYGE GEPTNVLIRD GVIDSLDAPT SGEYDHTIDG GGGVLLPGFV DMHVHLREPG REDTETIATG SAAAAKGGFT AVFTMANTTP VMDQPLIAEG VWFKGQNVGL CDVHPVGSIT KGLEGRELTE FGMMARSEAR VRMFSDDGKC VDDPQVMRRA LEYAKGMDVL IAQHCEDHRM TEGASAHEGE NAARLGLRGW PRVAEESIVV RDAILARDYG NRVHICHAST EGTIELLRWA KGQGIPITAE VTPHHLILTD ERLKTYDGVN RVNPPLREER DTLALREALL DGTIDVVATD HAPHGSEDKC CEFENAKPGM LGLETSLSII ADTFVASGLA DWRFVAKVMS ERPAEITRLP GHGRPIAVGE PANLTIVDPG RTWTARGEEF ASKASNTPYE GMEFGAKVSH TILRGHVTCE NGNATIAYNA //