ID PYRC_CITK8 Reviewed; 347 AA. AC A8AI14; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 09-APR-2025, entry version 90. DE RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00219}; DE Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00219}; DE EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00219}; GN Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00219}; GN OrderedLocusNames=CKO_02001; OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=290338; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696; RG The Citrobacter koseri Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., RA Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate CC to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}. 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_00219}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00219}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00219}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP- CC Rule:MF_00219}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00219}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC DHOase family. Class II DHOase subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00219}. 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; CP000822; ABV13127.1; -; Genomic_DNA. DR RefSeq; WP_012132863.1; NC_009792.1. DR AlphaFoldDB; A8AI14; -. DR SMR; A8AI14; -. DR STRING; 290338.CKO_02001; -. DR MEROPS; M38.A02; -. DR GeneID; 45135970; -. DR KEGG; cko:CKO_02001; -. DR HOGENOM; CLU_041558_1_0_6; -. DR OrthoDB; 9808095at2; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000008148; Chromosome. DR GO; GO:0005829; C:cytosol; 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:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:TreeGrafter. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01294; DHOase; 1. DR FunFam; 3.20.20.140:FF:000006; Dihydroorotase; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR HAMAP; MF_00219; PyrC_classII; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR004721; DHOdimr. DR InterPro; IPR002195; Dihydroorotase_CS. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR00856; pyrC_dimer; 1. DR PANTHER; PTHR43137; DIHYDROOROTASE; 1. DR PANTHER; PTHR43137:SF1; DIHYDROOROTASE; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF001237; DHOdimr; 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; Reference proteome; KW Zinc. FT CHAIN 1..347 FT /note="Dihydroorotase" FT /id="PRO_1000024008" FT ACT_SITE 251 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 17 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 19..21 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 19 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 45 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 103 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 103 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 140 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 178 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 223 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 251 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 267 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT MOD_RES 103 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" SQ SEQUENCE 347 AA; 38731 MW; 9A1EEBF605745458 CRC64; MTAPSQVLKI RRPDDWHVHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVDAAIAYR QRILDAVPAG HDFTPLMTCY LTDTLDPDEL ERGFREGVFT AAKLYPANAT TNSSHGVTSV DTIMPVLERM EKLGMPLLVH GEVTHADIDI FDREARFIET VMEPLRQRLT ALKVVFEHIT TKDAAEYVRD GNELLAATIT PQHLMFNRNH MLVGGIRPHL YCLPILKRNV HQQALRELVA SGFSRAFLGT DSAPHARHRK ETSCGCAGCF NAPTALGSYA TVFEEMNALA HFEAFCSLNG PRFYGLSVNE TYVELVREEQ LVPESITLAD DSLVPFLGGE RVRWSVK //