ID PYRC_HAHCH Reviewed; 345 AA. AC Q2SCE3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 09-APR-2025, entry version 98. 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=HCH_04992; OS Hahella chejuensis (strain KCTC 2396). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Oceanospirillales; Hahellaceae; Hahella. OX NCBI_TaxID=349521; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 2396; RX PubMed=16352867; DOI=10.1093/nar/gki1016; RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., RA Oh T.K., Kim J.F.; RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an RT algicidal agent."; RL Nucleic Acids Res. 33:7066-7073(2005). 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; CP000155; ABC31681.1; -; Genomic_DNA. DR RefSeq; WP_011398746.1; NC_007645.1. DR AlphaFoldDB; Q2SCE3; -. DR SMR; Q2SCE3; -. DR STRING; 349521.HCH_04992; -. DR KEGG; hch:HCH_04992; -. DR eggNOG; COG0418; Bacteria. DR HOGENOM; CLU_041558_1_0_6; -. DR OrthoDB; 9808095at2; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000000238; 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..345 FT /note="Dihydroorotase" FT /id="PRO_1000024015" FT ACT_SITE 247 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 15..17 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 41 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 99 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 99 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 136 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 136 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 219 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 251 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 263 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT MOD_RES 99 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" SQ SEQUENCE 345 AA; 37661 MW; 25913E5A9141005F CRC64; MSDLVITRPD DWHLHLRDGD ALATTVPATA RLFSRAIVMP NLVPPVTHTA QAEAYRHRIL SHVPAGAAFD PLMTLYLTNN TSPEEIVAAR QSGIVYGCKL YPAGATTNSD AGVTDVANVF SVLEKMSDMG MPLLIHGEVV QADVDIFDRE KRFIDETLTP LTERFPNLKI VLEHITTRDA VEFVNQAGSN VGATITAHHL LYNRNHMLVG GIRPHFYCLP ILKRSEHQLA LRDAAASGSD RFFLGTDSAP HPKEKKEAAC GCAGCFTAPS ALELYAEAFD ELGALDKLEG FASLHGPTFY GLPINSGKVR LSKQEWTMPA SMALGDSSIV PFRAGETIRW KAELL //