ID PYRC_BACP2 Reviewed; 428 AA. AC A8FD15; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 02-SEP-2026, entry version 96. 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=BPUM_1449; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=315750; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). 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; CP000813; ABV62132.1; -; Genomic_DNA. DR RefSeq; WP_012009895.1; NC_009848.4. DR AlphaFoldDB; A8FD15; -. DR SMR; A8FD15; -. DR STRING; 315750.BPUM_1449; -. DR PaxDb; 315750-BPUM_1449; -. DR GeneID; 23399395; -. DR KEGG; bpu:BPUM_1449; -. DR eggNOG; COG0044; Bacteria. DR HOGENOM; CLU_015572_1_0_9; -. DR OrthoDB; 9765462at2; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000001355; 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; NF006837; PRK09357.1-2; 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; Metal-binding; Pyrimidine biosynthesis; Reference proteome; KW Zinc. FT CHAIN 1..428 FT /note="Dihydroorotase" FT /id="PRO_1000058653" 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; 46993 MW; B50A9168280389E2 CRC64; MSYLIKNGFI LTSTGEKVQQ DIRVEGEVIQ AIGHLEREDG EEVIDAKGLF VSPGLIDLHV HLREPGGEKK ETIETGSKAA ARGGYTTIAA MPNTRPVPDT KEQMEWLMNR IEETSSVRVL PYASITTRQI GEEMTDFAAL KEAGAFAFTD DGVGIQTAGM MYEAMKKAAS LDQAIVAHCE DNSLIYGGCV HEGEFSKANG LNGIPSICES VHIARDVLLA EAANCHYHVC HISTKESVRV VRDAKKAGIR VTAEVSPHHL LLCDADIPGL DTNYKMNPPL RGKEDREALI EGLLDGTIDF IATDHAPHTE EEKNETMQRA PFGIVGLETA FPLLYTRFVK TGEWTLKELV DYMTIKPAEA FSLPYGKLEK GQIADITLID LNKEMAIDKK SFLSKGQNTP FDKLTVSGWP VMTLASGKVV YEEGRLVK //