ID PYRC_EHRCJ Reviewed; 447 AA. AC Q3YRI2; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 28-JAN-2026, entry version 112. 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=Ecaj_0639; OS Ehrlichia canis (strain Jake). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=269484; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Jake; RX PubMed=16707693; DOI=10.1128/jb.01837-05; RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.; RT "The genome of the obligately intracellular bacterium Ehrlichia canis RT reveals themes of complex membrane structure and immune evasion RT strategies."; RL J. Bacteriol. 188:4015-4023(2006). 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; CP000107; AAZ68673.1; -; Genomic_DNA. DR RefSeq; WP_011304750.1; NC_007354.1. DR AlphaFoldDB; Q3YRI2; -. DR SMR; Q3YRI2; -. DR FunCoup; Q3YRI2; 267. DR STRING; 269484.Ecaj_0639; -. DR KEGG; ecn:Ecaj_0639; -. DR eggNOG; COG0044; Bacteria. DR HOGENOM; CLU_015572_1_0_5; -. DR InParanoid; Q3YRI2; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000000435; 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; 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..447 FT /note="Dihydroorotase" FT /id="PRO_0000325592" FT ACT_SITE 325 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 81 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 83..85 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 83 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 115 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 171 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 171 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 198 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 252 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 298 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 325 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 329 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 343..344 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" SQ SEQUENCE 447 AA; 49115 MW; 9B695F6620AEBE43 CRC64; MYKQSWKLLG RGQDADFTVA YINARIIDPE SKLDIIGSLL TKGDKIVDFG QDLFNNGIPS TIDEVVDCNN NILMPGLIDI HVHFREPGQE HKETIHTGSK SAAAGGVTTV VCQPNTIPTI SSIITAKYIK MRALESAYVN IEFYASITKP DNSLSDMALL KEAGAVGFTD DGMPVMNSLT MRQALSYSSM LDTVVAQHAE DLNLSNNGHI NEGTVSYELG LKGIPDISES IIVNRDIALM KNIKNVHYHI LHVSSQDSLN IIKQAKNQGL KVTCEVTPHH LTLTEQDVIT HGTLAKINPP LRTENDRLSM VEGLKNGIID CIATDHAPHE VNTKELPLDT AAFGIVGLET MLPISLELYH NGTISLIDLL ATLTYKPANI IKVPRGRIKK GFVADLIILD LNHEWTIDIL KFASKSKNSP FHNRKVKGKV LRTIVSGKTT YTAVRNI //