ID PYRC_ANAPZ Reviewed; 447 AA. AC Q2GL89; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 28-JAN-2026, entry version 102. 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=APH_0245; OS Anaplasma phagocytophilum (strain HZ). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Anaplasmataceae; Anaplasma; phagocytophilum group. OX NCBI_TaxID=212042; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HZ; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(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; CP000235; ABD43938.1; -; Genomic_DNA. DR RefSeq; WP_011450385.1; NC_007797.1. DR AlphaFoldDB; Q2GL89; -. DR SMR; Q2GL89; -. DR STRING; 212042.APH_0245; -. DR PaxDb; 212042-APH_0245; -. DR EnsemblBacteria; ABD43938; ABD43938; APH_0245. DR GeneID; 92747549; -. DR KEGG; aph:APH_0245; -. DR eggNOG; COG0044; Bacteria. DR HOGENOM; CLU_015572_1_0_5; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000001943; 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_0000325581" FT ACT_SITE 328 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 86..88 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 86 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 118 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 301 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 328 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 332 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" FT BINDING 346..347 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220" SQ SEQUENCE 447 AA; 48529 MW; B09D15AE95C66DC9 CRC64; MVSERQTWSL LQGGQCNEYT VAYINARIID PASGTDYKGY LLTRGKEILD FGPGFFDPNG AAFAASEVVD CNGHVLMPGI VDLHVHLREP GGEHKETVDT GSRAAAAGGV TTVVCQPNTI PRLENVLVAK YLKMRALESS CVNIEFYGAV TKSDGELCDM ASLKDAGALG FTDDGLPVMN ALYMKRAFEY AQDLDVVVAQ HAEDCNLSDG GCINEGLVSR ELGLKGIPDI SESIMVSRDI QLLREVPGAH YHVLHISTKK ALDIVRAAKR EGLRVTCEVT PHHFLLNESA VLEHGTMAKM NPPLRTEEDR LSMISGLEDG TIDCIATDHA PHAAQEKTRP ISCCAFGIVG LETLLPLSLE LYHNAGMSLM DVLSKLTSKP AEIVRLPRGK IAKGLVADLV IFDLEHVWTI DTAKFSSKSK NSPFQGRKVK GKVLRTVVSG KTVYRAE //