ID A3PBU3_PROM0 Unreviewed; 349 AA. AC A3PBU3; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 04-NOV-2026, entry version 120. DE RecName: Full=Dihydroorotase {ECO:0000256|ARBA:ARBA00012860, ECO:0000256|HAMAP-Rule:MF_00219}; DE Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00219}; DE EC=3.5.2.3 {ECO:0000256|ARBA:ARBA00012860, ECO:0000256|HAMAP-Rule:MF_00219}; GN Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00219}; GN OrderedLocusNames=P9301_05951 {ECO:0000313|EMBL:ABO17218.1}; OS Prochlorococcus marinus (strain MIT 9301). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO17218.1, ECO:0000313|Proteomes:UP000001430}; RN [1] {ECO:0000313|EMBL:ABO17218.1, ECO:0000313|Proteomes:UP000001430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO17218.1, RC ECO:0000313|Proteomes:UP000001430}; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate CC to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368, ECO:0000256|HAMAP- CC 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:0000256|HAMAP-Rule:MF_00219, CC ECO:0000256|RuleBase:RU003440}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00219, ECO:0000256|RuleBase:RU003440}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00219, CC ECO:0000256|RuleBase:RU003440}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 3/3. CC {ECO:0000256|ARBA:ARBA00004880, ECO:0000256|HAMAP-Rule:MF_00219, CC ECO:0000256|RuleBase:RU003440}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00219}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC DHOase family. Class II DHOase subfamily. CC {ECO:0000256|ARBA:ARBA00005631, ECO:0000256|HAMAP-Rule:MF_00219, CC ECO:0000256|RuleBase:RU003440}. 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; CP000576; ABO17218.1; -; Genomic_DNA. DR RefSeq; WP_011862585.1; NC_009091.1. DR AlphaFoldDB; A3PBU3; -. DR STRING; 167546.P9301_05951; -. DR MEROPS; M38.A02; -. DR KEGG; pmg:P9301_05951; -. DR eggNOG; COG0418; Bacteria. DR HOGENOM; CLU_041558_1_0_3; -. DR OMA; AACAYRD; -. DR OrthoDB; 9808095at2; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000001430; 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 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00219}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00219}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_00219}; Reference proteome {ECO:0000313|Proteomes:UP000001430}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00219}. FT DOMAIN 11..306 FT /note="Amidohydrolase-related" FT /evidence="ECO:0000259|Pfam:PF01979" FT ACT_SITE 245 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT BINDING 15..17 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT BINDING 41 FT /ligand="substrate" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00219" FT BINDING 136 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT BINDING 136 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT BINDING 217 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT BINDING 245 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT BINDING 249 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT BINDING 260 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" FT MOD_RES 99 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219" SQ SEQUENCE 349 AA; 39638 MW; 1816077F7079A8CF CRC64; MKTLTIIKPD DWHLHLREGL VLKNIIHFTS EYFGRAIVMP NTKVPITSIK SAISYKKSII EALPESSKFK PLMTMYLTDE TDKGELINGF KNNVFFAAKL YPANATTNSS HGVRKIENLY KIFESMQDSG MPLLIHGEVT DSEVDVFDRE EVFIDKELSQ ITKRFPKLKI VLEHITTSYA VNFVKENNIG ATITPHHLHI NRNAMFFGGL NSDFYCLPVA KRENNRLALR KAATSGEKCF FLGTDSAPHL RKWKAFCGCA GIFNSPVAIE SYLTVFEEED ALDNFEKFAS LNGPNFYNVP PNKEKLKLVS RPNKIKEFID VIQEKNTVGQ IKPFHAGETL QWQVEGKLI //