ID Q6FPD8_CANGA Unreviewed; 358 AA. AC Q6FPD8; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 116. DE RecName: Full=dihydroorotase {ECO:0000256|ARBA:ARBA00012860}; DE EC=3.5.2.3 {ECO:0000256|ARBA:ARBA00012860}; GN OrderedLocusNames=CAGL0J04598g {ECO:0000313|CGD:CAL0133520, GN ECO:0000313|EMBL:CAG60855.1}; OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces. OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG60855.1, ECO:0000313|Proteomes:UP000002428}; RN [1] {ECO:0000313|EMBL:CAG60855.1, ECO:0000313|Proteomes:UP000002428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS RC 138 {ECO:0000313|Proteomes:UP000002428}; RX PubMed=15229592; DOI=10.1038/nature02579; RG Genolevures; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L., RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 3/3. CC {ECO:0000256|ARBA:ARBA00004880}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC DHOase family. Class II DHOase subfamily. CC {ECO:0000256|ARBA:ARBA00005631}. 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; CR380956; CAG60855.1; -; Genomic_DNA. DR AlphaFoldDB; Q6FPD8; -. DR FunCoup; Q6FPD8; 286. DR STRING; 284593.Q6FPD8; -. DR KEGG; cgr:2889447; -. DR CGD; CAL0133520; CAGL0J04598g. DR VEuPathDB; FungiDB:CAGL0J04598g; -. DR eggNOG; KOG2902; Eukaryota. DR HOGENOM; CLU_041558_0_0_1; -. DR InParanoid; Q6FPD8; -. DR OMA; TLHHISM; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000002428; Chromosome J. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:EnsemblFungi. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01294; DHOase; 1. DR FunFam; 3.20.20.140:FF:000041; Dihydroorotase, variant; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR HAMAP; MF_00219; PyrC_classII; 1. 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 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}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}; KW Reference proteome {ECO:0000313|Proteomes:UP000002428}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. SQ SEQUENCE 358 AA; 39700 MW; 9098C15A8E020AF5 CRC64; MSEIDLGITC DMHVHVREGD MCELVTPSIR DGGVSVCYVM PNLQPPITTL DRVVAYKKKL QELAPETTFL MSFYLSRDLT PELIHEAARA KAIQGVKCYP AGVTTNSSAG VDPNDFTAFY PIFKAMEEEH LVLNLHGEKP SVAKEDIHVL NAEESFLPAL KKLHTDFPNL KIILEHCTTE AAVNAIEEIN KNVTNISDVK VAATLTAHHL YLTIDDWAGN PINFCKPVAK LPRDRRALVA AATSGKPYFF FGSDSAPHPL EMKGRHIGVC AGVYTQSLAI PYVAQVFHEA NAMDKLKGFV SDFGLAFYDV PQSEIRSTQH AILYKQEQTV QDTIQGKNNL KVALFKPGEK LDFSVKWQ //