ID PYRC_KLEP7 Reviewed; 348 AA. AC A6T7D6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 28-NOV-2012, entry version 37. DE RecName: Full=Dihydroorotase; DE Short=DHOase; DE EC=3.5.2.3; GN Name=pyrC; OrderedLocusNames=KPN78578_10460; ORFNames=KPN_01074; OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH OS 78578). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=272620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700721 / MGH 78578; RG The Klebsiella pneumonia Genome Sequencing Project; RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L- CC aspartate. CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 3/3. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the DHOase family. Type 1 subfamily. 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; CP000647; ABR76507.1; -; Genomic_DNA. DR RefSeq; YP_001334737.1; NC_009648.1. DR ProteinModelPortal; A6T7D6; -. DR SMR; A6T7D6; 5-347. DR STRING; A6T7D6; -. DR PRIDE; A6T7D6; -. DR GeneID; 5341622; -. DR GenomeReviews; CP000647_GR; KPN78578_10460. DR KEGG; kpn:KPN_01074; -. DR PATRIC; 20456428; VBIKlePne13394_1102. DR eggNOG; COG0418; -. DR HOGENOM; HOG000256259; -. DR KO; K01465; -. DR OMA; FEHITTE; -. DR ProtClustDB; PRK05451; -. DR UniPathway; UPA00070; UER00117. DR GO; GO:0004151; F:dihydroorotase activity; IEA:EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR HAMAP; MF_00219; PyrC_type1; 1; -. DR InterPro; IPR006680; Amidohydro_1. DR InterPro; IPR004721; DHOdimr. DR InterPro; IPR002195; Dihydroorotase_CS. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF001237; DHOdimr; 1. DR TIGRFAMs; TIGR00856; pyrC_dimer; 1. DR PROSITE; PS00482; DIHYDROOROTASE_1; FALSE_NEG. DR PROSITE; PS00483; DIHYDROOROTASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; KW Zinc. FT CHAIN 1 348 Dihydroorotase. FT /FTId=PRO_1000024020. FT METAL 17 17 Zinc 1 (By similarity). FT METAL 19 19 Zinc 1 (By similarity). FT METAL 103 103 Zinc 1; via carbamate group (By FT similarity). FT METAL 103 103 Zinc 2; via carbamate group (By FT similarity). FT METAL 140 140 Zinc 2 (By similarity). FT METAL 178 178 Zinc 2 (By similarity). FT METAL 251 251 Zinc 1 (By similarity). FT MOD_RES 103 103 N6-carboxylysine (By similarity). SQ SEQUENCE 348 AA; 38821 MW; 2B841BB50B30506D CRC64; MTAQSQVLKI RRPDDWHIHL RDDDMLKTVV PYTSEFYGRA IVMPNLVPPV TTVAAAIAYR QRIMDAVPAG HDFTPLMTCY LTDSLDPAEL ERGFNEGVFT AAKLYPANAT TNSSHGVTST DAIMPVLERM EKLGMPLLVH GEVTHAEIDI FDREARFIET VMEPLRQRLP GLKVVFEHIT TKDAAEYVRD GNELLAATIT PQHLMFNRNH MLVGGIRPHL YCLPVLKRNI HQQALRELVA SGFSRAFLGT DSAPHARHRK EASCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSLNG PRFYGLPVNE SYVELVREET TVVDSIALPN DTLVPFLAGE TVRWTVKK //