ID PYRC_AZOSB Reviewed; 344 AA. AC A1K3T5; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 16-JUN-2009, entry version 20. DE RecName: Full=Dihydroorotase; DE Short=DHOase; DE EC=3.5.2.3; GN Name=pyrC; OrderedLocusNames=azo0873; OS Azoarcus sp. (strain BH72). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Azoarcus. OX NCBI_TaxID=62928; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17057704; DOI=10.1038/nbt1243; RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.; RT "Complete genome of the mutualistic, N2-fixing grass endophyte RT Azoarcus sp. strain BH72."; RL Nat. Biotechnol. 24:1385-1391(2006). 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; UMP from HCO(3)(-): step 3/6. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the DHOase family. Type 1 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM406670; CAL93490.1; -; Genomic_DNA. DR RefSeq; YP_932377.1; -. DR GeneID; 4606619; -. DR GenomeReviews; AM406670_GR; azo0873. DR KEGG; azo:azo0873; -. DR OMA; A1K3T5; IMPNLVP. DR GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP. DR GO; GO:0019856; P:pyrimidine base biosynthetic process; IEA:InterPro. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00219; -; 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; 1. DR PROSITE; PS00483; DIHYDROOROTASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; KW Zinc. FT CHAIN 1 344 Dihydroorotase. FT /FTId=PRO_0000325569. FT METAL 13 13 Zinc 1 (By similarity). FT METAL 15 15 Zinc 1 (By similarity). FT METAL 99 99 Zinc 1; via carbamate group (By FT similarity). FT METAL 99 99 Zinc 2; via carbamate group (By FT similarity). FT METAL 136 136 Zinc 2 (By similarity). FT METAL 174 174 Zinc 2 (By similarity). FT METAL 247 247 Zinc 1 (By similarity). FT MOD_RES 99 99 N6-carboxylysine (By similarity). SQ SEQUENCE 344 AA; 37002 MW; D7B70D3E29E5EDFA CRC64; MQSITFTRPD DWHLHVRDGA ALAAVVPHTA ERFGRALIMP NLRPPVTTTA QALAYRDRIR AAVPAGLAFE PLMSLYLTDN TAPDEIERAR ASGAVIAAKL YPAGATTNSD AGVTAIDKIY PVLERMEACG LVLCVHGEVT GGEVDVFDRE RVFMEKILSP LVRRFPALKV VFEHITTAEA AQFVRAAGAN VAATVTAHHL LLNRNAIFAG GIRPHHYCLP VLKRETHRVA LVEAVTSGNP RFFLGTDSAP HARSTKEAAC GCAGCYTAHA GIELYAEVFD AAGALERLEA FASLNGPAFY GLAPNADKIT LVRESWSVPA GFPYLDDDPL VPLRAGESVG WRLA //