ID PYRC_ANADE Reviewed; 433 AA. AC Q2IIB0; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 02-SEP-2008, entry version 22. DE RecName: Full=Dihydroorotase; DE Short=DHOase; DE EC=3.5.2.3; GN Name=pyrC; OrderedLocusNames=Adeh_1619; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-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; UMP from HCO(3)(-): step 3/6. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the DHOase family. Type 2 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; CP000251; ABC81392.1; -; Genomic_DNA. DR RefSeq; YP_464829.1; -. DR GeneID; 3888118; -. DR GenomeReviews; CP000251_GR; Adeh_1619. DR KEGG; ade:Adeh_1619; -. DR HOGENOM; Q2IIB0; -. DR BioCyc; ADEH290397:ADEH_1619-MON; -. DR GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00220; -; 1. DR InterPro; IPR006680; Amidohydro_1. DR InterPro; IPR004722; DHOmult. DR InterPro; IPR002195; Dihydroorotase_CS. DR Pfam; PF01979; Amidohydro_1; 1. DR TIGRFAMs; TIGR00857; pyrC_multi; 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 1 433 Dihydroorotase. FT /FTId=PRO_0000325580. FT METAL 63 63 Zinc 1 (By similarity). FT METAL 65 65 Zinc 1 (By similarity). FT METAL 145 145 Zinc 1; via carbamate group (By FT similarity). FT METAL 145 145 Zinc 2; via carbamate group (By FT similarity). FT METAL 182 182 Zinc 2 (By similarity). FT METAL 235 235 Zinc 2 (By similarity). FT METAL 310 310 Zinc 1 (By similarity). FT MOD_RES 145 145 N6-carboxylysine (By similarity). SQ SEQUENCE 433 AA; 45437 MW; 36351670669BD114 CRC64; MSDVLFIEGG RVIDPAGGVD GVRTVVIRDG KVAEVAERVE RPRDARVLDA RNRWVTPGFV DLHVHLREPG QEYKETVATG ARAAVAGGFT AVCAMPNTKP VNDCAAVTEL VLARAAAAGL ARVYPVGAIS KGSGGEELAE YGELKASGCV ALSDDGRPVM SSALMRRALE YARAFGLPLT VHEEDLHLVG KGVMHEGAAA TRLGLKGIPS QAEDVMVLRD IALVELTGGR LHVAHVSTAG AVRAIREAKR RGLPVTGEVT PHHLALTDDD VAASGYSTDF KMNPPLRSAD DVRACREGLA DGTLDAIATD HAPHSAVEKD VEFDAAANGI VGLETAFSVC LGLVREGALT ERRLVEALTA GPARVFGLPA GTLARGAAAD VAVLDAAAEW TLDPARLQSK GRNTPWKGRR LAGRCTHTIV GGRIVHEEGK ADR //