ID PYRC_LISIN Reviewed; 426 AA. AC Q92AH1; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 16-JUN-2009, entry version 52. DE RecName: Full=Dihydroorotase; DE Short=DHOase; DE EC=3.5.2.3; GN Name=pyrC; OrderedLocusNames=lin1951; OS Listeria innocua. OC Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=1642; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIP 11262 / Serovar 6a; RX MEDLINE=21537279; PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). 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; AL596170; CAC97181.1; -; Genomic_DNA. DR PIR; AE1676; AE1676. DR RefSeq; NP_471285.1; -. DR HSSP; P81006; 1GKR. DR MEROPS; M38.972; -. DR GeneID; 1130647; -. DR GenomeReviews; AL592022_GR; lin1951. DR KEGG; lin:lin1951; -. DR NMPDR; fig|272626.1.peg.1938; -. DR ListiList; LIN01951; -. DR HOGENOM; Q92AH1; -. DR OMA; Q92AH1; GIFAEKE. DR BioCyc; LINN272626:LIN1951-MON; -. DR BRENDA; 3.5.2.3; 270396. 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 ProDom; PD000518; DHOase; 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 1 426 Dihydroorotase. FT /FTId=PRO_0000147239. FT METAL 58 58 Zinc 1 (By similarity). FT METAL 60 60 Zinc 1 (By similarity). FT METAL 140 140 Zinc 1; via carbamate group (By FT similarity). FT METAL 140 140 Zinc 2; via carbamate group (By FT similarity). FT METAL 177 177 Zinc 2 (By similarity). FT METAL 230 230 Zinc 2 (By similarity). FT METAL 303 303 Zinc 1 (By similarity). FT MOD_RES 140 140 N6-carboxylysine (By similarity). SQ SEQUENCE 426 AA; 46201 MW; D8591D40D111FED3 CRC64; MYVLKNGQVL NESGELENKD VLIQNGKVNL IADSIEVTSG EEFDATGKLI APGFIDVHVH LREPGGEHKE TILTGTKAAA RGGYTTICSM PNTKPVPDSK EVMNSLQAKI KETAEVRVLP YASITTSLGT DELVDFEALK EAGAFAFTDD GVGVQLAGTM YEAMKRAAAL DMAIVAHCED NSLIYGGVVH DGIFAEKEGL KGIPNIAESV QIARDVLLAE AAGCHYHVCH ISTKESVRVV RDAKRAGIRV TAEVSPHHLI LDEEDIPGND GNWKMNPPLR SKEDRAALLE GLLDGTIDFI ATDHAPHAAE EKNVPMEQAA FGIVGLETAF PLLYTHFVKT NEWTLKQLID WMTVKPAECF KLPYGKLEEG AVADIVVLDL EKEATIDPAT FYSKGKNTPF VGETCIGWPV ATFAEGELVY NEGENK //