ID PYRC_AZOSE Reviewed; 344 AA. AC Q5P6Y5; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 16-JUN-2009, entry version 29. DE RecName: Full=Dihydroorotase; DE Short=DHOase; DE EC=3.5.2.3; GN Name=pyrC; OrderedLocusNames=AZOSEA08010; ORFNames=ebA1456; OS Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)). OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Rhodocyclaceae; Aromatoleum. OX NCBI_TaxID=76114; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9; RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., RA Reinhardt R.; RT "The genome sequence of an anaerobic aromatic-degrading denitrifying RT bacterium, strain EbN1."; RL Arch. Microbiol. 183:27-36(2005). 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; CR555306; CAI06926.1; -; Genomic_DNA. DR RefSeq; YP_157827.1; -. DR GeneID; 3181227; -. DR GenomeReviews; CR555306_GR; AZOSEA08010. DR KEGG; eba:ebA1456; -. DR NMPDR; fig|76114.4.peg.353; -. DR HOGENOM; Q5P6Y5; -. DR OMA; Q5P6Y5; IMPNLVP. DR BioCyc; ASP76114:EBA1456-MON; -. 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_0000325570. 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; 37310 MW; 75E74BD36B3B7FC3 CRC64; MQTISLIRPD DWHLHVRDGA ALATVVPHTA RRFGRALIMP NLRPPVTTAA QALEYRARIL AAVPPGQHFE PLMSLYLTDN TSPDEIDRAK ASGAVVAVKL YPAGATTNSD AGVTAIEKVH AVLERMEKLG MVLCVHGEVT HGDVDVFDRE QVFIEQVLAP LVARFPALRV VFEHITTAEA ARFVQDAGPN VAATVTAHHL LLNRNAIFAG GIRPHHYCLP VLKRETHRRA LVEAATSGNA KFFLGTDSAP HSRAAKETAC GCAGCYTAHA AIELYAEAFE QAGALDRLEA FASLNGPAFY GLAPNAERIT LAKDAWEVPG EYEYLHDDPL VPLRAGETVA WRVL //