ID ADEC2_OENOB Reviewed; 567 AA. AC Q04DZ9; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 05-MAY-2009, entry version 16. DE RecName: Full=Adenine deaminase 2; DE Short=Adenase 2; DE Short=Adenine aminase 2; DE EC=3.5.4.2; GN Name=ade2; OrderedLocusNames=OEOE_1462; OS Oenococcus oeni (strain BAA-331 / PSU-1). OC Bacteria; Firmicutes; Lactobacillales; Oenococcus. OX NCBI_TaxID=203123; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., RA Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., RA Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., RA Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J., RA Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., RA Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., RA Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., RA Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., RA Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., RA Weimer B.C., Mills D.A.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). CC -!- CATALYTIC ACTIVITY: Adenine + H(2)O = hypoxanthine + NH(3). CC -!- COFACTOR: Manganese (By similarity). CC -!- SIMILARITY: Belongs to the adenine deaminase family. 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; CP000411; ABJ57323.1; -; Genomic_DNA. DR RefSeq; YP_810988.1; -. DR GeneID; 4415931; -. DR GenomeReviews; CP000411_GR; OEOE_1462. DR KEGG; ooe:OEOE_1462; -. DR NMPDR; fig|203123.1.peg.1782; -. DR OMA; Q04DZ9; MPLEGHV. DR GO; GO:0000034; F:adenine deaminase activity; IEA:HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR HAMAP; MF_01518; -; 1. DR InterPro; IPR006680; Amidohydro_1. DR Pfam; PF01979; Amidohydro_1; 1. DR ProDom; PD001248; Amidohydro_like; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Manganese. FT CHAIN 1 567 Adenine deaminase 2. FT /FTId=PRO_0000292390. SQ SEQUENCE 567 AA; 62656 MW; A544B8689616BC2E CRC64; MIKADLKIIN GQIYNTFTRQ FTAKEVAIVD GKFFQIADKL SDDFKFEDIL DLKGSYVIPG LIDSHMHIES SMATPTNFSE TAIRFGTTTV IADAHEIANT SGIKGLKRFM DQPSLIDTFF AIPSSVPSTN PELETTGGII DLEEVKELLA DPRIICLGEA MNFKGITSEP NSLIRKIIAL CQKKRPRMPL EGHVPNISKE DLAKFIFAGI LSDHTQQTPA LIKEKIENGM FIQLQKKSLN KENIETIVKN HFYDYSALVT DDTMADDLIN GHLNSIIKLA VKCGLPLEWA IYMTTYTPAQ HMHFQDRGVI APGKIADFVV LNNLDGFSIK NVYKRGVPID KLSIDDEKPF ASEEYHSIYV PNRSAKDFTL RVSKDLKKIT ANVIEIAAKG TFTKAVKKEL LVKDGIVDWQ KAGLALLAVQ ERYGKTGQLT LALVSKSINK SGAIATTWAH DHHNLMVLGT NPDSMAIAYD KVASQQGGYL VVKDKEIVAN VQLPIAGIIS DEPIDIIGHK LKKVRLAMKD LGYVNTNEIM SLSTLSLLVS PSIKVSDKGI FDVKTQTKIP LLLAGEE //