ID ADEC_BORBU Reviewed; 548 AA. AC O50821; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 05-MAY-2009, entry version 56. DE RecName: Full=Adenine deaminase; DE Short=Adenase; DE Short=Adenine aminase; DE EC=3.5.4.2; GN Name=ade; OrderedLocusNames=BB_K17; OS Borrelia burgdorferi (Lyme disease spirochete). OG Plasmid lp36. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia; OC Borrelia burgdorferi group. OX NCBI_TaxID=139; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680; RX MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., RA Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., RA Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., RA Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., RA Roberts K.M., Hatch B., Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia RT burgdorferi."; RL Nature 390:580-586(1997). 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; AE000788; AAC66139.1; -; Genomic_DNA. DR PIR; C70253; C70253. DR RefSeq; NP_045591.1; -. DR GeneID; 1194225; -. DR GenomeReviews; AE000788_GR; BB_K17. DR KEGG; bbu:BBK17; -. DR NMPDR; fig|224326.1.peg.1442; -. DR TIGR; BB_K17; -. DR HOGENOM; O50821; -. DR OMA; O50821; IMIREGS. DR BioCyc; BBUR224326:BB_K17-MON; -. DR BRENDA; 3.5.4.2; 142596. DR GO; GO:0000034; F:adenine deaminase activity; IEA:HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0006146; P:adenine catabolic process; IEA:InterPro. DR HAMAP; MF_01518; -; 1. DR InterPro; IPR006679; Adenine_deam. DR InterPro; IPR006680; Amidohydro_1. DR Pfam; PF01979; Amidohydro_1; 1. DR TIGRFAMs; TIGR01178; ade; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Manganese; Plasmid. FT CHAIN 1 548 Adenine deaminase. FT /FTId=PRO_0000142406. SQ SEQUENCE 548 AA; 60864 MW; 012AE5222AD8301E CRC64; MDLFKIEANY IDIFNKEIYP ASIAIANGHI ASIEKINATL DEYVLPGFID AHIHIESSFL VPSNFAHLVV AHGTVATISD PHEIANVNGI DGINFMINNS KKTEFKFFFG APSCVPALSQ EFETSGYVLN DKDIDELMKL DDIYYLAEVM DFKGVINKDI EIINKINSAL KRNKVVDGHA PGLSPNLTLK YASSGISTDH ECLTIEDARY KLSLGMKILI REGSAAKNFE SLHPLISECS KKYCDSLMFC FDDAHPNDIL NGHINLIVAR AIKHGHDFFD VLKIACINPV LHYKIPVGLL RIGDPADFII TKDIKTFKIN KTYINGKLVF NDGISLIPLI NEIPINNFNC SKKSISDFKF STKNKMIPVI KCISNQIITH KTMIDSNLLA PDFQSNIAED ILKIAIINRY KDNSKISIGF IKNFGIRNGA IGSTVAHDSH NIILVGSNDE YLCKAANTII QNKGGLCALN NEKTIIMELP ISGLMSTLSA ERVASQYIKL NDFCKNVLGS RLDDPLMTLS FMSLTVVPHL KINDKGLFDV DSFCFVDY //