ID ADD_ECOLU Reviewed; 333 AA. AC B7NB76; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 02-SEP-2026, entry version 86. DE RecName: Full=Adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_00540}; DE EC=3.5.4.4 {ECO:0000255|HAMAP-Rule:MF_00540}; DE AltName: Full=Adenosine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_00540}; GN Name=add {ECO:0000255|HAMAP-Rule:MF_00540}; GN OrderedLocusNames=ECUMN_1913; OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMN026 / ExPEC; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2- CC deoxyadenosine. {ECO:0000255|HAMAP-Rule:MF_00540}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine + H2O + H(+) = inosine + NH4(+); CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2'-deoxyadenosine + H2O + H(+) = 2'-deoxyinosine + NH4(+); CC Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00540}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00540}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00540}; CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Adenosine and AMP deaminases family. Adenosine deaminase subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00540}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU928163; CAR13110.1; -; Genomic_DNA. DR RefSeq; WP_000567490.1; NC_011751.1. DR AlphaFoldDB; B7NB76; -. DR SMR; B7NB76; -. DR STRING; 585056.ECUMN_1913; -. DR GeneID; 75171683; -. DR GeneID; 75204467; -. DR KEGG; eum:ECUMN_1913; -. DR PATRIC; fig|585056.7.peg.2097; -. DR HOGENOM; CLU_039228_0_2_6; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:RHEA. DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006154; P:adenosine catabolic process; IEA:TreeGrafter. DR GO; GO:0043103; P:hypoxanthine salvage; IEA:TreeGrafter. DR GO; GO:0046103; P:inosine biosynthetic process; IEA:TreeGrafter. DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01320; ADA; 1. DR FunFam; 3.20.20.140:FF:000009; Adenosine deaminase; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR HAMAP; MF_00540; A_deaminase; 1. DR InterPro; IPR006650; A/AMP_deam_AS. DR InterPro; IPR028893; A_deaminase. DR InterPro; IPR001365; A_deaminase_dom. DR InterPro; IPR006330; Ado/ade_deaminase. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR01430; aden_deam; 1. DR NCBIfam; NF006846; PRK09358.1-1; 1. DR PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1. DR PANTHER; PTHR11409:SF43; ADENOSINE DEAMINASE; 1. DR Pfam; PF00962; A_deaminase; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PROSITE; PS00485; A_DEAMINASE; 1. PE 3: Inferred from homology; KW Hydrolase; Metal-binding; Nucleotide metabolism; Zinc. FT CHAIN 1..333 FT /note="Adenosine deaminase" FT /id="PRO_1000128844" FT ACT_SITE 200 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540" FT BINDING 12 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540" FT BINDING 14 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540" FT BINDING 14 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540" FT BINDING 16 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540" FT BINDING 170 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540" FT BINDING 197 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540" FT BINDING 278 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540" FT BINDING 279 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540" FT SITE 221 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00540" SQ SEQUENCE 333 AA; 36397 MW; 6234BBC13C505ED6 CRC64; MIDTTLPLTD IHRHLDGNIR PQTILELGRQ YNISLPAQSL ETLIPHVQVI ANEPDLVSFL TKLDWGVKVL ASLDACRRVA FENIEDAARH GLHYVELRFS PGYMAMAHQL PVAGVVEAVI DGVREGCRTF GVQAKLIGIM SRTFGEAACQ QELEAFLAHR DQITALDLAG DELGFPGSLF LSHFNRARDA GWHITVHAGE AAGPESIWQA IRELGAERIG HGVKAIEDRA LMDFLAEQQI GIESCLTSNI QTSTVAELAA HPLKTFLEHG IRASINTDDP GVQGVDIIHE YTVAAPAAGL SREQIRQAQI NGLEMAFLSA EEKRALREKV AAK //