ID A5CNP8_CLAM3 Unreviewed; 333 AA. AC A5CNP8; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 04-NOV-2026, entry version 110. DE RecName: Full=Adenine deaminase {ECO:0000256|HAMAP-Rule:MF_01962}; DE Short=ADE {ECO:0000256|HAMAP-Rule:MF_01962}; DE EC=3.5.4.2 {ECO:0000256|HAMAP-Rule:MF_01962}; DE AltName: Full=Adenine aminohydrolase {ECO:0000256|HAMAP-Rule:MF_01962}; DE Short=AAH {ECO:0000256|HAMAP-Rule:MF_01962}; GN Name=addB {ECO:0000313|EMBL:CAN00686.1}; GN OrderedLocusNames=CMM_0659 {ECO:0000313|EMBL:CAN00686.1}; OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Microbacteriaceae; Clavibacter. OX NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN00686.1, ECO:0000313|Proteomes:UP000001564}; RN [1] {ECO:0000313|EMBL:CAN00686.1, ECO:0000313|Proteomes:UP000001564} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN00686.1, RC ECO:0000313|Proteomes:UP000001564}; RX PubMed=18192381; DOI=10.1128/JB.01595-07; RA Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M., RA Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O., RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C., RA Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O., RA Bartels D.; RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved RT in pathogenicity."; RL J. Bacteriol. 190:2138-2149(2008). CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenine to CC hypoxanthine. Plays an important role in the purine salvage pathway and CC in nitrogen catabolism. {ECO:0000256|HAMAP-Rule:MF_01962}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenine + H2O + H(+) = hypoxanthine + NH4(+); CC Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01962}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01962}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01962}; CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Adenosine and AMP deaminases family. Adenine deaminase type 2 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01962}. 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; AM711867; CAN00686.1; -; Genomic_DNA. DR RefSeq; WP_011931879.1; NC_009480.1. DR AlphaFoldDB; A5CNP8; -. DR GeneID; 92949691; -. DR KEGG; cmi:CMM_0659; -. DR eggNOG; COG1816; Bacteria. DR HOGENOM; CLU_039228_7_0_11; -. DR OMA; AAFCTDQ; -. DR OrthoDB; 105475at2; -. DR Proteomes; UP000001564; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006146; P:adenine catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0043103; P:hypoxanthine salvage; IEA:UniProtKB-UniRule. DR CDD; cd01320; ADA; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR HAMAP; MF_01962; Adenine_deaminase; 1. DR InterPro; IPR001365; A_deaminase_dom. DR InterPro; IPR028892; ADE. DR InterPro; IPR006330; Ado/ade_deaminase. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR01430; aden_deam; 1. DR NCBIfam; NF006850; PRK09358.1-6; 1. DR PANTHER; PTHR43114; ADENINE DEAMINASE; 1. DR PANTHER; PTHR43114:SF6; ADENINE DEAMINASE; 1. DR Pfam; PF00962; A_deaminase; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01962}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01962}; KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP- KW Rule:MF_01962}; Reference proteome {ECO:0000313|Proteomes:UP000001564}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01962}. FT DOMAIN 7..328 FT /note="Adenosine deaminase" FT /evidence="ECO:0000259|Pfam:PF00962" FT ACT_SITE 195 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962" FT BINDING 12 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962" FT BINDING 14 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962" FT BINDING 192 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962" FT BINDING 273 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962" FT BINDING 274 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962" FT SITE 216 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962" SQ SEQUENCE 333 AA; 36540 MW; 6B8FDF462A257587 CRC64; MISTLPPTAE LHLHVEGTLE PELVFELAER NGVELPYQGI EDLRSRYAFT DLQSFLDLYY ACTAVLRTRR DFHDLAAAYL ERAAADGIRH VEMSFDPQAH TTRGVPVDDV VDGLLDALRD ARVRHGISGG LILSFLRDRP VDEAMATLES VAGRAHELLA VGLDSAEVGY PPSLFVDVFA RARELGLHAV AHAGEEGPPA YIHEALDLLR VERVDHGVRC LEDPALVDRL VADRIPLTVC PLSNVRLGVN ESLDEHALPE LLARGVLATV NSDDPAYFGG YLGENLRQLR QAHAFDDDAV ALLARNSFEA SFLSDERRAE LLAAVDAWRA SAL //