ID G2WLW5_YEASK Unreviewed; 347 AA. AC G2WLW5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 14-DEC-2022, entry version 50. DE RecName: Full=Adenine deaminase {ECO:0000256|HAMAP-Rule:MF_03145}; DE Short=ADE {ECO:0000256|HAMAP-Rule:MF_03145}; DE EC=3.5.4.2 {ECO:0000256|HAMAP-Rule:MF_03145}; DE AltName: Full=Adenine aminohydrolase {ECO:0000256|HAMAP-Rule:MF_03145}; DE Short=AAH {ECO:0000256|HAMAP-Rule:MF_03145}; GN Name=K7_AAH1 {ECO:0000313|EMBL:GAA25957.1}; GN Synonyms=AAH1 {ECO:0000256|HAMAP-Rule:MF_03145}; GN ORFNames=SYK7_059211 {ECO:0000313|EMBL:GAA25957.1}; OS Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's OS yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=721032 {ECO:0000313|EMBL:GAA25957.1, ECO:0000313|Proteomes:UP000001608}; RN [1] {ECO:0000313|EMBL:GAA25957.1, ECO:0000313|Proteomes:UP000001608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608}; RX PubMed=21900213; DOI=10.1093/dnares/dsr029; RA Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D., RA Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S., RA Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T., RA Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A., RA Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A., RA Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.; RT "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no. RT 7."; RL DNA Res. 18:423-434(2011). 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_03145}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenine + H(+) + H2O = 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_03145}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine + H(+) + H2O = 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:0000256|ARBA:ARBA00001466}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03145}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03145}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03145}. CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03145}. 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_03145}. 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; DG000050; GAA25957.1; -; Genomic_DNA. DR AlphaFoldDB; G2WLW5; -. DR SMR; G2WLW5; -. DR HOGENOM; CLU_039228_7_0_1; -. DR Proteomes; UP000001608; Chromosome XIV. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC. 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 GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro. DR CDD; cd01320; ADA; 1. DR HAMAP; MF_01962; Adenine_deaminase; 1. DR InterPro; IPR006650; A/AMP_deam_AS. DR InterPro; IPR001365; A_deaminase_dom. DR InterPro; IPR028892; ADE. DR InterPro; IPR006330; Ado/ade_deaminase. DR InterPro; IPR032466; Metal_Hydrolase. DR PANTHER; PTHR43114; ADENINE DEAMINASE; 1. DR Pfam; PF00962; A_deaminase; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR TIGRFAMs; TIGR01430; aden_deam; 1. DR PROSITE; PS00485; A_DEAMINASE; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03145}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03145}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03145}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03145}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03145}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03145}. FT DOMAIN 11..340 FT /note="A_deaminase" FT /evidence="ECO:0000259|Pfam:PF00962" FT ACT_SITE 207 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145" FT BINDING 16 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145" FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145" FT BINDING 204 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145" FT BINDING 285 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145" FT BINDING 286 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145" FT SITE 228 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145" SQ SEQUENCE 347 AA; 39635 MW; E25573A9F9EB7BB6 CRC64; MVSVEFLQEL PKCEHHLHLE GTLEPDLLFP LAKRNDIILP EGFPKSVEEL NEKYKKFRDL QDFLDYYYIG TNVLISEQDF FDLAWAYFKK VHKQGLVHAE VFYDPQSHTS RGISIETVTK GFQRACDKAF SEFGITSKLI MCLLRHIEPE ECLKTIEEAT PFIKDGTISA LGLDSAEKPF PPHLFVECYG KAASLNKDLK LTAHAGEEGP AQFVSDALDL LQVTRIDHGI NSQYDEELLD RLSRDQTMLT ICPLSNVKLQ VVQSVSELPL QKFLDRDVPF SLNSDDPAYF GGYILDVYTQ VSKDFPHWDH ETWGRIAKNA IKGSWCDDKR KNGLLSRVDE VVTKYSH //