ID G2WLW5_YEASK Unreviewed; 347 AA. AC G2WLW5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 02-NOV-2016, entry version 34. 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}; 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; OC Saccharomycetes; 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., RA Watanabe D., Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., RA Kajiwara S., Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., RA Masubuchi T., Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., RA Ogata T., Ohta A., Sato M., Shibasaki S., Takatsume Y., Tanimoto S., RA Tsuboi H., Nishimura A., Yoda K., Ishikawa T., Iwashita K., Fujita N., RA Shimoi H.; RT "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai RT no. 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 CC pathway and in nitrogen catabolism. {ECO:0000256|HAMAP- CC Rule:MF_03145}. CC -!- CATALYTIC ACTIVITY: Adenine + H(2)O = hypoxanthine + NH(3). CC {ECO:0000256|HAMAP-Rule:MF_03145}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03145}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC 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 adenosine and AMP deaminases family. CC Adenine deaminase type 2 subfamily. {ECO:0000256|HAMAP- CC 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 ProteinModelPortal; G2WLW5; -. DR SMR; G2WLW5; -. DR EnsemblFungi; GAA25957; GAA25957; SYK7_059211. DR OrthoDB; EOG092C2UZH; -. 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-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006146; P:adenine catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0043103; P:hypoxanthine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro. DR HAMAP; MF_01962; Adenine_deaminase; 1. DR InterPro; IPR006650; A/AMP_deam_AS. DR InterPro; IPR001365; A/AMP_deaminase_dom. DR InterPro; IPR028892; ADE. DR InterPro; IPR006330; Ado/ade_deaminase. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF00962; A_deaminase; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR01430; aden_deam; 1. DR PROSITE; PS00485; A_DEAMINASE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001608}; KW Cytoplasm {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|HAMAP-Rule:MF_03145}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03145}. FT DOMAIN 10 336 A_deaminase. {ECO:0000259|Pfam:PF00962}. FT ACT_SITE 207 207 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_03145}. FT METAL 16 16 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03145}. FT METAL 18 18 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03145}. FT METAL 204 204 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03145}. FT METAL 285 285 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_03145}. FT BINDING 286 286 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03145}. FT SITE 228 228 Important for catalytic activity. FT {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 //