ID   ADE_CUPPJ               Reviewed;         351 AA.
AC   Q46YJ3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01962};
DE            Short=ADE {ECO:0000255|HAMAP-Rule:MF_01962};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01962};
DE   AltName: Full=Adenine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_01962};
DE            Short=AAH {ECO:0000255|HAMAP-Rule:MF_01962};
GN   OrderedLocusNames=Reut_A2428;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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:0000255|HAMAP-Rule:MF_01962}.
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:0000255|HAMAP-Rule:MF_01962};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01962};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01962}.
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DR   EMBL; CP000090; AAZ61790.1; -; Genomic_DNA.
DR   RefSeq; WP_011298579.1; NC_007347.1.
DR   AlphaFoldDB; Q46YJ3; -.
DR   SMR; Q46YJ3; -.
DR   STRING; 264198.Reut_A2428; -.
DR   EnsemblBacteria; AAZ61790; AAZ61790; Reut_A2428.
DR   KEGG; reu:Reut_A2428; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_0_4; -.
DR   OMA; NHFTIHA; -.
DR   OrthoDB; 554648at2; -.
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   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01320; ADA; 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   PANTHER; PTHR43114; PTHR43114; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01430; aden_deam; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Nucleotide metabolism; Zinc.
FT   CHAIN           1..351
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000017688"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   SITE            224
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
SQ   SEQUENCE   351 AA;  38795 MW;  CADC427E7FBB6452 CRC64;
     MTIDAALADK IRRTPKAELH VHIEGTLEPE LIFRLAQRNH VNLPYPSVEA LRAAYAFTDL
     QSFLDIYYAG ASVLLTEEDF FDMTMDYVKR AVADNVRHAE IFFDPQTHTA RGVPIGTVID
     GISDALAQAR TEYDFSSSLI LCFLRHLSEE DAFATLEAAL PYRDRFVGVG LDSSEKGNPP
     EKFARVFTRA RELGLHLVAH AGEEGPAQYV TDALDILKVE RIDHGVRSID DAALIERLAR
     ERVALTVCPL SNQKLKVHPD LSEHPLKRML DAGVAITLHS DDPAYFGGYM NANWEATFAA
     LPLDAADAHK LARNSFEAAF LPPMQKAEFL AEVDHFWSAT PTSPPATAPA A