ID   ADE_CUPTR               Reviewed;         351 AA.
AC   B3R3T1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=RALTA_A0998;
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(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: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; CU633749; CAQ68963.1; -; Genomic_DNA.
DR   RefSeq; WP_012352296.1; NC_010528.1.
DR   AlphaFoldDB; B3R3T1; -.
DR   SMR; B3R3T1; -.
DR   STRING; 977880.RALTA_A0998; -.
DR   EnsemblBacteria; CAQ68963; CAQ68963; RALTA_A0998.
DR   GeneID; 29760436; -.
DR   KEGG; cti:RALTA_A0998; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_0_4; -.
DR   OMA; NHFTIHA; -.
DR   OrthoDB; 554648at2; -.
DR   BioCyc; CTAI977880:RALTA_RS04735-MON; -.
DR   Proteomes; UP000001692; Chromosome 1.
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_1000128838"
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;  38700 MW;  594A3F8827C0B09E CRC64;
     MTIDAALAEQ IRRTPKAELH VHIEGTLEPE LIFRLAQRNQ VALPYPSVDA LRAAYAFTDL
     QSFLDIYYAG ASVLLTEEDF FDMTMDYVKR AVADNVRHAE IFFDPQTHTA RGVPIGVVID
     GIADALAQAR TEYDFSSSLI LCFLRHLSEE DAFATLEAAL PYRDRFVGVG LDSSEKGNPP
     EKFARVFARA RELGLHLVAH AGEEGPAQYV ADALDILKAE RIDHGVRAID DAALVERLAR
     ERVALTVCPL SNVKLKVYPD LRDHPLKRML DAGVAITLHS DDPAYFGGYM NANWEATFDA
     LPLDAADAHK LARNSFEAAF LPAMQKAEFL AEVDHFWSAP PKSPPATAPA A