ID   ADE_PARPJ               Reviewed;         350 AA.
AC   B2T672;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   04-NOV-2026, entry version 92.
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=Bphyt_3044;
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX   PubMed=21551308; DOI=10.1128/jb.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(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:0000255|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:0000255|HAMAP-Rule:MF_01962};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         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; CP001052; ACD17436.1; -; Genomic_DNA.
DR   RefSeq; WP_012434015.1; NC_010681.1.
DR   AlphaFoldDB; B2T672; -.
DR   SMR; B2T672; -.
DR   STRING; 398527.Bphyt_3044; -.
DR   KEGG; bpy:Bphyt_3044; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_0_4; -.
DR   OMA; AAFCTDQ; -.
DR   OrthoDB; 105475at2; -.
DR   Proteomes; UP000001739; Chromosome 1.
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   FunFam; 3.20.20.140:FF:000039; Adenine deaminase; 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; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT   CHAIN           1..350
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000128835"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         288
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   SITE            231
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
SQ   SEQUENCE   350 AA;  38771 MW;  1046B8E88942CEAE CRC64;
     MTTTTVTPTP LAEKTALAPK AELHIHIEGS LEPELIFALA ERNGVKLAYD SIDALRAAYA
     FTDLQSFLDI YYAGASVLLH EQDFYDMTMA YVERCLADNV IHSEIFFDPQ THTERGVPIA
     TVVAGIERAL ADAEKRGMTS KLILCFLRHL SEEDALATFE EALPLFEQYK HRLIGVGLDS
     SERGHPPSKF ERVFAKARAL GLKLVAHAGE EGPPSYIYEA LDLLKVDRVD HGVRSIEDPA
     LVTRLADSRV ALTVCPLSNL KLCVFDDLTK HTLKDLLDRG VAVTVNSDDP AYFGGYVNAN
     YFATIDALKL NDAEVYTIIR NSFEASFVTP EQRSELIAKL DAHWHPSGPH
//