ID   ADE_PSEU5               Reviewed;         316 AA.
AC   A4VQI5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=PST_3608;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(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; CP000304; ABP81236.1; -; Genomic_DNA.
DR   RefSeq; WP_011914630.1; NC_009434.1.
DR   AlphaFoldDB; A4VQI5; -.
DR   SMR; A4VQI5; -.
DR   STRING; 379731.PST_3608; -.
DR   EnsemblBacteria; ABP81236; ABP81236; PST_3608.
DR   KEGG; psa:PST_3608; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_0_6; -.
DR   OMA; DERLMQR; -.
DR   Proteomes; UP000000233; Chromosome.
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; Reference proteome; Zinc.
FT   CHAIN           1..316
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000017685"
FT   ACT_SITE        197
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   SITE            218
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
SQ   SEQUENCE   316 AA;  35601 MW;  E3793C3550B2D7E7 CRC64;
     MHDWLNNLPK AELHLHLEGS LEPELMFRLA ERNKIALPWN DVEALRSAYN FGNLQEFLDL
     YYAGADVLRT EQDFYDLTWA YLQKCEEQNV VHTEPFFDPQ THTDRGVPFE AALNGISAAL
     ADGRELLGIS SGLILSFLRH LPEEEAFKTL EQALPYRNAF FAVGLDSSEV GHPPSKFQRV
     FDKARGEGLL TVAHAGEEGP PEYIWQALDL LKVSRIDHGV RAAEDPKLIA RLIEEQIPLT
     VCPLSNTKLK VFADMRQHNI LDLLEQGVKV TVNSDDPAYF GGYVTENFVA LHESLGMTEA
     QARRLAQNSL DARLAY