ID   ADEC_LYSSC              Reviewed;         581 AA.
AC   B1HR71;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=Bsph_3357;
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41;
RX   PubMed=18296527; DOI=10.1128/jb.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
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_01518};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
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DR   EMBL; CP000817; ACA40851.1; -; Genomic_DNA.
DR   RefSeq; WP_012294915.1; NC_010382.1.
DR   AlphaFoldDB; B1HR71; -.
DR   SMR; B1HR71; -.
DR   EnsemblBacteria; ACA40851; ACA40851; Bsph_3357.
DR   KEGG; lsp:Bsph_3357; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000002164; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR   CDD; cd01295; AdeC; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01518; Adenine_deamin; 1.
DR   InterPro; IPR006679; Adenine_deam.
DR   InterPro; IPR026912; Adenine_deam_C.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11113:SF2; PTHR11113:SF2; 1.
DR   Pfam; PF13382; Adenine_deam_C; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01178; ade; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese.
FT   CHAIN           1..581
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146243"
SQ   SEQUENCE   581 AA;  63343 MW;  6D93DF4A6EF4FDDB CRC64;
     MTTKLQQLTQ NILSSQGKLE ADFILKNAQV ADVYTLTWRK ADIVVKNGTI VALDHSNRFH
     AKEVEDAAGS YVIPGLIDGH IHIESSMLTP GEFSRVLIPH GITTVITDPH EIANVAGAEG
     IQFMLDDAQK ADMDIFVMLP SSVPGTQFEN AGATLTAQDL EPFLHHEQVR GLAEVMDFPA
     VLNGEEGMLQ KILLSKEANL VIDGHCAGLQ SEQITGYRAA GIQTDHECVT AEEAIDRVEQ
     GMYVLIREGS AAKNLRDLLP AIQSHNARRF GFCTDDKYVD ELMDEGSINY DVAMAIAEGM
     TPLQAIQLAT VNTAECYRLF DRGVLAPGYK ADFVLVDDLS TMQAKAVWKN GHKVAENGEM
     LTSRQEAKVP AHIHHSVHLP SMTKDSLQLS FKKGTRANVM EIVPNQLITN HLVIDVPVKE
     GVFVPSIEQD LLKLAVIERH HHLHTTGLGI VKGFGLQKGA VATTVAHDSH NALVVGTNDE
     DMILALSRIQ EIQGGFVIVA DGEILAEMPL TIGGLMTDVP AQQAKEQLAG LHNALQKLNP
     TLDFHFLLTF SFVALPVIPA LKLTDTGLFD VTTFQHIEVE A