ID   ADEC_DESHY              Reviewed;         569 AA.
AC   Q24R88;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=DSY3665;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51;
RX   PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE85454.1; -; Genomic_DNA.
DR   RefSeq; WP_011461279.1; NC_007907.1.
DR   AlphaFoldDB; Q24R88; -.
DR   SMR; Q24R88; -.
DR   STRING; 138119.DSY3665; -.
DR   EnsemblBacteria; BAE85454; BAE85454; DSY3665.
DR   KEGG; dsy:DSY3665; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000001946; 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; Reference proteome.
FT   CHAIN           1..569
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000296721"
SQ   SEQUENCE   569 AA;  62452 MW;  9EF7DEA8E9DD27D4 CRC64;
     MNDKDLKKLT AKSLGREKAE LVLKNAQVIN VFSEEILVRD VAVGDGMIVG VGQYQGREEV
     DLSGKYLCPG FIDAHLHLES TLVAPPELIH SALQWGTTTF IIDPHEVVNV AGEEGLDYML
     EQTEGLAANV FVMLPSCVPA VPFEENGGVF TAEKMEPYLA NPRVLGLGEV MDYVSVIGAE
     EEMVKKLRLF RERIKDGHAP YLQDKQLAAY ALAGIKTDHE CIDYAYALEE IRNGMQVLIR
     EGSGARNLAA IVRGIRENNL DTGNFSFCTD DKHINDIQRE GHISYNIKKS IALGLPPLKA
     IKMATLNTAR CYNLTELGAV APGYQADFVI LDSLEEVAVH AVYHKGKKVE REKKIDIKPC
     SEQLRRTVHL PALSAEDLKL AVPDSPSSLI QMSEGQITTK HVRDVLPARD GCFVPNAQYN
     KVVVVERHKG TGHFAVAPVL GFNLGQGAIA TSVSHDSHNV VAIGDNDESI LLALQELQRV
     QGGYTMIREQ RVLATLPLPI MGLISDAGHQ AVESMLNTMV GYAHEMGVPA SIHPFIALSF
     IALPVIPEIR ITTRGLYDAV EQKFIRYIP