ID   ADEC_DESHD              Reviewed;         566 AA.
AC   B8FPU4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=Dhaf_1712;
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2;
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL19758.1; -; Genomic_DNA.
DR   RefSeq; WP_015943614.1; NC_011830.1.
DR   AlphaFoldDB; B8FPU4; -.
DR   SMR; B8FPU4; -.
DR   EnsemblBacteria; ACL19758; ACL19758; Dhaf_1712.
DR   KEGG; dhd:Dhaf_1712; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000007726; 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..566
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000185086"
SQ   SEQUENCE   566 AA;  62342 MW;  F74F4E78D3EAA2FA CRC64;
     MNDRNLKKLA PKSLGREKAQ LVLKNAQVIN VFSEEILVRD VAVEDGVIVG VGQYQGREEV
     DLSGKYLCPG FIDAHLHLES TLVAPPELIH SALQWGTTTF IIDPHEVVNV AGEEGLDYML
     EQTEGLAANV FLMLPSCVPA VPFEENGGVF SAEKMEPYLA NPRVLGLGEV MDYVSVIEAE
     EGMVKKLRLF RERIKDGHAP YLQDKQLAAY ALAGIKTDHE CIDYAYALEE VRNGMQVLIR
     EGSGARNLEA IVRGIRDNSM DTGNFSFCTD DKHINDIQRE GHISYNIKKS IALGIPPLKA
     IKMATINTAR CYNLTKLGAV APGYQADFVI LDSLEEVAVH AVYHKGKKVD REKKIEIKPC
     PEQLRRTVHL PNLSADDLKL AVPDSPSSLI QMIEGQITTK HVRDVLPAQD GCFVPNAQYN
     KVVVVERHKG TGHFAVAPVL GFNLRQGAIA TSVSHDSHNV VAIGDNDESI LLALQELQRV
     QGGYTMIRGQ RVLATLPLPI MGLISDAGYQ AVENTLNQMI GYAHEMGVPA HTHPFIALSF
     IALPVIPEIR ITTRGLYDVV DQEFIR