ID   ADEC_METB6              Reviewed;         558 AA.
AC   A7I8N1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=Mboo_1575;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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; CP000780; ABS56092.1; -; Genomic_DNA.
DR   RefSeq; WP_012107135.1; NC_009712.1.
DR   AlphaFoldDB; A7I8N1; -.
DR   SMR; A7I8N1; -.
DR   STRING; 456442.Mboo_1575; -.
DR   EnsemblBacteria; ABS56092; ABS56092; Mboo_1575.
DR   GeneID; 5410587; -.
DR   KEGG; mbn:Mboo_1575; -.
DR   eggNOG; arCOG00693; Archaea.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 12286at2157; -.
DR   Proteomes; UP000002408; 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; 2.
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..558
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000318550"
SQ   SEQUENCE   558 AA;  58705 MW;  A7B500DFA84FA4F3 CRC64;
     MDAPPLHANL IPAARGTEPA DLVLKNAMLF DAFSCSWEEG DLAIKDGIIV GTGRSYRGIR
     ERDLGGALVV PGLIDAHVHI ESSLLVPQEY AHLVAAHGTT TVIADPHEIA NIAGKEGIEY
     MLACRAGLPV DILYMLPSCV PATPADVGGA VLDAGDLAGF PGRDGILGLG EMMNVPGVLG
     GDPGVLAKLV LSRIRDGHAP HLSGPDLNAY LLSGPDSDHE CTTASEAKEK LRCGMYLFVR
     EGSTEKNIAA LVPVVTPYTV SRCSFCTDDC HADLLAHSGH IDRCIRTAVA GGLEPELALR
     MATLSPAERF SLPDRGALAP GRRADFCIVD DPRHFAVKET YSRGRPVAEY AAPQARPPVF
     AALRCTVPSR DQIRLFGTGR ARVIGLVPGQ ILTESLTFDL DAAALPDISR DLLKLVVCNR
     YGKGSVGTGI VHGFGFKDGA IAASISHDAH NIVAAGTGDE VILSALTAVI RAGGGMAAVH
     KKDVTVLPLD CAGLMSTHPA REVIAGLDAL SAATRRIGGI DDPFMYLSFL ALTVIPALRL
     TDRGLFDAVA FRDVPVFP