ID   ADEC_METTP              Reviewed;         567 AA.
AC   A0B6I9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, 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=Mthe_0522;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000477; ABK14313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B6I9; -.
DR   SMR; A0B6I9; -.
DR   EnsemblBacteria; ABK14313; ABK14313; Mthe_0522.
DR   KEGG; mtp:Mthe_0522; -.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; IEGHFPG; -.
DR   Proteomes; UP000000674; 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..567
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292404"
SQ   SEQUENCE   567 AA;  61411 MW;  99BB02F4641810A7 CRC64;
     MRIEDLIAAA RGELEADLLL EGGKLVNVFS GEIHRADISI YGGFVAGFDC PSARRVISVE
     DHLIAPGSID AHVHIESSML MPSEYARAVV PRGTLTVIAD PHEIANVLGV DGISYLLRCA
     EGIPMRFLVT APSCVPATHL ETSGAALGVS EIASLLDDHR VVGLGEMMNY PGVIHRDKPV
     LAKLKVAASK NKTICGHAPG LGGRDLHAYA AALIEDDHEC TRAEEAMEQL RAGICIMIRE
     GSAARNLDEL VKIIREYNTP NIMLCTDDLD PRDIVHRHID HMIRRIIEAG TDPVAAIQMA
     TINPARHFGL RRTGAVAPGY RADIIVMDHD FNVRRVIFEG EEVARDGRLT ASFESKRLPV
     QTSMNVRLPI TRESFRIPAT GRIVRVIGVA PNQILTETIA ARPEVRNGEV ISDTRNDILK
     VAVVERHRAT GNVGLGLVSG FGLKRGAIAS SVSHDSHNII VVGEDEESMV RAVESLISMG
     GGWVSVDGTT IASLPLPIAG LLSERRVEDV VEEAENVIAA SHSLGSELED SFMTLSFLAL
     PVIPELRITD RGLVDVREFG HVPLFME