ID   ADEC_METST              Reviewed;         542 AA.
AC   Q2NER8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Msp_1308;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(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; CP000102; ABC57685.1; -; Genomic_DNA.
DR   RefSeq; WP_011406884.1; NC_007681.1.
DR   AlphaFoldDB; Q2NER8; -.
DR   SMR; Q2NER8; -.
DR   STRING; 339860.Msp_1308; -.
DR   EnsemblBacteria; ABC57685; ABC57685; Msp_1308.
DR   GeneID; 41325878; -.
DR   KEGG; mst:Msp_1308; -.
DR   eggNOG; arCOG00693; Archaea.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 12286at2157; -.
DR   Proteomes; UP000001931; 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..542
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292405"
SQ   SEQUENCE   542 AA;  59673 MW;  0D7DD1B4B636449B CRC64;
     MLIKGNILNV FTDEIYPGEI KIEHGIIESI KEVNADFNDI IVPGFIDAHI HIESSMLTPS
     RFAEIALRHG TTSVIADPHE IANVMGMDGI DYMIDDAKKT PLKYYFTAPS CVPATKFEKS
     GATISPNIID NLLSRPEFVA LGEVMDYNAV ISNEKSILEK IKIAKKYHKP IDGHAPLLSG
     KNLQKYVKHG VITDHESTTK KEVAEKKRMG MKIMIREGSE SKMLEKLIYS NCDFIVSDDL
     KPEDLINGHL DKCLRKAVDY GMDPYEAIKL VTINPAEHYN LNAGSISPGK SADLVFIDNL
     RDFTVKRVVI NGNTIFKKQK LLFRANPRPI DTTLHVSLTK PEDFDLKAQN PAHKSATVNL
     INVSDNTIIT KQSSAKLSIQ KKTIIPSVFE DILKISVVDR YGGNTISNGF VKGFGIKNGA
     IASSVSHDSH NIIVVGTNSE YMSRATNHLI ENKGGLAAIS NQAKLDVTLP IAGLMSDKPA
     KVVANNSAKL NELVSNMGCE LSSPFTSLSF MALPVVPEVK MTTNGLFNVN THQFIDIIKE
     EK