ID   ADEC_METS3              Reviewed;         571 AA.
AC   A5ULK1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Msm_0874;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ87079.1; -; Genomic_DNA.
DR   RefSeq; WP_011954140.1; NC_009515.1.
DR   AlphaFoldDB; A5ULK1; -.
DR   SMR; A5ULK1; -.
DR   STRING; 420247.Msm_0874; -.
DR   EnsemblBacteria; ABQ87079; ABQ87079; Msm_0874.
DR   GeneID; 5217333; -.
DR   KEGG; msi:Msm_0874; -.
DR   PATRIC; fig|420247.28.peg.871; -.
DR   eggNOG; arCOG00693; Archaea.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000001992; 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   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..571
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000300160"
SQ   SEQUENCE   571 AA;  62633 MW;  EA400AF050B920FB CRC64;
     MQFSAYMLDV ITDSIYPARI SVEGGFFKEI VPIVINDDSE LDISGIILPG FIDSHIHIES
     TMLTPAQFAK LAVRFGTTSV VCDPHEIANV AGTDGIDFMI ENSKSVPFNF YFSIPSCVPA
     TCFETSGAIL DSETIGELLK KDEAVALGEM MNFPGVINGD GEVLAKLEKA KELGKPIDGH
     APLLSGKDLD KYMAEHISTD HECSNFAEAI EKKEKGMKIM VREGSSAKNM EALFDFSDRL
     DYWKNHESFG KMPNEVLEKR IHLPIFDFIV SDDKHTTDLI KGHLNESIKK AIDLEVSPIS
     AIEMVTVNPS THYNLNTGAI VKGMQADYVV VDNLNDLNIL KTYVAGKCVF DGENVLFDVE
     ETEFKNTFDV SKKESEDFEI SCDEPSADVN VIRCFNGELI TEAESATLET KKGFVQPDLE
     EDILKIAVVE RYGGNSIANG FITGFNLKKG AIASSVAHDS HNIVVVGTNS EDMANAVNCL
     IDNEGGFAIV DGDFEDSLAL PIAGLMTNED SHEVAEKLEK LHKTAADFGC KLDSPFMTMS
     FMALLVIPAI KISDKGLFDC INFEFIDVIK N