ID   ADEC_METMJ              Reviewed;         518 AA.
AC   A3CVR8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Memar_1539;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN57468.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3CVR8; -.
DR   SMR; A3CVR8; -.
DR   STRING; 368407.Memar_1539; -.
DR   EnsemblBacteria; ABN57468; ABN57468; Memar_1539.
DR   KEGG; mem:Memar_1539; -.
DR   eggNOG; arCOG00693; Archaea.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000002146; 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..518
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292403"
SQ   SEQUENCE   518 AA;  55311 MW;  1B35F0DA990B03CB CRC64;
     MDFGVKDGRI IGFGEYRGTR EYDLSGAYVV PGLIDAHVHI ESSLLAPAEY ARLVLAHGTT
     TVIADPHEIA NVCGAPGIDY MLAQGARTPL DILVMLPSCV PATPFDAGGA VLTAADLARF
     RGREGVVGLA EVMNVPGVLF GDEDLRAKMD LFEVVDGHAP FLSGKDLNAY IYAGVQSDHE
     CTALPEAREK LLRGMYVMIR EGSTERNLHD LLPLVDACTA PRCCFATDDR HADMLAGEGH
     IDDCVRKAVS GGLEVEQALR MATLSAAGRF GLHDRGALAP GRLADFCVAD DPDRFRVLRT
     FKRGVEVVDA GYLPPACPKS PMHARVPEPG DIRITGRGEA RVIEIVPGQI TTRDLRYPVD
     AAGIPDLDRD ILKAVVIDRY RATGSGVGLV HGFHLQEGAI AGSVSHDSHN IVAVGAGDAD
     IVRAVAEVVR LGGGLAVVSG DDITALPLEC AGLMSALPYD EVVRRLAALE EHARRLGAIA
     NPFMYLSFLA LTVIPEVRVT ERGVFDVGAF TDVPLFEE