ID   ADEC_METBF              Reviewed;         551 AA.
AC   Q466H2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=Mbar_A3342;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(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; CP000099; AAZ72220.1; -; Genomic_DNA.
DR   RefSeq; WP_011308260.1; NC_007355.1.
DR   AlphaFoldDB; Q466H2; -.
DR   SMR; Q466H2; -.
DR   STRING; 269797.Mbar_A3342; -.
DR   EnsemblBacteria; AAZ72220; AAZ72220; Mbar_A3342.
DR   GeneID; 3626200; -.
DR   KEGG; mba:Mbar_A3342; -.
DR   eggNOG; arCOG00693; Archaea.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 12286at2157; -.
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..551
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000296736"
SQ   SEQUENCE   551 AA;  60380 MW;  29C26A3E9646A7EF CRC64;
     MQTYQGIIVD AIYRRKFKGE IAVEHGKIIS IEEKEHDIEQ YILPGLVDAH VHIESSMTVP
     SVFARMAVAR GTVAVVSDPH EIANVMGEEG IDYMLEDARK APLKVFFGVP SCVPATPFES
     AGAVLDAEAV DRLLAREDLH YLSEMMNFPG VVMEFPEVIA KLESAKKYGK NIDGHAPGLN
     GTDLQKYVGA GISTDHESFA YEEAVEKIKL GMNILIREGS SARNFDTLYK LIDEYPESVM
     LCTDDSHPDT LIYEGHIDKL LRRGQEKGLD IYNLIRAAVI NPVEHYGLNV GLLREGDPAD
     FIIVDDLKAF NVLKTFIDGS CVYNDGKVLF SVEQAPAKNV FNRNKISVDD VKLAMPASGN
     NGEQMKKIRV IVAQDGELVT GQELALPKVE NGNLISDPAR DILKMVVLSR YADDPVQIGF
     IKNIGLKKGA IASSIAHDSH NIIAVGATDE DIVGAVNRLV ENRGGIVVGT ADNLIDLPLE
     VSGLMSTLDG KEVAVRYEQL NEEARKLGTS LMSPFMTLSF MSLLVIPELK LGDKGLFDVT
     KFEFVELFAG E