ID   ADEC_METS4              Reviewed;         564 AA.
AC   B0UDG6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=M446_2226;
OS   Methylobacterium sp. (strain 4-46).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4-46;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL   Submitted (FEB-2008) 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; CP000943; ACA16687.1; -; Genomic_DNA.
DR   RefSeq; WP_012332096.1; NC_010511.1.
DR   AlphaFoldDB; B0UDG6; -.
DR   SMR; B0UDG6; -.
DR   STRING; 426117.M446_2226; -.
DR   EnsemblBacteria; ACA16687; ACA16687; M446_2226.
DR   KEGG; met:M446_2226; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
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..564
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146244"
SQ   SEQUENCE   564 AA;  59003 MW;  B01EDA57B1B71E58 CRC64;
     MSDEIARRIA QGAGRAPADL VIRDARLLDL VTGDLVDTDI AVCGDGIVGT YGEYAGTRVI
     EAEGRVAVPG FIDTHLHVES SLITPHEFDR CVLPHGVTTA IWDPHELANV LGTAAFDYAL
     QAARETVMDI RVQLSSCVPA TDLESSGARI EAEALRPYRD HPGSLGLAEF MNFPGIVAGD
     PACLAKLALF AGRHVDGHAP LLSGRDLNAY VAAGIRTDHE TTGPAEALEK IRKGMTVLIR
     EGSVSKDLRA LAPLLTVATS PFLAFCTDDR NPLDIAEEGH LDALIRMAIG LGVAPLAAYR
     AASLSAATAF GLADRGMIAP GRRADIVLLD DVETCAVARV IAGGRPAEEA LAAPRTRTPA
     PGRGSVKAAP VAPEAFRVAA APGETSVIGV VPGRIITEHR RLTLPARDGA ALCDLAQDAV
     KVAVIARHGA PGMACGFVQG FGLRRGAIAS SVGHDSHNLC VVGADEADMA LAVNRLIALQ
     GGFVVAEGGA VRAELALPIA GLMSDLPFEA VRDALHPLRE AARGLGCTLP EPFLQVAFLP
     LPMIPHLKIT DRGLVDVDRM RILP