ID   ADEC_METNO              Reviewed;         565 AA.
AC   B8IB34;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=Mnod_0385;
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL   Submitted (JAN-2009) 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; CP001349; ACL55427.1; -; Genomic_DNA.
DR   RefSeq; WP_015927138.1; NC_011894.1.
DR   AlphaFoldDB; B8IB34; -.
DR   SMR; B8IB34; -.
DR   STRING; 460265.Mnod_0385; -.
DR   EnsemblBacteria; ACL55427; ACL55427; Mnod_0385.
DR   KEGG; mno:Mnod_0385; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000008207; 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..565
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000185089"
SQ   SEQUENCE   565 AA;  59016 MW;  BC0D44384ACD7401 CRC64;
     MPAEIARRIA QGAGREPADL VIRGARLLDL VTGELVPTDI AVCGEVVVGT YGEYEGARVI
     EAASRIAVPG FIDTHLHIES SLITPHEFDR CVLPHGVTTA IWDPHELANV LGTAAFDYAL
     QASTETAMDI RVQLSSCVPA TDLESAGARI EAADLLPYRD HPRSLGIAEF MNFPGVVQAD
     PGCLAKLAAF AGRHVDGHAP LLSGSGLNAY AAAGIRTDHE ATGAAEALEK IRKGMTVLIR
     EGSVSKDLAA LAPLLTVATS PFLAFCTDDR NPLDIAEEGH LDHLIRTAIR LGVPPLAAYR
     AASLSAATAF GLTDRGMIAP GRRADIVLLD DLEACAVARV IAGGRAVEEA LFAGRARTPA
     PGRGSVKAAP VAAEDFRIPG ADGAETSVIG VVPGRIITEH RRLELPAANG CAGCDLDQDV
     VKVAVIARHG RPGMGRGFVQ GFGLRRGAIA SSVGHDSHNL CVVGADDADM AVAINRLIAL
     QGGFVVAAGG TVLAELALPI AGLMSDLPFE AVRDALHPLR EAARTLGCTL PEPFLQVAFL
     PLPVIPHLKI TDRGLVDVDR MRLLG