ID   ADEC1_BRADU             Reviewed;         600 AA.
AC   Q89QG3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Adenine deaminase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade1 {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=blr3165;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC48430.1; -; Genomic_DNA.
DR   RefSeq; NP_769805.1; NC_004463.1.
DR   RefSeq; WP_011085949.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89QG3; -.
DR   SMR; Q89QG3; -.
DR   STRING; 224911.27351423; -.
DR   PRIDE; Q89QG3; -.
DR   EnsemblBacteria; BAC48430; BAC48430; BAC48430.
DR   GeneID; 64022919; -.
DR   KEGG; bja:blr3165; -.
DR   PATRIC; fig|224911.44.peg.2806; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   InParanoid; Q89QG3; -.
DR   OMA; MVTACAY; -.
DR   PhylomeDB; Q89QG3; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IBA:GO_Central.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..600
FT                   /note="Adenine deaminase 1"
FT                   /id="PRO_0000142407"
SQ   SEQUENCE   600 AA;  64149 MW;  FB3193C08C6A7DA4 CRC64;
     MTRLTRFAVA PLHSMTRRLA DVASARVAPD LVVTGARVLS TYSERIHANR EVWITGGRVA
     AVKPAGTARK AWSGVALYDA AGAIIAPGLV DPHIHIESSM VTACAYAEAA LLNGTTTIFC
     DSHEIGNVMD VAGVEAMLED ARQAPLSIFL TVPSTVPATS AELETAGGDL TPDKIAGLFD
     RWPEAVALGE KMDFVPVTMG DERSHAILAA ALKRGRPVSG HVYGREFVAA YAASGVTDTH
     EAIDRDIADD LLDAGVWVFL RGGPPTTPWH SLPQAIRTIT ELGASHKRTA VCTDDRDADD
     LLLFGLDWVV REAVKAGMSP EQAWSMGSLH GATRFGMEGD IGGLGGGRRA DLVLMDDQLK
     PQCTWYGGEL VVEHGKITPR LDQALSQRYQ YPKAAYATVK LPEKVKLTPE LPAKACTVNA
     IKTALPGITL IHEKVAIEPA KDWPTLFARY GLCFVTVVER HGKSAGNVAY GLLKDFGLKR
     GAVASSVGHD SHNIIVAGTN EPDMQVAIAA IKEHQGAVCV VADGKVRALV PLPIAGLLSD
     KRVTEVAEEV KVLKKEWAEA GCTIPYMGFN LIPLSVIPEI RITDKGLVLV PQMELAPLFE