ID   ADEC2_BRADU             Reviewed;         625 AA.
AC   Q89H53;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Adenine deaminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade2 {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=bll6142;
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; BAC51407.1; -; Genomic_DNA.
DR   RefSeq; NP_772782.1; NC_004463.1.
DR   AlphaFoldDB; Q89H53; -.
DR   SMR; Q89H53; -.
DR   STRING; 224911.27354420; -.
DR   EnsemblBacteria; BAC51407; BAC51407; BAC51407.
DR   KEGG; bja:bll6142; -.
DR   PATRIC; fig|224911.5.peg.6275; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   InParanoid; Q89H53; -.
DR   OMA; CEASHEF; -.
DR   PhylomeDB; Q89H53; -.
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..625
FT                   /note="Adenine deaminase 2"
FT                   /id="PRO_0000142408"
SQ   SEQUENCE   625 AA;  69695 MW;  1C769BA03F284F8A CRC64;
     MRQVMNAIPD DLLITAPDEV RIRQDLVLTA LGHRPADRSL RVGRLLDVHS RTWSEDQEIV
     IKGRRIAWVG PAGSYPGEVR ERVHRPDVAA VPGFGEVHKH IESSHLTPEW EAALVLPHGN
     TWTCEASHEF SNVNGARNLE FWFEARRRGS PLKIFPQPGS AVPPTAYEWG GGWYGRDEQA
     RFMAESLMVT GLDEVMDWPA VWNPDNPSYK RLWGMIEATF AARGVVEGHA SGLRDLPSIN
     AFAAAGLASD HEVQTPEETW DKLTRGLFVE LRVYAMDEIV RWLLAKGLQD WSQIAFTTDD
     RSASHTLELG ASDHNARLAI EAGLAPEIAI QCLTINPARH MRLTPFVGSL APGRFGDVVL
     LSDVGKLTIA EVWADGVQIS EGERYIGQVP EIVWPDWATK TVNIKRSIKP QDFELRAEPG
     RATMKAAVIR PFHWHPEFYT LELPVRDGAV QRDESEAITK FAIVDRFSGD GRIAKMFWRG
     CGPRTPETAV ACSVAHDKHN IWVVGSSDAA MAKAVNALIE LQGGWALVRE GELVATVRFE
     VGGLMSCRSA QALDAEMQAL YAEGRKVDWM YEPTYRPRWY PGFPERLMFA TLTCAPWSWV
     LVAPCEQAPL GFINVQTGEA HPVIW