ID   A0A1G7BBJ7_9PROT        Unreviewed;       530 AA.
AC   A0A1G7BBJ7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE            EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN   ORFNames=SAMN04488071_2445 {ECO:0000313|EMBL:SDE24393.1};
OS   Kordiimonas lacus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC   Kordiimonadaceae; Kordiimonas.
OX   NCBI_TaxID=637679 {ECO:0000313|EMBL:SDE24393.1, ECO:0000313|Proteomes:UP000183685};
RN   [1] {ECO:0000313|EMBL:SDE24393.1, ECO:0000313|Proteomes:UP000183685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9109 {ECO:0000313|EMBL:SDE24393.1,
RC   ECO:0000313|Proteomes:UP000183685};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
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DR   EMBL; FNAK01000005; SDE24393.1; -; Genomic_DNA.
DR   RefSeq; WP_068307554.1; NZ_LRUA01000007.1.
DR   AlphaFoldDB; A0A1G7BBJ7; -.
DR   STRING; 637679.GCA_001550055_03610; -.
DR   Proteomes; UP000183685; Unassembled WGS sequence.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProt.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR   PANTHER; PTHR11409:SF43; ADENOSINE DEAMINASE; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000183685};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..530
FT                   /note="adenosine deaminase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010339606"
FT   DOMAIN          248..470
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   530 AA;  58857 MW;  BE3549F203C08CE8 CRC64;
     MRDGKISLIR QAVRAMLGGL VASLLVVAAT PAGAQDDDQR AVKARMAGSA LSWAAENGRL
     RQFMEAFPKG GDIHSHLRGA IYAESWLEWA AADGLCADMS VPALRFKVKD SCAASGWLTA
     GEAQANEDHR RELINSLSNR SYVPTLNWSG HNDFFATFAR ISASPKRLGD QLANVAARAG
     RQNILYLELM ETIILPELFP LLSGVQLSSD LAADYQTLMS GPFGQAMPTL VASARTQIAA
     ARARKDQLLR CGTANADAGC GVKIRFLHQV IREFEPAMVY GQMILGWALM KDEPMMLGMN
     LVAPEDGRVA LRDYKLHMRM IDHLYTNLGP RNVALHAGEL TMGLVRPKQL TFHIRDAIEV
     GHAKRIGHGI AVGYERDSEG LLKKMAQEGI MVEINLTSND TILGVKGKDH PLVLYRDMLV
     PYALSTDDEG VSRIDLTHEY MRLYTEHRVP YFELRHSARN SLTYSFLPGD SLWESEACKK
     DVETGAQAGA ECAAFLETSE KAKLQWELEE RLRVFEDERR IPERKRTSFK
//