ID   I1DXC8_9GAMM            Unreviewed;       408 AA.
AC   I1DXC8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE            EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN   Name=add {ECO:0000313|EMBL:GAB58706.1};
GN   ORFNames=RNAN_1693 {ECO:0000313|EMBL:GAB58706.1};
OS   Rheinheimera nanhaiensis E407-8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB58706.1, ECO:0000313|Proteomes:UP000004374};
RN   [1] {ECO:0000313|EMBL:GAB58706.1, ECO:0000313|Proteomes:UP000004374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E407-8 {ECO:0000313|EMBL:GAB58706.1,
RC   ECO:0000313|Proteomes:UP000004374};
RX   PubMed=23209246; DOI=10.1128/JB.01922-12;
RA   Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., Zhou B.-C.,
RA   Zhang Y.-Z.;
RT   "Genome Sequence of the Protease-Producing Bacterium Rheinheimera
RT   nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South China
RT   Sea.";
RL   J. Bacteriol. 194:7001-7002(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAB58706.1}.
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DR   EMBL; BAFK01000008; GAB58706.1; -; Genomic_DNA.
DR   RefSeq; WP_008220624.1; NZ_BAFK01000008.1.
DR   AlphaFoldDB; I1DXC8; -.
DR   STRING; 562729.RNAN_1693; -.
DR   OrthoDB; 105475at2; -.
DR   Proteomes; UP000004374; Unassembled WGS sequence.
DR   GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
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   Hydrolase {ECO:0000313|EMBL:GAB58706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004374}.
FT   DOMAIN          13..382
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   408 AA;  46631 MW;  746861C85BFA0CE2 CRC64;
     MPRYSAEFIK EMPKSDLHLH LDGSLRLDSL LEMAKRTGTK LPADSVEGLK QRVFKEKYNN
     LGEYLHCFQY TCAVLRDMEN LERAAYELAI DNQLEGVNYI EVRFAPQLLI DLANGIDFDR
     VMHAVNNGLK RAMSEYNRSE VVLSGHKPPF AYGIINCAMR MFGDKGFSPY YTNLFQLMRD
     FAPMDVIKLA AMELVRASVR LRDEEGVPIV GLDLAGQESG YPASKFKEVY EYAHQHFLLK
     TLHAGEAYGA ESVFEAITEC YADRIGHGYS MFIPQMITDP DITDKAAYIR NLASYIADKR
     IAIEVCLTSN LQTNPAISDI KQHKFKAMLD NRMATVICTD NRLVSNTTVS REYQLALDNF
     DIPLKRLKDI VAYGFKKSFF PGSYVEKREY AKQCLEYFDR VAQRYGFI
//