ID   A0A1H4BHW9_9GAMM        Unreviewed;       518 AA.
AC   A0A1H4BHW9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE            EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN   ORFNames=SAMN05660964_01672 {ECO:0000313|EMBL:SEA47763.1};
OS   Thiothrix caldifontis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thiothrix.
OX   NCBI_TaxID=525918 {ECO:0000313|EMBL:SEA47763.1, ECO:0000313|Proteomes:UP000199397};
RN   [1] {ECO:0000313|EMBL:SEA47763.1, ECO:0000313|Proteomes:UP000199397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21228 {ECO:0000313|EMBL:SEA47763.1,
RC   ECO:0000313|Proteomes:UP000199397};
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; FNQP01000008; SEA47763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4BHW9; -.
DR   STRING; 525918.SAMN05660964_01672; -.
DR   OrthoDB; 105475at2; -.
DR   Proteomes; UP000199397; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199397};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..518
FT                   /note="adenosine deaminase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011473492"
FT   DOMAIN          242..460
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   518 AA;  57011 MW;  BC6F06E020CB88D2 CRC64;
     MVSLLKVCGV VVVASFLSSC ASVGESVPNL ITTAADDLSG STAKTAQWFA DNRNSPLRLR
     AFLKKMPKGG DIHTHLSGAV YAESYLQWAT DEKLCVNPET GVISENNHEP CQVKPEVPVA
     TAMKDSELYG KLVDKMSLRN LEYAEQSGHD QFFEAFAKFA GGSKGQMIAE LSNRASRQNI
     AYLEMLITVG KKYSKQFSQQ VRFDGDIDAA YQQIITAGLK ATIPAGQREL QGVEQQAKAV
     LACDSANAQA GCAVERRYLL QINRTGEPSR VFAEMVYAFE TVKAEPLAVG VNMVAPEDNV
     VALRDYDLHM RMMGYLSARY PSVSISLHAG ELALGLVPPD HLHDHIRKAV EIAGAKRIGH
     GVDVMHEDNP FQLLKTMKDK NVLVEVCLTS NDAILGVEGK QHPFPEYLNA GVPATLASDD
     EGISRIDLTH EYQRAALDYG LSYPDLKTLA RNSIHYAFLK GESLWTNPTY RQIQPVCNKA
     DVAELSASCQ QFLNANDKAK VEWTLEKQFR AFENGSWM
//