ID   A0A1C4M683_9ACTN        Unreviewed;       340 AA.
AC   A0A1C4M683;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Adenosine deaminase {ECO:0000313|EMBL:SCD81435.1};
GN   ORFNames=GA0115234_1049132 {ECO:0000313|EMBL:SCD81435.1};
OS   Streptomyces sp. DvalAA-43.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839762 {ECO:0000313|EMBL:SCD81435.1, ECO:0000313|Proteomes:UP000199186};
RN   [1] {ECO:0000313|EMBL:SCD81435.1, ECO:0000313|Proteomes:UP000199186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DvalAA-43 {ECO:0000313|EMBL:SCD81435.1,
RC   ECO:0000313|Proteomes:UP000199186};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; FMBW01000037; SCD81435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4M683; -.
DR   OrthoDB; 105475at2; -.
DR   Proteomes; UP000199186; Unassembled WGS sequence.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   GO; GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IEA:UniProt.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01430; aden_deam; 1.
DR   PANTHER; PTHR43114; ADENINE DEAMINASE; 1.
DR   PANTHER; PTHR43114:SF6; ADENINE DEAMINASE; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
FT   DOMAIN          9..334
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   340 AA;  36862 MW;  ED5A269E75ED0A4B CRC64;
     MERDVRLLPK AHLHLHFTGS MRPTTLLELA DKYGVHLPDA LTGGEPPKLR ATDERGWFRF
     QRLYDIARSC LRAPEDIQRL VREAAQEDVA DGSGWMEIQV DPTSYAPLLG GLIPAIEIIL
     DAVDSASRET GLPIRVVIAA NRMKHPLDAR TLARLAVRYV DRGVVGFGLS NDERRGMARD
     FDRAFAIARE GGLLAAPHGG ELSGPASVRD CLDDLDAARI GHGVRAAEDP RLLRTLAERG
     VTCEVCPSSN VALGVYEKPA DVPLRTLFEA GVPMALGADD PLLFGSRLAA QYDLVRRHHG
     FTDAELAELA RQSVRGSAAP APVRAELLAG VDDWLAKPAG
//