ID   ADDL_STRVG              Reviewed;         339 AA.
AC   P53984;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Putative adenosine/adenine deaminase;
DE            EC=3.5.4.-;
DE   AltName: Full=Adenosine aminohydrolase;
OS   Streptomyces virginiae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces virginiae group.
OX   NCBI_TaxID=1961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8675024; DOI=10.1016/0378-1119(96)00067-4;
RA   Katayama M., Sakai Y., Okamoto S., Ihara F., Nihira T., Yamada Y.;
RT   "Gene organization in the ada-rplL region of Streptomyces virginiae.";
RL   Gene 171:135-136(1996).
CC   -!- FUNCTION: Putative nucleoside deaminase. May catalyze the hydrolytic
CC       deamination of adenosine or some similar substrate and play a role in
CC       purine metabolism (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000305}.
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DR   EMBL; D50624; BAA09298.1; -; Genomic_DNA.
DR   PIR; T11785; T11785.
DR   RefSeq; WP_033225040.1; NZ_JNYC01000038.1.
DR   AlphaFoldDB; P53984; -.
DR   SMR; P53984; -.
DR   STRING; 1961.JOAK01000021_gene7142; -.
DR   eggNOG; COG1816; Bacteria.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01320; ADA; 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   PANTHER; PTHR43114; PTHR43114; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01430; aden_deam; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Nucleotide metabolism; Zinc.
FT   CHAIN           1..339
FT                   /note="Putative adenosine/adenine deaminase"
FT                   /id="PRO_0000194395"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            224
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  37181 MW;  7C1C221FB927E5AD CRC64;
     MEHARDLTLL PKAHLHLHFT GSMRPSTLLE LADKYGVRLP DALTAGEPPK LRATDERGWF
     RFQRLYDAAR SCLREPDDIR RLVREAAEED VRDGSGWLEI QVDPTSYAPL LGGMIPAVEI
     ILDAVDAASR ETGLGMRVLI AANRMKHPLD ARTLARLAVR YADRGIVGFG LSNDERRGMA
     RDFDRAFAIA REGGLLAAPH GGELTGPSSV RDCLDDLHAS RIGHGVRAAE DPRLLKRLAD
     RQITCEVCPA SNVALGVYER PEDVPLRTLF EAGVPMALGA DDPLLFGSRL AAQYEIARRH
     HAFTDTELAE LARQSVRGSA APDDVQAKLL AGIDHWLTG