ID   ADD_CLOBL               Reviewed;         335 AA.
AC   A7GC28;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   02-SEP-2026, entry version 89.
DE   RecName: Full=Adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_00540};
DE            EC=3.5.4.4 {ECO:0000255|HAMAP-Rule:MF_00540};
DE   AltName: Full=Adenosine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_00540};
GN   Name=add {ECO:0000255|HAMAP-Rule:MF_00540};
GN   OrderedLocusNames=CLI_1072;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium; Clostridium botulinum group.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
CC       deoxyadenosine. {ECO:0000255|HAMAP-Rule:MF_00540}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + H2O + H(+) = inosine + NH4(+);
CC         Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyadenosine + H2O + H(+) = 2'-deoxyinosine + NH4(+);
CC         Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00540};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00540};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00540};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. Adenosine deaminase subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00540}.
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DR   EMBL; CP000728; ABS40607.1; -; Genomic_DNA.
DR   RefSeq; WP_011987906.1; NC_009699.1.
DR   AlphaFoldDB; A7GC28; -.
DR   SMR; A7GC28; -.
DR   KEGG; cbf:CLI_1072; -.
DR   HOGENOM; CLU_039228_0_0_9; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:RHEA.
DR   GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006154; P:adenosine catabolic process; IEA:TreeGrafter.
DR   GO; GO:0043103; P:hypoxanthine salvage; IEA:TreeGrafter.
DR   GO; GO:0046103; P:inosine biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01320; ADA; 1.
DR   FunFam; 3.20.20.140:FF:000093; Adenosine deaminase; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   HAMAP; MF_00540; A_deaminase; 1.
DR   InterPro; IPR028893; A_deaminase.
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; 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; Metal-binding; Nucleotide metabolism; Zinc.
FT   CHAIN           1..335
FT                   /note="Adenosine deaminase"
FT                   /id="PRO_1000017656"
FT   ACT_SITE        200
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   BINDING         278
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
FT   SITE            221
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00540"
SQ   SEQUENCE   335 AA;  37691 MW;  88F7E3CCF3FFB851 CRC64;
     MNFKKLPKIE LHCHLDGSLR VDTILDIAKK DNIPLPSYNK KELINYVSIM DDCNSLDEYL
     NKFFIPNKVM QTKENLKRIA FELLEDVAAD NVKYIEVRFA PLLHVEKGLN IEEIIESVLE
     GIKEAEKLYD IKGNLILGCM RNMDIPSAFE VVKKGAKFIG KGVVAIDLCA GEEPHFPGKY
     IEVLKLAKEC GYRITIHAGE AGVGENVLEA INLLNAERIG HGIYIKDCAE AYKLVKEKNI
     PLEVCPTSNL HTKAFESYET HPFMDFLKDG IKVTINTDNM TVSNTTITKE LEMLNKFCGL
     SIGDYKILYL NAVEASFASS ETKKMLKSYV KEITG
//