ID   ADD_CLOBM               Reviewed;         335 AA.
AC   B1KY93;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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}; OrderedLocusNames=CLK_0436;
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
CC       deoxyadenosine. {ECO:0000255|HAMAP-Rule:MF_00540}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine + H(+) + H2O = 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 + H(+) + H2O = 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;
CC         Evidence={ECO:0000255|HAMAP-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; CP000962; ACA56094.1; -; Genomic_DNA.
DR   RefSeq; WP_012343997.1; NC_010520.1.
DR   AlphaFoldDB; B1KY93; -.
DR   SMR; B1KY93; -.
DR   EnsemblBacteria; ACA56094; ACA56094; CLK_0436.
DR   KEGG; cbl:CLK_0436; -.
DR   HOGENOM; CLU_039228_0_0_9; -.
DR   OMA; NHFTIHA; -.
DR   Proteomes; UP000000722; Chromosome.
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:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01320; ADA; 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   PANTHER; PTHR11409; PTHR11409; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01430; aden_deam; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Nucleotide metabolism; Zinc.
FT   CHAIN           1..335
FT                   /note="Adenosine deaminase"
FT                   /id="PRO_1000128837"
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;  37714 MW;  0F4B3D1BF9603E28 CRC64;
     MNFKKLPKIE LHCHLDGSLR VDTILDIAKK DNIHLPSYNK 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 ETKEVLKSYV KEITA