ADD_CLOB6
ID ADD_CLOB6 Reviewed; 331 AA.
AC C3L357;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=CLJ_B1035;
OS Clostridium botulinum (strain 657 / Type Ba4).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=515621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=657 / Type Ba4;
RA Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL Submitted (MAY-2008) 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 + 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; CP001083; ACQ54388.1; -; Genomic_DNA.
DR RefSeq; WP_003360944.1; NC_012658.1.
DR AlphaFoldDB; C3L357; -.
DR SMR; C3L357; -.
DR EnsemblBacteria; ACQ54388; ACQ54388; CLJ_B1035.
DR KEGG; cbi:CLJ_B1035; -.
DR HOGENOM; CLU_039228_0_0_9; -.
DR OMA; NHFTIHA; -.
DR Proteomes; UP000002333; 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..331
FT /note="Adenosine deaminase"
FT /id="PRO_1000211946"
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 170
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 331 AA; 37561 MW; C67273961784FC2B CRC64;
MNFKKLPKIE LHCHLDGSLR VDTILDIAKK DNIPLPSYNE KELINYVSIM DDCNSLDEYL
NKFFIPNKVM QTKENLKRIA FELLEDVAAD NVKYIEVRFA PLLHVEKGLN IEEIIESVLE
GIKEAEKLYD IKGNLILGCM RNMDIPSAFE VVKKGAKFIG KGVVAIDLCG GEEPHFPGKY
VEVLKLAKEY GYRITIHAGE AGVGENVLEA INLLNAERIG HGIYIKNCAE AYKLVKEKNI
PLEVCPTSNL HTKAFESYET HPFMDFLKDD IKITINTDNM TVSNTTITKE LEMLNKFCGL
SIEDYKTIYL NSVEAAFTTK EAKKRLKKFV E