ID   ADD_VIBVU               Reviewed;         331 AA.
AC   Q8D6Q8;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=VV2_0468;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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; AE016796; AAO07421.1; -; Genomic_DNA.
DR   RefSeq; WP_011081421.1; NC_004460.2.
DR   AlphaFoldDB; Q8D6Q8; -.
DR   SMR; Q8D6Q8; -.
DR   EnsemblBacteria; AAO07421; AAO07421; VV2_0468.
DR   KEGG; vvu:VV2_0468; -.
DR   HOGENOM; CLU_039228_0_0_6; -.
DR   OMA; NHFTIHA; -.
DR   Proteomes; UP000002275; Chromosome 2.
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_0000194400"
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;  36983 MW;  F9166A8937B547F3 CRC64;
     MNYFDLPKID LHCHLDGSVR PQTIIDLADE QNLTLPSRDI NVIKEMMVAP ETCPNLDEYL
     KRFELPGMVM QTAEALERIS FELFEDAANE NVKYLEVRFG PLLHQVKGLS LDDIMDSVVR
     GMKRAEAQYD IHGNYILSIL RTMPKDQIKA VLEAGAKHLN DGIVAFDLAG SEVPGFCHEF
     VPYAQYAKEL GYRITIHAGE QGAGQNVYDA ISLLGAERVG HGIFIHNHPE AYQLVKGEEV
     ALETCPSSNV QTKAVNSLSE HPIKAFYKDG IAVTINTDNR TVSNTTMTDE VRKVVEAFEL
     TEAEYFDIYT ISVNNAFTSD AVKQHLLSFA Q