ID A0A495JI72_9ACTN Unreviewed; 358 AA.
AC A0A495JI72;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Adenosine deaminase {ECO:0000256|ARBA:ARBA00012784, ECO:0000256|HAMAP-Rule:MF_00540};
DE EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784, ECO:0000256|HAMAP-Rule:MF_00540};
DE AltName: Full=Adenosine aminohydrolase {ECO:0000256|ARBA:ARBA00031852, ECO:0000256|HAMAP-Rule:MF_00540};
GN Name=add {ECO:0000256|HAMAP-Rule:MF_00540};
GN ORFNames=BDK92_2935 {ECO:0000313|EMBL:RKR88607.1};
OS Micromonospora pisi.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR88607.1, ECO:0000313|Proteomes:UP000277671};
RN [1] {ECO:0000313|EMBL:RKR88607.1, ECO:0000313|Proteomes:UP000277671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR88607.1,
RC ECO:0000313|Proteomes:UP000277671};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
CC deoxyadenosine. {ECO:0000256|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:0000256|ARBA:ARBA00034443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191;
CC Evidence={ECO:0000256|ARBA:ARBA00034443};
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:0000256|ARBA:ARBA00001600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC Evidence={ECO:0000256|ARBA:ARBA00001600};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00540};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00540};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenosine deaminase subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00540}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00540}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKR88607.1}.
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DR EMBL; RBKT01000001; RKR88607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495JI72; -.
DR OrthoDB; 9779574at2; -.
DR Proteomes; UP000277671; Unassembled WGS sequence.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
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 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00540};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00540};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080, ECO:0000256|HAMAP-
KW Rule:MF_00540}; Reference proteome {ECO:0000313|Proteomes:UP000277671};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00540}.
FT DOMAIN 13..350
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT SITE 230
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
SQ SEQUENCE 358 AA; 38806 MW; 7ADF93CC6BD784A7 CRC64;
MVAIGYEDIV KAPKALLHDH LDGGLRPATI IELADAIGHP LPSTDPEELG RWFVTAADSG
SLERYLETFA HTVAVMQTAD ALRRVAAECA LDLAADGVVY AEVRFAPEQH LDHGLTLDEV
VEATVAGFAE GTALAAAAGQ RIRIGTLLTA MRHAARSQEI AELAVRFRDS GVVGFDIAGA
EAGFPPTRHL DAFEYLQREN FHFTIHAGEA FGLPSIWQAI QWCGADRLGH GVRIVDDITT
GATPVLGRLA AYVRDKRIPL ELCPSSNVQT GAAASIAEHP IGLLRDLRFR ATVNTDNRLM
SGTSMSREMA LLVEAFGYGW AELQWFTINA MKSAFIPFDE RLAIIDEVIK PGYAKLLP
//
