ID A0A316TYL2_9ACTN Unreviewed; 359 AA.
AC A0A316TYL2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=DJ010_02790 {ECO:0000313|EMBL:PWN04986.1};
OS Nocardioides silvaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2201891 {ECO:0000313|EMBL:PWN04986.1, ECO:0000313|Proteomes:UP000245507};
RN [1] {ECO:0000313|EMBL:PWN04986.1, ECO:0000313|Proteomes:UP000245507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2018079 {ECO:0000313|EMBL:PWN04986.1,
RC ECO:0000313|Proteomes:UP000245507};
RA Li C., Wang G.;
RT "Nocardioides silvaticus genome.";
RL Submitted (MAY-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:PWN04986.1}.
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DR EMBL; QGDD01000001; PWN04986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316TYL2; -.
DR OrthoDB; 9779574at2; -.
DR Proteomes; UP000245507; 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:UP000245507};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00540}.
FT DOMAIN 16..348
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 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 25
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 298
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 359 AA; 39185 MW; 40D298C47362AECF CRC64;
MEPTRVPTVD ELRSAPKVLL HDHLDGGLRP ATIVELAAES GHELPASDPE SLGAWFAESA
DSGSLVRYLE TFEHTVGVMQ SAPALTRVAR ECAEDLAADG VVYAEIRYAP ELHVQQGLTL
DEVVGAVAEG FAQGVEASGG RIVVRQLLTA MRQAAPSLEI AELAIRYRDH GVAGFDIAGP
EAGYPPTRFL DAFDYVRQEN GHATCHAGEA FGLPSIWEAV QWCGADRLGH GVRIIDDIAV
AEDGTAKLGL LASYVRDKRI PLEMCPSSNL QTGAAPSIAE HPIGLLADLR FRVTVNTDNR
LMSSTSMTRE HQLLCEAFGW GLDKVEWLTV NAMKSAFLPY DERYRLIMDT IKPWYREHA
//
