ID A0A078KNL5_9FIRM Unreviewed; 339 AA.
AC A0A078KNL5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=CCDG5_0954 {ECO:0000313|EMBL:CDZ24073.1};
OS [Clostridium] cellulosi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=29343 {ECO:0000313|EMBL:CDZ24073.1, ECO:0000313|Proteomes:UP000032431};
RN [1] {ECO:0000313|Proteomes:UP000032431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5 {ECO:0000313|Proteomes:UP000032431};
RA Wibberg D.;
RL Submitted (JUL-2014) 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}.
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DR EMBL; LM995447; CDZ24073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078KNL5; -.
DR STRING; 29343.CCDG5_0954; -.
DR KEGG; ccel:CCDG5_0954; -.
DR PATRIC; fig|29343.3.peg.1007; -.
DR HOGENOM; CLU_039228_0_0_9; -.
DR OrthoDB; 9779574at2; -.
DR Proteomes; UP000032431; Chromosome.
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 CDD; cd01320; ADA; 1.
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:UP000032431};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00540}.
FT DOMAIN 8..332
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
FT SITE 222
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00540"
SQ SEQUENCE 339 AA; 38190 MW; 577C65297BD5A35E CRC64;
MDFIERMPKI DLHNHLDGSL RPRTVIEIAR DEGIELPTYD EKELMKYLSV GDNCESLVEY
LEKFDLPLKC LQSEKAQRRV AKEAVEDAAK HNVKYIEVRF APQLMTEKGM TCADVIRNVI
SGLLEGEKET GTIARAIVCC MRHHSDEKNL EVIRAASEFM YRGLGGVDLA GDEAHYPPQL
FKRVFDEANK YGIPVTIHAG EAGGAENVRV AIEELGAVRI GHGIRINEDE SVVNLVKERK
IPLEICVTSN VQTKAAPSFE QHPVRKYFDL GLNVTVNTDN TTVSNTDMKR ELNILKNKFG
FSNSELMQLQ MNAARAAFLD KPEKEKLLSE LKNSFENII
//
