ID A0A1C4R4W1_9ACTN Unreviewed; 338 AA.
AC A0A1C4R4W1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Adenine deaminase {ECO:0000256|HAMAP-Rule:MF_01962};
DE Short=ADE {ECO:0000256|HAMAP-Rule:MF_01962};
DE EC=3.5.4.2 {ECO:0000256|HAMAP-Rule:MF_01962};
DE AltName: Full=Adenine aminohydrolase {ECO:0000256|HAMAP-Rule:MF_01962};
DE Short=AAH {ECO:0000256|HAMAP-Rule:MF_01962};
GN ORFNames=GA0115234_10768 {ECO:0000313|EMBL:SCE29950.1};
OS Streptomyces sp. DvalAA-43.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839762 {ECO:0000313|EMBL:SCE29950.1, ECO:0000313|Proteomes:UP000199186};
RN [1] {ECO:0000313|EMBL:SCE29950.1, ECO:0000313|Proteomes:UP000199186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DvalAA-43 {ECO:0000313|EMBL:SCE29950.1,
RC ECO:0000313|Proteomes:UP000199186};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenine to
CC hypoxanthine. Plays an important role in the purine salvage pathway and
CC in nitrogen catabolism. {ECO:0000256|HAMAP-Rule:MF_01962}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenine + H(+) + H2O = hypoxanthine + NH4(+);
CC Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01962};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01962};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01962};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenine deaminase type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01962}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01962}.
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DR EMBL; FMBW01000060; SCE29950.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4R4W1; -.
DR OrthoDB; 9779574at2; -.
DR Proteomes; UP000199186; Unassembled WGS sequence.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043103; P:hypoxanthine salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR HAMAP; MF_01962; Adenine_deaminase; 1.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR028892; ADE.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01430; aden_deam; 1.
DR PANTHER; PTHR43114; ADENINE DEAMINASE; 1.
DR PANTHER; PTHR43114:SF6; ADENINE DEAMINASE; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01962};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01962};
KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01962};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01962}.
FT DOMAIN 13..333
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT SITE 224
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
SQ SEQUENCE 338 AA; 37154 MW; 828301FB6AF9EC5A CRC64;
MTTTIDAFIA GLPKCELHLH IEGTLEPGLK FALAERNGIE LPYTDEAALQ AAYDFDDLPG
FLAVYYEGMS VLRTEQDFYD LAAAYAAKAH SQNVRYAEIF FDPQAHTARG VSFDTVIRGL
TRALDDAGRA TGFTGRLVMC FLRDFQAEFA MATLVQSLPY KDWIVGVGLD SDEAGNPPVK
FREVFARARA EGYRMTMHCD VDQKNSTEHI RQVIEEIGVD RIDHGVNALE DPALIAAIRE
KGLGLTVCPI SNSHVTDGPK AAEIRALLDQ GVKVTVNSDD PAYFPGYVAE NLAVLRPAPA
SLTDADLVRL QRNAIDISWA APAIRDRFLA ELDAYANR
//
