ID A0A1M5QZA8_9ALTE Unreviewed; 335 AA.
AC A0A1M5QZA8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05216361_3974 {ECO:0000313|EMBL:SHH19196.1};
OS Marisediminitalea aggregata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Marisediminitalea.
OX NCBI_TaxID=634436 {ECO:0000313|EMBL:SHH19196.1, ECO:0000313|Proteomes:UP000184520};
RN [1] {ECO:0000313|Proteomes:UP000184520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8995 {ECO:0000313|Proteomes:UP000184520};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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}.
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DR EMBL; FQWD01000007; SHH19196.1; -; Genomic_DNA.
DR RefSeq; WP_073324922.1; NZ_FQWD01000007.1.
DR AlphaFoldDB; A0A1M5QZA8; -.
DR STRING; 634436.SAMN05216361_3974; -.
DR OrthoDB; 105475at2; -.
DR Proteomes; UP000184520; 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 CDD; cd01320; ADA; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000184520};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01962}.
FT DOMAIN 11..331
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
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 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT SITE 220
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
SQ SEQUENCE 335 AA; 38015 MW; 5681E4D6B3D322F2 CRC64;
MNLIKLIHAL PKTELHLHIE GSLEPAMMWN LASKHGVSLP YDSIADIEAA YQFEDLQSFL
DLYYQGADVL RDEDDFYQLM MAYLTRCHDD NVVHAEIMFD PQTHTSRGVG FDVFMPGFER
AIQDAKQKWG ISVYLIMSFL RHLSEKDAID TLNQARAYYP MIKAVGLDSS ELGNPPEKFV
KVFAAARALG FKCVAHAGEE GPPEYIWQAL DLLHVDRIDH GVRCVEDASL MQRLKDEGMP
LTVCPQSNIK LCVFDHMKDH NILSLLDDDL CVTVNADDPS YFGGYLNDNY RALMTHLSMN
ESQLVKLVKN SFVASFLPTD EKNHWLRKID ALAAQ
//
