ID A0A1B9NBK1_9MICO Unreviewed; 349 AA.
AC A0A1B9NBK1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 Name=add {ECO:0000313|EMBL:QBR74720.1};
GN ORFNames=A7J15_07120 {ECO:0000313|EMBL:OCG73966.1}, E3O41_10155
GN {ECO:0000313|EMBL:QBR74720.1};
OS Microbacterium sediminis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=904291 {ECO:0000313|EMBL:OCG73966.1, ECO:0000313|Proteomes:UP000093355};
RN [1] {ECO:0000313|EMBL:OCG73966.1, ECO:0000313|Proteomes:UP000093355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-01 {ECO:0000313|EMBL:OCG73966.1,
RC ECO:0000313|Proteomes:UP000093355};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QBR74720.1, ECO:0000313|Proteomes:UP000295661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-01 {ECO:0000313|EMBL:QBR74720.1,
RC ECO:0000313|Proteomes:UP000295661};
RA Yu L.;
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QBR74720.1, ECO:0000313|Proteomes:UP000295661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-01 {ECO:0000313|EMBL:QBR74720.1,
RC ECO:0000313|Proteomes:UP000295661};
RA Xu X.;
RT "Genomic analysis of Microbacterium sediminis YLB-01 reveals backgrounds
RT related to its deep sea enviroment adaptation.";
RL Submitted (APR-2019) 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; LXMD01000023; OCG73966.1; -; Genomic_DNA.
DR EMBL; CP038256; QBR74720.1; -; Genomic_DNA.
DR RefSeq; WP_067026374.1; NZ_KV744784.1.
DR AlphaFoldDB; A0A1B9NBK1; -.
DR STRING; 904291.A7J15_07120; -.
DR KEGG; msed:E3O41_10155; -.
DR OrthoDB; 105475at2; -.
DR Proteomes; UP000093355; Unassembled WGS sequence.
DR Proteomes; UP000295661; Chromosome.
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, ECO:0000313|EMBL:QBR74720.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01962};
KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01962};
KW Reference proteome {ECO:0000313|Proteomes:UP000093355};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01962}.
FT DOMAIN 18..337
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT SITE 229
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
SQ SEQUENCE 349 AA; 38558 MW; 7194C5FA9CCC1CD4 CRC64;
MSHTTAPPSL REFAFGLPKA ELHLHLEGTL EPELKFALAA RNGVELAEKT VSEVTATYDF
TDLTSFLAVY YPAMRVLQTA EDFHDLAWAY LQRAKEHGVV HVEMFFDPQA HTSRGVPFDT
VVSGYRRAAV RAQRELGVSA ELILCFLRDF SAEYAMATLM EALPYKAWIV GVGLDSDERD
NPPAKFAEVF ARAKAEGFLT TMHCDIDQAG SLENIRTVIE EIGVDRIDHG TNIVEDPELV
ELARQRGLGF TCCPVSNSFV TEQMKTDEIV GLLRRGVKVT VNSDDPAYFG AYVADNYIAL
AEKAGLSHAD LAQLAINSFD ASWMTPARRT AHVDAVRRYA AEHGVTLPS
//
