ID A0A316C5F8_PSESE Unreviewed; 324 AA.
AC A0A316C5F8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=C7441_106172 {ECO:0000313|EMBL:PWJ84256.1};
OS Pseudaminobacter salicylatoxidans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Pseudaminobacter.
OX NCBI_TaxID=93369 {ECO:0000313|EMBL:PWJ84256.1, ECO:0000313|Proteomes:UP000245396};
RN [1] {ECO:0000313|EMBL:PWJ84256.1, ECO:0000313|Proteomes:UP000245396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6986 {ECO:0000313|EMBL:PWJ84256.1,
RC ECO:0000313|Proteomes:UP000245396};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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: 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:PWJ84256.1}.
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DR EMBL; QGGG01000006; PWJ84256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316C5F8; -.
DR STRING; 1192868.GCA_000304395_00158; -.
DR OrthoDB; 105475at2; -.
DR Proteomes; UP000245396; 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:UP000245396};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01962}.
FT DOMAIN 4..321
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
FT SITE 210
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01962"
SQ SEQUENCE 324 AA; 35496 MW; 79BC0BB6944C8B87 CRC64;
MPLKAELHCH IEGAAAPDLV LRQAEKYGRD VSAVIRDGAF VWHDFTSFLA AYDVASDLFR
TEEDYARLAE HYLTSLARDG AIYSEVFTSP DHAIKAGLSP QAYTDALGEG ILRARDKTGI
EGRMIVTGVR HVGVESIEAA ARFAAKCNHP LVTGFGVAGD ERQGDMEDYV RAFEIAREAG
LGITVHAGEF GGWESVKAAL DHIRPSRIGH GVRAIENPDL VRRIADEGVV LECCPGSNIA
LKVFDDFASH PFLKLQEAGC KVTLNSDDPP YFWTTLKREY EIAATHFGMN DKQLAALTRT
AVEAAFVDRK TKAQLLARLD APKR
//
