ID A0A0P0D813_9FLAO Unreviewed; 539 AA.
AC A0A0P0D813;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Adenine deaminase {ECO:0000256|ARBA:ARBA00012782, ECO:0000256|HAMAP-Rule:MF_01518};
DE Short=Adenase {ECO:0000256|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase {ECO:0000256|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782, ECO:0000256|HAMAP-Rule:MF_01518};
GN Name=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN ORFNames=APS56_00865 {ECO:0000313|EMBL:ALJ03788.1};
OS Pseudalgibacter alginicilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pseudalgibacter.
OX NCBI_TaxID=1736674 {ECO:0000313|EMBL:ALJ03788.1, ECO:0000313|Proteomes:UP000057981};
RN [1] {ECO:0000313|EMBL:ALJ03788.1, ECO:0000313|Proteomes:UP000057981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ-22 {ECO:0000313|Proteomes:UP000057981};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000479, ECO:0000256|HAMAP-
CC Rule:MF_01518};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01518};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000256|ARBA:ARBA00006773,
CC ECO:0000256|HAMAP-Rule:MF_01518}.
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DR EMBL; CP012898; ALJ03788.1; -; Genomic_DNA.
DR RefSeq; WP_054723891.1; NZ_CP012898.1.
DR AlphaFoldDB; A0A0P0D813; -.
DR STRING; 1736674.APS56_00865; -.
DR KEGG; ahz:APS56_00865; -.
DR PATRIC; fig|1736674.3.peg.186; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000057981; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR CDD; cd01295; AdeC; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR HAMAP; MF_01518; Adenine_deamin; 1.
DR InterPro; IPR006679; Adenine_deam.
DR InterPro; IPR026912; Adenine_deam_C.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01178; ade; 1.
DR PANTHER; PTHR11113:SF2; ADENINE DEAMINASE; 1.
DR PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR Pfam; PF13382; Adenine_deam_C; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000057981}.
FT DOMAIN 40..320
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 367..532
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 539 AA; 59464 MW; 059ACD37D6E2D3CD CRC64;
MKLQGQIVDI QHKRIYKGEI TFENGKIISI DKKQHDISNY ILPGFIDAHI HIESSMLVPS
EFAKLAVKYG TVATVSDPHE IANVLGVMGV EFMVENGKKV PFKFNFGAPS CVPATHFESA
GAVIDSDDIK KLLENPDIKY LAEMMNYPGV LFDDAAVLKK IAWANYYNKP IDGHAPGIKG
NDISKYIDAG ISTDHECFTY EEALEKLQKG MKILIREGSA AKNFEALIDL LPKYFENMMF
CSDDKHPDDL LIGHINQLCS RAVSKGIDVF KVLQVACINP VSHYNLDVGL LKINDDADFI
VVEDLKDFNT LQTYINGELV FDKGISLIET ISFKNLNNFN CNTKEVSDFK IASSTQKIRV
IEALEGQLVT NELVEEALIE NGNLVSNVEK DILKITVVNR YQNQKPAMAF IKNFGLKEGA
IASSVGHDSH NIIAVGVSDE AICKAVNLII ENKGGICAVS NFKEKIVSLP VAGIMSDKNG
GIIGKQYAEL DDMAKQMGSN LHAPFMTLSF MALLVIPTLK LSDKGLFNGS DFKFIPLEV
//
