ID B1HTW1_LYSSC Unreviewed; 573 AA.
AC B1HTW1;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=adenine deaminase {ECO:0000256|ARBA:ARBA00012782};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782};
GN OrderedLocusNames=Bsph_0221 {ECO:0000313|EMBL:ACA37852.1};
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA37852.1, ECO:0000313|Proteomes:UP000002164};
RN [1] {ECO:0000313|EMBL:ACA37852.1, ECO:0000313|Proteomes:UP000002164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41 {ECO:0000313|EMBL:ACA37852.1,
RC ECO:0000313|Proteomes:UP000002164};
RX PubMed=18296527; DOI=10.1128/JB.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000256|ARBA:ARBA00006773}.
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DR EMBL; CP000817; ACA37852.1; -; Genomic_DNA.
DR RefSeq; WP_012292021.1; NC_010382.1.
DR AlphaFoldDB; B1HTW1; -.
DR EnsemblBacteria; ACA37852; ACA37852; Bsph_0221.
DR KEGG; lsp:Bsph_0221; -.
DR HOGENOM; CLU_027935_0_0_9; -.
DR Proteomes; UP000002164; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR026912; Adenine_deam_C.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11113:SF6; ADENINE DEAMINASE YERA-RELATED; 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|ARBA:ARBA00022801, ECO:0000313|EMBL:ACA37852.1}.
FT DOMAIN 75..355
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 421..564
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 573 AA; 64621 MW; 83B66F63117DA9AD CRC64;
MDPVWKITKI RQQLAVIDGK KAPDIVLKNA RYLHSMMKQW IVGNIWILGD RIVYAGDRMP
PLIEGTQVVD CTGKTVVPGY IEPHVHPFQL YHPQSFADFC GQLGTTTFIS DNLSFVLNLE
NKKAFSILDH LKKLPFSFYW WTRFDSQTEL EQEEEVFSNT SILEWLERSD VLLGGELTGW
PKLLHGDDQM LYRMQMAKGL GKKIEGHFPG ASERTLARMK LLGADGDHEA MTVEEVERRI
MQGYAVTLRH SSIRPDLPHL LKGIVEKELP IFDHLMMTTD GSPPSFHEDG VMDKCIQAAL
DAGVSPIDAY QMASYNVARY YNMSNLHGFI ATGRFASLNI LQDEYHPVPE SVLSKGVWLK
RDGDRVHRLA AIDYSAIPAF HLDFSLDAQD FQFSMPFGIQ LVNDVITKPY NSLITREGQL
ADHDECYLML INRQGHWHVN TMIKGFATGV QGFASSYSNT GDILLIGKNK EDMIKAFEEM
KAMNGGIVLV EKGEVIADIP LSIGGLLYDG DVLTLAEKEK ALKQALAERG YHLGDAIYTL
LFLQSTHLPY IRITPKGIFD VMKNKLLLPA VMR
//
