ID A0A143HEB0_9BACL Unreviewed; 576 AA.
AC A0A143HEB0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=adenine deaminase {ECO:0000256|ARBA:ARBA00012782};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782};
GN ORFNames=ATY39_11960 {ECO:0000313|EMBL:AMX00075.1};
OS Rummeliibacillus stabekisii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX NCBI_TaxID=241244 {ECO:0000313|EMBL:AMX00075.1, ECO:0000313|Proteomes:UP000076021};
RN [1] {ECO:0000313|EMBL:AMX00075.1, ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|EMBL:AMX00075.1,
RC ECO:0000313|Proteomes:UP000076021};
RX PubMed=27231360;
RA da Mota F.F., Vollu R.E., Jurelevicius D., Seldin L.;
RT "Whole-Genome Sequence of Rummeliibacillus stabekisii Strain PP9 Isolated
RT from Antarctic Soil.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP9 {ECO:0000313|Proteomes:UP000076021};
RA Ploux O.;
RL Submitted (MAR-2016) 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};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000256|ARBA:ARBA00006773}.
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DR EMBL; CP014806; AMX00075.1; -; Genomic_DNA.
DR RefSeq; WP_066790082.1; NZ_CP014806.1.
DR AlphaFoldDB; A0A143HEB0; -.
DR STRING; 241244.ATY39_11960; -.
DR KEGG; rst:ATY39_11960; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000076021; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076021}.
FT DOMAIN 76..357
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 406..567
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 576 AA; 64929 MW; F38E8AC8A9AD72C4 CRC64;
MLEPNWKITE LRKQVAVIDG KTAPTIVITN ARYLHSMYKK WVEGNIWILG DRIVYAGPKM
PVNIEGTEIV DASGKTIVPG YIEPHVHPFQ LYNPQTLADY AAQLGTTTLI SDNLTFFLHT
TNEKAFSMLD QLKKLPFSFY WWARFDSQTE LQDEHKLFTP TVIHDWLERS DVLMGGELTG
WPKLVAGDDQ MLYSLQEAHM YGKKIEAHLP GSSSRTLARL KLFGADGDHE AMTVEEVENR
VLHGYGVTLR HSSIRPDLPD LLKGILEKDL NLFDHLMMTT DGATPSFYEK GIMDQCIQVA
LDAGVDPIDA YQMASYNIAR YYNMSDVHGF IATGRFATLN ILEDEYHPVP ESVLSKGVWL
KRDGEKVRTL EGVDFSALPP LNLSFDLTEE DCQFSMPFGI EMLNDVITKP YKVSVHPNQG
HLSEEHDECF LMLVDRKGQW RVNTLIKGFA NKLQGFASSY SSTGDIILIG KDIKEMLHAF
NVMKEMNGGI VLVENGEVIE TIPLPLCGGL SVEPVEHLIQ QQSALANALA ERGYAHGDAI
YTLLFLQSTH LPYVRITQQG IYEVMKKKVL FPSLMR
//
