ID A0A1Q8Q322_9BACI Unreviewed; 575 AA.
AC A0A1Q8Q322;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=BTO30_13330 {ECO:0000313|EMBL:OLN21749.1};
OS Domibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714264 {ECO:0000313|EMBL:OLN21749.1, ECO:0000313|Proteomes:UP000185568};
RN [1] {ECO:0000313|EMBL:OLN21749.1, ECO:0000313|Proteomes:UP000185568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XD80 {ECO:0000313|EMBL:OLN21749.1,
RC ECO:0000313|Proteomes:UP000185568};
RA Verma A., Krishnamurthi S.;
RT "Domibacillus antri genome sequencing.";
RL Submitted (DEC-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, 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}.
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:OLN21749.1}.
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DR EMBL; MSDU01000033; OLN21749.1; -; Genomic_DNA.
DR RefSeq; WP_075399220.1; NZ_MSDU01000033.1.
DR AlphaFoldDB; A0A1Q8Q322; -.
DR STRING; 1714264.BTO30_13330; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000185568; Unassembled WGS sequence.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 InterPro; IPR011612; Urease_alpha_N_dom.
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 Pfam; PF00449; Urease_alpha; 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:0000256|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 13..55
FT /note="Urease alpha-subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00449"
FT DOMAIN 66..348
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 399..566
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 575 AA; 62458 MW; E2C847C92A9B09C0 CRC64;
MNQLLKTLIH TAQHPEEADL IIQNGMVVDV FSLQTFEADI AIKDGYIVGI GTYKEGKTII
NAEGKYVMPG FIDGHIHIES TMVTPAEFSR ALLQHGVTTV VTDPHEIANV AGKKGIEYML
EDAEHAEIDI LMKLPSCVPA TPFEQNGAVL TAADLRPYLT HKNVIGLAEV MDYPSVLKAD
DGMLEKITIT TDHGLTVDGH AAGLSEDALN AYSTASIRND HEAVSAFEAE ARVRRGIHVI
VREGSAAKDL LAILPAITER NSTRFSFCTD DKHLDELAAE GTVNYAAQLA IENGLNPLIA
IQMATLNNAV CHQLKDKGAV APGYAADLLI VENLNELRPS TIVKKGKVID FSALQIKKTP
VPVLLKESVK MKKVDKQSLQ IPIQNGQKAI IIEVLPGKLI TKKLIEDVQT NEGFFEADVK
RDQLKIAVCE RHHATGSVGV GIVKGLKLKS GAIASTVAHD SHNLVVAGTN DEDMMTAIET
IEQMQGGLVI VDNGKVLASV TLRVGGIMSE KPYEEVMEEL HHLHEQLSIV AEESQNIFMI
LSFLCLPVIP SLKLTDKGLF DVDSFQHIEV GIKNN
//
