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Database: UniProt
Entry: A0A1Q8Q322_9BACI
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ID   A0A1Q8Q322_9BACI        Unreviewed;       575 AA.
AC   A0A1Q8Q322;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   08-MAY-2019, entry version 11.
DE   RecName: Full=Adenine deaminase {ECO:0000256|HAMAP-Rule:MF_01518, ECO:0000256|SAAS:SAAS00340006};
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|HAMAP-Rule:MF_01518, ECO:0000256|SAAS:SAAS00340006};
GN   Name=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN   ORFNames=BTO30_13330 {ECO:0000313|EMBL:OLN21749.1};
OS   Domibacillus antri.
OC   Bacteria; Firmicutes; 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;
CC         EC=3.5.4.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01518,
CC         ECO:0000256|SAAS:SAAS01117456};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01518};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Adenine deaminase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01518, ECO:0000256|SAAS:SAAS00847022}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {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   BioCyc; GCF_001936625:BTO30_RS13350-MONOMER; -.
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; 2.30.40.10; -; 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   PANTHER; PTHR11113:SF2; PTHR11113:SF2; 1.
DR   Pfam; PF13382; Adenine_deam_C; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01178; ade; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000185568};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01518,
KW   ECO:0000256|SAAS:SAAS00321417};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01518};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00321440}.
FT   DOMAIN       12     57       Urease_alpha. {ECO:0000259|Pfam:PF00449}.
FT   DOMAIN       66    348       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   DOMAIN      399    566       Adenine_deam_C. {ECO:0000259|Pfam:
FT                                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
//
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