ID A0A0A6VA07_9BACI Unreviewed; 572 AA.
AC A0A0A6VA07;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=NG54_16115 {ECO:0000313|EMBL:KHD84348.1};
OS Heyndrickxia ginsengihumi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=363870 {ECO:0000313|EMBL:KHD84348.1, ECO:0000313|Proteomes:UP000030588};
RN [1] {ECO:0000313|EMBL:KHD84348.1, ECO:0000313|Proteomes:UP000030588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2.11 {ECO:0000313|EMBL:KHD84348.1,
RC ECO:0000313|Proteomes:UP000030588};
RA Toymentseva A., Boulygina E.A., Kazakov S.V., Kayumov I., Suleimanova A.D.,
RA Mardanova A.M., Maria S.N., Sergey M.Y., Sharipova M.R.;
RT "Draft genome of phytase producing Bacillus ginsengihumi strain M2.11.";
RL Submitted (OCT-2014) 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:KHD84348.1}.
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DR EMBL; JRUN01000067; KHD84348.1; -; Genomic_DNA.
DR RefSeq; WP_035355919.1; NZ_JRUN01000067.1.
DR AlphaFoldDB; A0A0A6VA07; -.
DR STRING; 363870.NG54_16115; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000030588; Unassembled WGS sequence.
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 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 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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000030588}.
FT DOMAIN 66..347
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 400..568
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 572 AA; 62525 MW; 86E156FF301B494D CRC64;
MNKESLKRRI QVANKEILAD LVIKNGNILD IFNLELMSGD IAIVDGVIAG IGTYEGKQEV
DVQQRIIVPG LIDAHVHIES SMITPEEFAK VLLPHGVTTV ITDPHEIANV AGEDGISFMI
ADSEDLDLNV YIMLPSSVPA TPFENAGAVL HDQQLAPFYQ HSRVLGLAEV MDYPGVKNLD
DHIIDKLVTA SRFNIDGHGA GLDTHGVNVY ATAGIKTDHE CITIAEAKER LSRGMYLMIR
QGSVAKNLPE LIHIVNEKNS HRCLFCTDDK HLDDLIAEGS IDFNIRLAIQ HGLDPLLAIQ
LATINTANCF GLSQKGAIAP GYDADFLIID DLQSFQIQQV YTAGRLVAEQ GVYLEKTRVI
KDRTPLPHSV RIRDISAEDL AIAIPPEKKV HVIEIIPNQI ETIKQVIEVP NDGQYFISSV
TEDLLKVAVL ERHNGTGNIG LGIVKGLGLI DGAIATTVAH DSHNLIVAGT NDEDMLVAIQ
TIKQLGGGLV VVRHGVVLAS LQLAIGGLMS NKDYQEVAHE LNILHEALQQ VSKYDHFNLF
LTLSFLSLPV IPELKITDMG LFDVATFKHI RI
//
