ID   W8F364_9BACT            Unreviewed;       551 AA.
AC   W8F364;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
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=Hsw_0650 {ECO:0000313|EMBL:AHJ96245.1};
OS   Hymenobacter swuensis DY53.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ96245.1, ECO:0000313|Proteomes:UP000019423};
RN   [1] {ECO:0000313|EMBL:AHJ96245.1, ECO:0000313|Proteomes:UP000019423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY53 {ECO:0000313|EMBL:AHJ96245.1,
RC   ECO:0000313|Proteomes:UP000019423};
RA   Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT   "Complete genome sequence of ionizing-radiation resistance bacterium
RT   Hymenobacter swuensis DY53.";
RL   Submitted (JAN-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}.
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DR   EMBL; CP007145; AHJ96245.1; -; Genomic_DNA.
DR   RefSeq; WP_044001014.1; NZ_CP007145.1.
DR   AlphaFoldDB; W8F364; -.
DR   STRING; 1227739.Hsw_0650; -.
DR   KEGG; hsw:Hsw_0650; -.
DR   PATRIC; fig|1227739.3.peg.907; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_10; -.
DR   OrthoDB; 9775607at2; -.
DR   Proteomes; UP000019423; Chromosome.
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   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|HAMAP-Rule:MF_01518, ECO:0000313|EMBL:AHJ96245.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019423}.
FT   DOMAIN          48..329
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          378..544
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   551 AA;  58999 MW;  1E1E22E023C4ECEC CRC64;
     MPADFSLQAN VINLFQNTIT PATLHIAAGR IQRIEPTGAS APDPTLPYAL PGFVDAHVHV
     ESSLLVPSEF ARLAVVHGTV ATVSDPHEIG NVLGVAGVKY MLQNGAQVPF KFCFGAPSCV
     PATPFETAGA EITAQDIEHL FQEHPEIGYL AEMMNWPGVL NRDEQVMEKI RLAQQHGRPV
     DGHAPGLRGE DAARYASAGI STDHECFTAE EALDKLAVGM KVLIREGSAA RNFEALIDLL
     PEHYENLMFC SDDKHPDTLL LGHINQLVQR AVARGQEVLK VLRVACRNPV EHYNLPVGLL
     REDDPADFIV VDNLTDFPVR QTYLNGELVA ENGRTLIPAV PVAVVNNFDT NPTAPTDFAL
     PAPQAAATVR VIECFDGQLI TARHDLPARV ENGLVLPDIA QDVLKLTVVN RYHAAPPAVA
     FIQGFGLQGG ALASSVGHDS HNITAVGCDD ASLARAVNLV IAARGGLAVV TADGRELVLP
     LPVAGLMSDQ EGYHVAEAYA AVDALAKELG SPLQAPFMTL SFMALLVIPS LKLSDKGLFD
     GEAFRFVENV V
//