ID   ADEC_GLUOX              Reviewed;         565 AA.
AC   Q5FQ87;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=GOX1719;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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:0000255|HAMAP-Rule:MF_01518};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
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DR   EMBL; CP000009; AAW61459.1; -; Genomic_DNA.
DR   RefSeq; WP_011253241.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FQ87; -.
DR   SMR; Q5FQ87; -.
DR   STRING; 290633.GOX1719; -.
DR   EnsemblBacteria; AAW61459; AAW61459; GOX1719.
DR   KEGG; gox:GOX1719; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000006375; 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; 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   PANTHER; PTHR11113:SF2; PTHR11113:SF2; 1.
DR   Pfam; PF13382; Adenine_deam_C; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01178; ade; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..565
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142425"
SQ   SEQUENCE   565 AA;  60564 MW;  866624505C97EE24 CRC64;
     MQKTIMRRVA QGQGHEPVDL VIKNVRLFDL VTGDLIPTDI AICGDRIVGT YGEYEGVQAI
     DGAGRIAVPG FIDTHLHVES SLVTPFEFDR CVLPHGVTTA ICDPHEMANV LGRAAFDYFL
     AAAERTIMDL RVNLSSCVPA TSMETSGAVL NVDDLVAYRH HPKVIGLAEF MNIPGVLNGD
     PGCVDKLAAF ADGHIDGHAP LMCGKALNGY LAAGISTDHE ATAADEALEK VRKGMTVLIR
     EGSVCKDLEA LVPLLNVATS PFFAFCTDDR NPLEIAHEGH LDFLIRRAIE LGVEPLAAYR
     AASLSAATAF GLRDRGQIAP GKRADIVLLD DLERCQVSDV ISAGRLVNDA LFNSREIVSP
     VGLESVKLPR PVTAQDMAVE GSGRDRPVMG VIPGQIITEF LRLDLPEDHG HVLPDPEQDV
     AKVCVVARHG HNDNIGRGFV RGFGLKEGAL ASSVGHDSHN ICVVGTSDAD MACAVNHLEK
     TGGGFVAVRN GQVLADLCLP VAGLMSDAPY EQVRDDLIIL RKAAKTMGVV LEEPFLQLAF
     LPLPVIPHLK ITDFGMIDVR TMSFV