ID   ADEC_GEOKA              Reviewed;         577 AA.
AC   Q5KY53;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=GK2098;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD76383.1; -; Genomic_DNA.
DR   RefSeq; WP_011231583.1; NC_006510.1.
DR   AlphaFoldDB; Q5KY53; -.
DR   SMR; Q5KY53; -.
DR   STRING; 235909.GK2098; -.
DR   EnsemblBacteria; BAD76383; BAD76383; GK2098.
DR   KEGG; gka:GK2098; -.
DR   PATRIC; fig|235909.7.peg.2251; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000001172; 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..577
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142424"
SQ   SEQUENCE   577 AA;  62927 MW;  43ED8125C26386FC CRC64;
     MHSTLHNQIA AAAKQTKADL VIQNGKIVNV FTREIIEGDL AIVEGMIVGI GRYEGEKTID
     AEGRYICPGL IDGHVHIESS MVPPSEFARV VLPHGVTTVI ADPHEIANVA GVCGIQFMLD
     EAKRTPLDVY MMLPSCVPAA SFERAGAVLS AAELAPFFND ERVLGLAEVM DYPSLREQHP
     SMLDKLALAA NANRLIDGHL AGLDADAVNV YRSARIHTDH ECVTPDEALE RVRRGMYVLI
     RQGSVAKDLK KLLPAIHEHN ARRFLFCTDD KHLDDLWFEG SVDHNVRLAI QAGLDPLLAI
     QMATLNAAEC YRLPTKGAVA PGYDADFLFV DDLETLNITH VFKAGRLVAQ HGQTVFPAER
     SAESLEQPLL HSIRCQAVDE TDLRIPMKRG TKAHVIEIIP NHLHTNHLIT DVDVQEGAFC
     PSIERDLLKL VVVERHRGLG IGLGIVRGFG FKAGAIASSI AHDSHHIIAA GTNDRDLTAA
     IEQLRQQHGG LAVIKDGAVL ASLPLEIGGL MTRKDYTEVL SGLKQIDKAL KAIGANGSFN
     PFITLSFLAL PVIPELKLTD QGLFDVNKWE FIPVEAV