ID   ADEC_CLOBA              Reviewed;         581 AA.
AC   B2V525;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=CLH_1323;
OS   Clostridium botulinum (strain Alaska E43 / Type E3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=508767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alaska E43 / Type E3;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL   Submitted (MAY-2008) 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: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; CP001078; ACD51935.1; -; Genomic_DNA.
DR   RefSeq; WP_012450185.1; NC_010723.1.
DR   AlphaFoldDB; B2V525; -.
DR   SMR; B2V525; -.
DR   KEGG; cbt:CLH_1323; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
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.
FT   CHAIN           1..581
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146228"
SQ   SEQUENCE   581 AA;  63468 MW;  5FC1742AA228870D CRC64;
     MKIDMNLLKR RIKVANKEVK ADTVVKNGKI LNVFTGDITR GDIAIVDGFI AGIGKYDGEQ
     IIDAQDKVIV PGFIDGHMHI ESTMLTPNEL SKVLIQHGVT TVMADPHEIG NVAGIDGINF
     MLNASEKLPI DVFIMLPSCV PATSFENSGA KLDAEDLQPF YKHPRVLGLA EFMDFSSIVN
     LNEEMLQKII NAHLNGSIVD GHAPGLSKEE LNVYISTGIY ADHECANVKE AKERLELGMY
     LMIREGTAAK ELKKLIKVVT PTNSRRCMLV TDDKLPDDLI VEGSVDHNVR LAIKEGLDPV
     TAIQMVTINA AEFFGLRSFG AIAPGYQADL LILDELQTVS IDKVLKKGIC VVDNGEIKKE
     EFKINDNSKE LAMKLPKINM KALEKNAFEI PLSSDLCNVI EIVPNSLITH HRVEKVDIDK
     GNFSASISND QLKMAVIERH HATGNIGLGI VKGFGIKNGA IATTVAHDSH NIVVVGTSDE
     EMFLAVNHLK KMNGGIAIAS GKEIIASLPL AIGGLISENS YLEVQEQLKI LNQALSIIGV
     DADFNPFLTL SFLTLPVIPE IKLTDTGLFE FKRFSHIKVQ A