ID   ADEC_CLOBB              Reviewed;         581 AA.
AC   B2TJH6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=CLL_A1394;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
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 sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-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; CP001056; ACD22942.1; -; Genomic_DNA.
DR   RefSeq; WP_012423779.1; NC_018648.1.
DR   AlphaFoldDB; B2TJH6; -.
DR   SMR; B2TJH6; -.
DR   EnsemblBacteria; ACD22942; ACD22942; CLL_A1394.
DR   KEGG; cbk:CLL_A1394; -.
DR   PATRIC; fig|935198.13.peg.1341; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000001195; 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.
FT   CHAIN           1..581
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146229"
SQ   SEQUENCE   581 AA;  63487 MW;  A5576C71197C22C3 CRC64;
     MKIDMNLLKR RIKVANKEVK ADTVVKNGKI LNVFTGDIMR GDIAIVDGFI AGIGQYEGEQ
     IIYAQNKVIV PGFIDGHMHI ESTMLTPNEL SKVLIQHGVT TVMADPHEIG NVAGIDGINF
     MLNASEELPI DVFIMLPSCV PATSFENSGA KLDAEDLQPF YTHPRVLGLA EFMDFSSIVN
     LNEKMLQKII NANLNGSIVD GHAPGLSKEE LNVYISTGIY ADHECANVRE AKERLELGMY
     LMIREGTAAK ELKKLIKVVT PTNSRRCMLV TDDKLPDDLI VEGSVDHNVR LAIKEGLDPV
     TAIQMVTINA AEFFGLRSFG AIAPGYQADL LILDELQNVS IDKVLKKGIC VVDNGEIKKE
     EFKINDNSKE LAMKLPKINM KELEKNAFKI PLSSDLCNVI EIVPNSLITY HRVEKVDIDK
     GNFSVSIAND QLKMAVIERH HATGNIGLGI VKGFGIKNGA IATTVAHDSH NIVVVGTSDE
     EMFLAVNHLK KMNGGIAIAS GKEIIASLPL AIGGLISENG YLEVQQQLKI LNQALSIIGV
     NADFNPFLTL SFLTLPVIPE IKLTDTGLFE FKTFSHIGVQ A