ID   ADEC_CLOBM              Reviewed;         599 AA.
AC   B1KTS4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=CLK_3488;
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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; CP000962; ACA55991.1; -; Genomic_DNA.
DR   RefSeq; WP_012343902.1; NC_010520.1.
DR   AlphaFoldDB; B1KTS4; -.
DR   SMR; B1KTS4; -.
DR   EnsemblBacteria; ACA55991; ACA55991; CLK_3488.
DR   KEGG; cbl:CLK_3488; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000000722; 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..599
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146230"
SQ   SEQUENCE   599 AA;  65289 MW;  790B9FCAB156FC3D CRC64;
     MFNKFNTKPL WEVSKTLSSV AQGFEPADMV IINSRLINVC TREVIENTDV AISCGRIALV
     GDAKHCIGES TEVIDAKGQY IAPGFLDGHI HVESSMLSVS EYARSVVPHG TVGIYMDPHE
     ICNVLGLNGV RYMIEDGKGT PLKNMVTTPS CVPAVPGFED TGAAVGPEDV RETMKWDEIV
     GLGEMMNFPG ILYSTDHAHG VVGETLKASK TVTGHYSLPE TGKGLNGYIA SGVRCCHEST
     RAEDALAKMR LGMYTMFREG SAWHDLKEVS KAITGNKVDS RFAVLISDDT HPHTLLKDGH
     LDHIIKRAIE EGIEPLTAIQ MVTINCAQCF QMDHELGSIT PGKCADIVLI EDLKDVKITK
     VIIDGNLVAK DGVLTTSIAK YDYPENAMHS MHIRDKITPA SFNIMAQNKE KVTARVIEII
     PERVGTYERH IELNVKDDKV QCDPSKDVLK AVVFERHHET GKAGYGFVKG FGIKRGAMAA
     TVAHDAHNLL VIGTNDEDMA LAANTLIECG GGMVAVQDGK VLGLVPLPIA GLMSNKPLEE
     MAEMVEKLDS AWKEIGCDIV SPFMTMALIP LACLPELRLT NRGLVDCNKF EFVSLFVEE