ID   ADEC_CLOBL              Reviewed;         599 AA.
AC   A7GA53;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 68.
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=CLI_0367;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABS40266.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000728; ABS40266.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041173189.1; NC_009699.1.
DR   AlphaFoldDB; A7GA53; -.
DR   SMR; A7GA53; -.
DR   EnsemblBacteria; ABS40266; ABS40266; CLI_0367.
DR   KEGG; cbf:CLI_0367; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   Proteomes; UP000002410; 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_0000318546"
SQ   SEQUENCE   599 AA;  65351 MW;  0F7CE4D58BF7065E CRC64;
     MFNKFNTKPL WEVSKTLSSV AQGFEPADMV IINSRLINVC TREVIENTDV AVSCGRIALV
     GDAKHCIGEN TEVIDAKGQY IAPGFLDGHI HVESSMLSVS EYARSVVPHG TVGIYMDPHE
     ICNVLGLNGV RYMIEDGKGT PLKNMVTTPS CVPAVPGFED TGAAVGPEDV RETMKWDEIV
     GLGEMMNFPG ILYSTDHAHG VVGETLKASK TVTGHYSLPE TGKGLNGYIA SGVRCCHEST
     RAEDALAKMR LGMYAMFREG SAWHDLKEVS KAITENKVDS RFAVLISDDT HPHTLLKDGH
     LDHIIKRAIE EGIEPLTAIQ MVTINCAQCF QMDHELGSIT PGKCADIVFI EDLKDVKITK
     VIIDGNLVAK GGLLTTSIAK YDYPEDAMNS MHIKNKITPD SFNIMAPNKE KITARVIEII
     PERVGTYERH IELKVKDDKV QCDPNKDVLK AVVFERHHET GKAGYGFVKG FGIKRGAMAA
     TVAHDAHNLL VIGTNDEDMA LAANTLIECG GGMVAVQDGK VLGLVPLPIA GLMSNKPLEE
     MAEMVEKLDS AWKEIGCDIV SPFMTMALIP LACLPELRLT NRGLVDCNKF EFVSLFVEE