ID   ADEC_CLOB1              Reviewed;         599 AA.
AC   A7FQU9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=CLB_0338;
OS   Clostridium botulinum (strain ATCC 19397 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19397 / Type A;
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; CP000726; ABS34386.1; -; Genomic_DNA.
DR   RefSeq; WP_011986063.1; NC_009697.1.
DR   AlphaFoldDB; A7FQU9; -.
DR   SMR; A7FQU9; -.
DR   KEGG; cba:CLB_0338; -.
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..599
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000318545"
SQ   SEQUENCE   599 AA;  65250 MW;  BEE19A9E04B155EA CRC64;
     MFNKFDTKPL WEVSKTLSSV AQGLEPADMV IINSRLINVC TREVIENTDV AISCGRIALV
     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 VELNVKDDKV QCDPSKDVLK AVVFERHHET GTAGYGFVKG FGIKRGAMAA
     TVAHDAHNLL VIGTNDEDMA LAANTLIECG GGMVAVQDGK VLGLVPLPIA GLMSNKPLEE
     MAEMVEKLDS AWKEIGCDIV SPFMTMALIP LACLPELRLT NRGLVDCNKF EFVSLFVEE