ID   ADEC_CLOPE              Reviewed;         572 AA.
AC   Q8XKX4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 94.
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}; Synonyms=adeC;
GN   OrderedLocusNames=CPE1268;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB80974.1; -; Genomic_DNA.
DR   RefSeq; WP_011010354.1; NC_003366.1.
DR   AlphaFoldDB; Q8XKX4; -.
DR   SMR; Q8XKX4; -.
DR   STRING; 195102.gene:10490531; -.
DR   EnsemblBacteria; BAB80974; BAB80974; BAB80974.
DR   KEGG; cpe:CPE1268; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; MVTACAY; -.
DR   Proteomes; UP000000818; 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.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..572
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142413"
SQ   SEQUENCE   572 AA;  64763 MW;  6722C973DC5F4823 CRC64;
     MQVELIIKNL KVYNSYFKKF IKSDVLINEG KFLHIGKGYE DRLWSENIID GEDKYIIPGL
     IDIHMHIESS MTIPREFSKA AIKHGVTTVV ADPHEIANVF GVRGIEEFIK FKGNLDIFYG
     IPSSVPSTSS SLETTGEKIT HNEVKRLLEY DNIICLGEVM NFKDLIEDDD SNINKIINIS
     KEKNIPLEGH CPKIQGVDLS LYIYRGVNGD HTQQSVGSLQ EKIQNGMFIE MQHKSMTLEN
     IKFLIENNLY EHFALVTDDV MADKLVKGHL DEILKEAVKL GMSIENAIYA STYTPARRMN
     LLDRGTIAPG KLADFILLDS IEDFNIYEVY KNGEMVFNRD KGLKEEFFED KSKLDYRFYN
     SIELNNITKE SLEVKVPNKY KNKVNCRTMK VLKNTTFTEE GEVTLNVYNN ILQWEKSSCA
     LIAVFERYGK NNNISFGLVE GEIIKEGAIA TTWAHDHHNL MVMGRNISDM TIAANEVINS
     RGGYVVSKNN EVIAKLELPI GGIISDEPIE IIGEKLGEVR NAMRDLGYNH MNEIMSFSTL
     SLPVSPALKI TDKGLIDVKK GSIVSLFKKG LY