ID   ADEC_LISW6              Reviewed;         579 AA.
AC   A0AJJ5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=lwe1759;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS   NCTC 11857 / SLCC 5334 / V8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX   PubMed=16936040; DOI=10.1128/jb.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA   Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA   Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA   Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK21177.1; -; Genomic_DNA.
DR   RefSeq; WP_011702538.1; NC_008555.1.
DR   AlphaFoldDB; A0AJJ5; -.
DR   SMR; A0AJJ5; -.
DR   STRING; 386043.lwe1759; -.
DR   PRIDE; A0AJJ5; -.
DR   EnsemblBacteria; CAK21177; CAK21177; lwe1759.
DR   GeneID; 61189658; -.
DR   KEGG; lwe:lwe1759; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000000779; 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..579
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000296727"
SQ   SEQUENCE   579 AA;  62785 MW;  071563F45D1F8B62 CRC64;
     MENLKQLQER VAVSDGREKA DLVIKNGRIV NVFSGEIMEG DIAIKNGYIA GIGDFSEAEQ
     IMDAAGEFIV PGFIDAHVHV ESAMVTPAEF ARVLLPNGVT TIVTDPHEIA NVAGEKGIEF
     MLEDAKGAPL DMFVMLPSSV PATEGEHNGE TLHAKKLHPL YKHEKVIGLA EVMDFPSVAK
     GSSDILTKII DAKKEGGRID GHGAGLTSAD LNNYLAVGIR TDHESTNAKE AVDRLRAGMF
     VMLREGTVGR DLLQTISAVS EKNSHRFCFC TDDKLINDLI TEGSINYNIR LAIENNIDPI
     TAIQMATINA ANCHNLPYLG AVAAGYQADI VFLKDLQTIE ISKVLKNGQV VVENGARNEA
     AFEKKHSETF ISPKIQHHLS KQDLELPLTN DTCYVIGMKQ NNLFTEKLME QVNVENGKFV
     PSIEKDLLKM AVVERHHNTG CVGVGIVKGF GLKEGAIATT VAHDSHNIVA VGASDEAMEK
     AINYVTEMGG GIAVVDETGK VLHDLALPVA GLLSNKPYEE VERDLAGLLK AFNQISNAKG
     FDPFLTLSFL TLPVIPELKL TDQGLFDFAT FQIIPNEVN