ID   ADEC_LISIN              Reviewed;         579 AA.
AC   Q92AR6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=lin1853;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL596170; CAC97084.1; -; Genomic_DNA.
DR   PIR; AD1664; AD1664.
DR   RefSeq; WP_010990990.1; NC_003212.1.
DR   AlphaFoldDB; Q92AR6; -.
DR   SMR; Q92AR6; -.
DR   STRING; 272626.lin1853; -.
DR   EnsemblBacteria; CAC97084; CAC97084; CAC97084.
DR   KEGG; lin:adeC; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000002513; 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_0000142427"
SQ   SEQUENCE   579 AA;  62537 MW;  40BF66746569E42F CRC64;
     MENLKQLQER VAVSDGRAKA DLVIKNGRIV NVFSGEIMEG DIAIKNGYIA GIGHFPDADQ
     IIDAAGEFIS PGFIDAHVHV ESAMVTPSEF ARVLLPNGVT TIITDPHEIA NVAGEKGIEF
     MLEDAKGAPL DMFVMLPSSV PATEGEHNGE TLHAKQLHPL YKHEKVIGLA EVMDFPSVAK
     GSADILTKII DAKQEGGRID GHGAGLTSAD LNNYLAVGIR TDHESTSAKE ALDRLRAGMF
     VMLREGTVGR DLKQTISAVT EKNSHRFCFC TDDKLINDLL TEGSINYNIR LAIENGVEPI
     TAIQMATINA ANCHNLPYLG AVAAGYQADI VFLKDLKTIE ISKVLKNGQV VVENGTRKEA
     AFKKENKAKF ISPKINHHLS IKDLELPLTN ETCYVIGMQQ NNLFTEKLME QVTIKNGKFV
     PSIEKDLLKM AVVERHHNTG CVGVGIVKGF GLTEGAIATT VAHDSHNIVA VGVSDEAMEK
     AIDHVTKTGG GIAVVDAAGN VLHDLALQVA GLLSDKPYEE VENDLAGLLK AFNQISKAKG
     FDPFLTLSFL TLPVIPELKL TDQGLFDFAT FQIIPNEVN