ID   ADEC_LIGS1              Reviewed;         578 AA.
AC   Q1WTM3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=LSL_0929;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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; CP000233; ABD99739.1; -; Genomic_DNA.
DR   RefSeq; WP_011476052.1; NC_007929.1.
DR   RefSeq; YP_535822.1; NC_007929.1.
DR   AlphaFoldDB; Q1WTM3; -.
DR   SMR; Q1WTM3; -.
DR   STRING; 362948.LSL_0929; -.
DR   EnsemblBacteria; ABD99739; ABD99739; LSL_0929.
DR   KEGG; lsl:LSL_0929; -.
DR   PATRIC; fig|362948.14.peg.1004; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000006559; 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; Reference proteome.
FT   CHAIN           1..578
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292386"
SQ   SEQUENCE   578 AA;  62987 MW;  68DDF35C205490A3 CRC64;
     MEKQKLIKLI DVAAGRKKAD LVLKNAKIVD VFQAKILTGD IAISDGYIAG IGGSYQGVVE
     CNYTGKYVAP GFIEAHIHIE SSYVSPEEFS RVFIPRGTTT ILADPHEIVN VAGLKGLDYM
     VNAAKNAKMD IRYMMPPCVP ATNFETSGAD LYADDMEDAL KTGEVDGLAE LMNFPGVINA
     DDKMIDEILM AKKYGARIDG HAPQVVGKDL NAYIAAGPAN DHECSTLEEA EERLARGMYL
     LLREGSVTQD LRKLLPIVNT ANSRRCLLSG DDVQAKTAIN KGHLDNSIRI CIDEGLNPIT
     AIQMATLNPA EYCGLNDRGA IAPGRRADMV VFESLEDFAV EETYILGEKL SQGNEYLGEV
     NYYPIDSVES SMHVKDFTRE KLQLHLNSDK VRAIGVVPGE VLTTEEHVTV KRDGDGNFVY
     NDQEDVTKIV VVERHHNTGN VNVNLLSGYG IKAGAIAISI GHDSHNIIAT GTNDDDIFMA
     VNELIKQEGG AVVVKDEKVI SRMELKIAGL MCNLPAEKMI AQQDALDEAV HEELGVPDNV
     NPVMTLSFMP LAVIPKLKIT DKGLVDVEKN AFVSNELD