ID   ADEC_LEUCK              Reviewed;         551 AA.
AC   B1MY57;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=LCK_00627;
OS   Leuconostoc citreum (strain KM20).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=349519;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM20;
RX   PubMed=18281406; DOI=10.1128/jb.01862-07;
RA   Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA   Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT   "Complete genome sequence of Leuconostoc citreum KM20.";
RL   J. Bacteriol. 190:3093-3094(2008).
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; DQ489736; ACA82459.1; -; Genomic_DNA.
DR   RefSeq; WP_004907287.1; NC_010471.1.
DR   AlphaFoldDB; B1MY57; -.
DR   SMR; B1MY57; -.
DR   STRING; 349519.LCK_00627; -.
DR   EnsemblBacteria; ACA82459; ACA82459; LCK_00627.
DR   KEGG; lci:LCK_00627; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000002166; 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..551
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146242"
SQ   SEQUENCE   551 AA;  60470 MW;  C5C3875F8E3158FD CRC64;
     MAKTVSWHII NAKILDVFNL TFETSELWID HDKIVYRGRR SDLQAQHTFD AQGQYIVPGL
     IDAHMHIESS LLAPSEFSKL VVPHGITRVI ADPHEIASVA GVSGIQYMLE EARQSQLHIH
     YMLPSSVPAT PFEHAGATLH ADALKPFYSV PEVNGLAEVM DFPAVFNEDE DMHQKISDSQ
     AAGKHVDGHA SGLSREQLAI YRKYGIDTDH ESENAQQARD RLNAGFSVFV REGTVERDES
     AILPAISVAN QAHFSFATDD KTANDIQHEG AIDFNVKLAI QSGMSPAMAF TIASYNAATA
     HRLDNVGALT DGYVADLVII DSLDDFNIKK VMISGQWYVE PETTVLPLAN QSLNFTLTVD
     DLKLPINDKK PAHVIEIMPH HITTTHLVED VPSQEGLFVA DKTYTKIVVA ERYHNLGHGV
     GIIKGFQMTD GAIASTIAHD SHNIIIAGTN DEDMLLAANK LREIGGGEVV VNNGQITTLP
     LAIGGLMSEQ SYTTVIQENN TLQAAFSKIS HLNFDPFLTL SFMALPVIPS LKITDQGLFD
     FNTFSFINIQ D