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ADEC_LACDA
ID   ADEC_LACDA              Reviewed;         565 AA.
AC   Q1G825;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Ldb2182;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC   11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(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; CR954253; CAI98906.1; -; Genomic_DNA.
DR   RefSeq; WP_003621704.1; NC_008054.1.
DR   AlphaFoldDB; Q1G825; -.
DR   SMR; Q1G825; -.
DR   STRING; 390333.Ldb2182; -.
DR   EnsemblBacteria; CAI98906; CAI98906; Ldb2182.
DR   KEGG; ldb:Ldb2182; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; MVTACAY; -.
DR   BioCyc; LDEL390333:LDB_RS09505-MON; -.
DR   Proteomes; UP000001259; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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..565
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292383"
SQ   SEQUENCE   565 AA;  62389 MW;  7E773BB46EC4B865 CRC64;
     MTKIDLLVKN AHVFNVYLRK FEDVNITIKD GKFYWINKEL PGIEAAKVID LQGKYVIPGF
     VDAHMHIDSS MTTPKVMGQT IGKYGTTTII ADDHEITNVA GVKGLKDFID EKAPIDIFFG
     IPSSVPSTNP NMETTGGLIG VKETEELLKD PRFVCLGEVM NFKDMTSDHD TLIKKIIAAC
     RKARPTMPLE GHVPAYHSED LAKVIYAGIT TDHTQQTSSL VDEKIRSGMF VEIQLKSMHQ
     EVIDTVIEHG YFEHVALVTD DSMPDTLLKG HLNLLVKKAI DMGMRPEDAI YISTYTPARH
     MGLWDRGAIA PGRVADFIVL NNLEDLSIAQ VYKNGLPFAA KDEKDNNVYP EELLHSVKAP
     KLSEADFDLK TDLVQNGKVV ANIIQINEVG TFTNHIQKCL EVKDGHVQWK KAGLALMLCQ
     ERYGKNEGRY AFALIDRGIV GDGAIGATWA HDHHNLIILG TNIAGMVSVQ NLLVEEQGGY
     IAAKGSQIVA NAPLPLGGVV SLEPMSVLGK QISKVRETMV DLGYKNTNEI MSFSTLSLLV
     SPTLKISDKG IFEVKTQRHI PLFEC
 
 
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