ID   ADEC_BDEBA              Reviewed;         586 AA.
AC   Q6MJY0;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=Bd2636;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
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; BX842653; CAE80429.1; -; Genomic_DNA.
DR   RefSeq; WP_011165032.1; NC_005363.1.
DR   AlphaFoldDB; Q6MJY0; -.
DR   SMR; Q6MJY0; -.
DR   STRING; 264462.Bd2636; -.
DR   EnsemblBacteria; CAE80429; CAE80429; Bd2636.
DR   KEGG; bba:Bd2636; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_7; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000008080; 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..586
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142405"
SQ   SEQUENCE   586 AA;  63714 MW;  95757416BD3FDC62 CRC64;
     MSLSNKKTQK IASDLLPARL SQARGDGTLD LLITNVQMLD VITGDIYPTC IAIGGEHIVG
     VGMEYQTQSA RRTWNALGAF VTPGFIDGHL HIESSMMSPF EFEKATLPLG TTTAICDPHE
     ITNVLGGRGF SWFLRSSELM HQNLFVQMSS CVPALPGFET TGSDFPLEEM KSFKDHPSVL
     GLAEMMNFPG VIHADEEVLA KIEAFDDLNM DGHAPLLRGK ALNAYLLAGI QNCHETVTLE
     EGREKLQKGM GLIIREGSVA KNLRTLAPLV NEFSSPQCLL CTDDRNPFEI AHEGHINYLI
     KELINKHGVA VHVAYRLATY SAARHFGLKR LGLVAPGKKA DLVFLKDLKA VDIQEVMIGG
     KFVSELKLQD SLQEKLQTSQ PPLENTMKRS PLTEKELTVN LLPGVYNVIE IVPHEIITQH
     LTVAFDGQKF AESDVLYMAN IERYGKGLPP ALGLVKGMGL KSGALASSVA HDSHNIMVIG
     TNPADMVLAV NTLIKSGGGF AVADQGEIKA LVELPIAGLL SLKSAEEIKD GIADLKTAFR
     SLGVHLDEPF IQMAFLALPV IPTLKLTDRG LVNVTNFSFI PLQVEA