ID   ADEC_BRUA4              Reviewed;         563 AA.
AC   A6X5D7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-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=Oant_3735;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC   15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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; CP000759; ABS16441.1; -; Genomic_DNA.
DR   RefSeq; WP_012093108.1; NC_009668.1.
DR   AlphaFoldDB; A6X5D7; -.
DR   SMR; A6X5D7; -.
DR   STRING; 439375.Oant_3735; -.
DR   EnsemblBacteria; ABS16441; ABS16441; Oant_3735.
DR   KEGG; oan:Oant_3735; -.
DR   PATRIC; fig|439375.7.peg.3899; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   PhylomeDB; A6X5D7; -.
DR   Proteomes; UP000002301; Chromosome 2.
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..563
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000318548"
SQ   SEQUENCE   563 AA;  60454 MW;  2E87B8F25D555D23 CRC64;
     MLERMIDQGA GREPADIVLK GGRFFDLVTG ELVESDIAIC GDRIVGTFGN YQGKHEIDIS
     GRIVVPGFID THLHIESSHV TPHEFDRCVL PQGVTTVICD PHEIANVLGA EGIKFFLDSA
     LETVMDIRVQ LSSCVPATHM ETSGAELLID DLLPFADHPK VIGLAEFMNF PGVLAKDPEC
     MAKLKAFQGR HIDGHAPLLR GLDLNGYISA GIRTEHEATS AEEALEKMRK GMHVLVREGS
     VSKDLKALMP IITERHAQFL ALCTDDRNPL DIADQGHLDY LIRTAIAGGV EPIAIYRAAS
     VSAARAFGLF DRGLVAPGQR ADLVVVDSLE GCHAEIVLSA GRVISEDLFA ARKTVAPVGR
     NSVKASKVSA SSFRSHSNSG KTRAIGIIPG KIITESLEFD LKVGPNGVEP DFEKDVVKIA
     VVERHGKNGN IATGFVHGFG LKSGAIASTV SHDSHNICVV GTSDEDIAAA ANRLGEIEGG
     FVVVRDGKVL AEMPLPIAGL MSAEPYETVR DQLRVLRHAA EELGSVLEEP FLQLAFIALP
     VIPHLKITDR GLVDVDKFAF VGN