ID   ADEC_BRUAB              Reviewed;         581 AA.
AC   Q578E4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=BruAb2_0573;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017224; AAX75990.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q578E4; -.
DR   SMR; Q578E4; -.
DR   EnsemblBacteria; AAX75990; AAX75990; BruAb2_0573.
DR   KEGG; bmb:BruAb2_0573; -.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000000540; Chromosome II.
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..581
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142409"
SQ   SEQUENCE   581 AA;  62688 MW;  8FE87E90AE559DF4 CRC64;
     MRHCDSFCEL IPMKGCEAML EWMIDQGAGR EPADIVLKGG RFLDLITGEL VESDIAICED
     RIVGTFGTYR GKHEIDVSGR IVVPGFIDTH LHIASSQVTP HEFDRCVLPQ GVTTAICDPH
     EIANVLGAEG IRFFLDSALE TVMDIRVQLS SCVPATHMET SGAELLIDDL LPFADHPKVI
     GLAEFMNFPG VLAKDPECMA KLRAFQGRHI DGHAPLLRGL DLNGYIAAGI RTEHEATNAE
     EALEKLRKGM YVLVREGSVS KDLKALMPII TERHAQFLAL CTDDRNPLDI ADQGHLDYLI
     RTAIAGGVEP LAIYRAASVS AARVFGLFDR GLVAPGQRAD LVVVDSLEGC HAEIVLSAGR
     VVSEALFAAR KPVAEVGRNS VKAPRVTASN FRSQSNSGKT RAIGIVPGKI ITQNLEFDLK
     VGPNGVEPDL ERDVVKVAVI ERHGKNGNIA TGFVHGFGLK AGAIASTVSH DSHNICVVGA
     SDEDIATAAN RLGEIEGGFV VVRDGKVLAE MPLPIAGLMS TEPYETVREA LRKLRHAAED
     LGSVLEEPFL QLAFIALPVI PHLKITDRGL VDVDKFEFVG N