ID   ADEC_BRUME              Reviewed;         581 AA.
AC   Q8YCA5;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=BMEII0627;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL53869.1; -; Genomic_DNA.
DR   PIR; AB3588; AB3588.
DR   AlphaFoldDB; Q8YCA5; -.
DR   SMR; Q8YCA5; -.
DR   STRING; 224914.BMEII0627; -.
DR   EnsemblBacteria; AAL53869; AAL53869; BMEII0627.
DR   KEGG; bme:BMEII0627; -.
DR   eggNOG; COG1001; Bacteria.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000000419; 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_0000142410"
SQ   SEQUENCE   581 AA;  62652 MW;  8FED6EE07A22248B CRC64;
     MRHCDSFCEL IPMKGCEAIL 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 IPLPIAGLMS TEPYETVREA LRKLRHAAED
     LGSVLEEPFL QLAFIALPVI PHLKITDRGL VDVDKFEFVG N