ID   Y3012_BACCR             Reviewed;         589 AA.
AC   Q81BX6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Putative adenine deaminase BC_3012;
DE            Short=Adenase;
DE            Short=Adenine aminase;
DE            EC=3.5.4.2;
GN   OrderedLocusNames=BC_3012;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenine deaminase family. {ECO:0000305}.
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DR   EMBL; AE016877; AAP09959.1; -; Genomic_DNA.
DR   RefSeq; NP_832758.1; NC_004722.1.
DR   AlphaFoldDB; Q81BX6; -.
DR   SMR; Q81BX6; -.
DR   STRING; 226900.BC_3012; -.
DR   PRIDE; Q81BX6; -.
DR   EnsemblBacteria; AAP09959; AAP09959; BC_3012.
DR   KEGG; bce:BC3012; -.
DR   PATRIC; fig|226900.8.peg.3088; -.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; IEGHFPG; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IBA:GO_Central.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR   CDD; cd01295; AdeC; 1.
DR   Gene3D; 2.30.40.10; -; 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   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; Reference proteome.
FT   CHAIN           1..589
FT                   /note="Putative adenine deaminase BC_3012"
FT                   /id="PRO_0000142445"
SQ   SEQUENCE   589 AA;  67373 MW;  D185BC6BDB0A7323 CRC64;
     MELNTMGKNH YKWSNKQLRE HVEVLDGKRS THILLKNATY LNSYMREWMT ANIWIYNDRI
     VYVGEQLPEQ LTECEVVDCE GKYVVPGYIE PHAHPYQLYN PETLANHAMQ FGTTTFINDN
     LTLFFTLKRE EAFRLLDEFN KIPASMYWWC RFDGQTELQN GESLFNSEEI IEWLQHEAVL
     QGGELTAWPK LLHGDDEMLT WVQETKRLQK KVEGHFPGAS ETTLAKLKLL GTDCDHEAMT
     GQEAFTRLMQ GYTVSLRNSS IRPDLEVILK ELLELGVKQF DRFFFTTDGS HPSFYENGMT
     NVMISTAIKQ GVPVIDAYDM ASYNIARYYN MEHVHGSIAT GRIANINILE SKENPVPISV
     LAKGKWVKRD GVNTHEALHI DWSKHKVTPL SLDWSIEKED MIFSNKTGIH LLNNVITKPY
     TSEINIDCDE LSTDHDECFF MMIARDGSWQ VNIAVKGFAK ELGGLASSYS GTGDIILIGK
     RKEDMLTAFR RVKELGGGMV IAEKNEVLHE IALPLLGIMS NLKMRELIQE EKQMVKLLQE
     RGYAHDDPAF TILFFSATHL PFIRVTPIGL YDVKSSKVVA PPVNLIKQY