ID   ADEC2_ALKCK             Reviewed;         573 AA.
AC   Q5WD17;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Adenine deaminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade2 {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=ABC3209;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD65743.1; -; Genomic_DNA.
DR   RefSeq; WP_011248051.1; NC_006582.1.
DR   AlphaFoldDB; Q5WD17; -.
DR   SMR; Q5WD17; -.
DR   STRING; 66692.ABC3209; -.
DR   EnsemblBacteria; BAD65743; BAD65743; ABC3209.
DR   KEGG; bcl:ABC3209; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; MVTACAY; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..573
FT                   /note="Adenine deaminase 2"
FT                   /id="PRO_0000142403"
SQ   SEQUENCE   573 AA;  62460 MW;  04194FCCD724E3F6 CRC64;
     MHVDTLVKNV RVYNAYTQQF IASDVAIDEG RFVAIGHSDE LESIQANTII DGQGQQMIPG
     LIDIHLHIES SMVTPETFSW ALLRNGVTTI VAEPHEMANV FGIEGIKAMI EASAACTVDM
     KYAIPSSVPA TSLETTGGAI GIAEMDELMD TEDIQCLGEI MNYVDVLSKP DSKTNQILKH
     FRRSYPALPI EGHVPKLTGL DLHQIVAAGI GSDHTHQTRE GMEARIKAGM FLEIQEKSMT
     DDVLSYLIEN DTREHFCFVT DDVMADSLYK RGHLNVLANK ALAAGMKFED VIYACTMAPA
     KRMKLEDRGA IAPGKIADFI LLAEDGQFVF SAVYKDGMLA FDAASPYKQT PKPRQFPPHF
     YESVKLAPLQ EEDFHVVADR QDGIHVCRVM NVADGSTFTK ETQERVPVAN GLLQWQDSDF
     RLIATFERYG KTGGRAHGLI AGDILQRGAV ATTYSHDNHN LLVVGANILD MVCAANAVIQ
     AQGGCAVVEN GEVKAMLELP VGGILSEAPL AELAPKVESF VKALTALGYK HYNPIMSLST
     LSLPVSPALK ITDFGLIDVN NGQVVPLFVN EKS