ID   ADEC2_DESPS             Reviewed;         576 AA.
AC   Q6ANH1;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=DP1374;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG36103.1; -; Genomic_DNA.
DR   RefSeq; WP_011188615.1; NC_006138.1.
DR   AlphaFoldDB; Q6ANH1; -.
DR   SMR; Q6ANH1; -.
DR   STRING; 177439.DP1374; -.
DR   EnsemblBacteria; CAG36103; CAG36103; DP1374.
DR   KEGG; dps:DP1374; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_7; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000000602; Chromosome.
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..576
FT                   /note="Adenine deaminase 2"
FT                   /id="PRO_0000142418"
SQ   SEQUENCE   576 AA;  61944 MW;  83CA0C5ECAD344A7 CRC64;
     MNKEALKRLI AVAAGREEPD LVIKNAKVVD VFNARVIQGD IAIVDGLIAG VGDYSCKNEL
     DAEGQYAAPG FIDSHIHIES SYVSPEELGR LLVPHGTTTI IADPHEIANV CGLKGLDYMI
     EAAKRTALDV QMMLPSCVPA TPFEHSGANI DAREMEKPIT YDEVLGLGEF MDFPGVINGV
     DATIEKLLVA KRAGKPIDGH SPGVSGNALN AYASARIGTD HECATVEEMH ERIARGMYVL
     LRQGSACYNL RTLLKGVTPV NSRRCLFCAD DCQPKTILSL GHLDNHLRIC AEEGIDPIMA
     IQMATINAAE CFGLKDRGAI APGLKADIVL MDSLTNCRVE KVWIDGVLIA DSGKYLPEIK
     RHDISSTKGN FKVKDFSVKK LKLAIQSPQA HVINILPGGV VTSKEVVAIN RNSDNEFVYG
     HGQDVVKIAV VERHQNTGNV AVALLQGYGI KRGAIALSVA HDSHNIIVVG VDDTDMACAV
     EALIAQDGGI VLVNGEEVVE SMPMPIAGLM SDQCGEWVEA KLTSIHSKAH EVLGVNADVE
     PVMTLCFMSL AVIPEIKLTD MGLFDVTKFD FISLEA