ID   ADEC1_DESPS             Reviewed;         594 AA.
AC   Q6ANH2;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Adenine deaminase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase 1 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade1 {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=DP1373;
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; CAG36102.1; -; Genomic_DNA.
DR   RefSeq; WP_011188614.1; NC_006138.1.
DR   AlphaFoldDB; Q6ANH2; -.
DR   SMR; Q6ANH2; -.
DR   STRING; 177439.DP1373; -.
DR   EnsemblBacteria; CAG36102; CAG36102; DP1373.
DR   KEGG; dps:DP1373; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_7; -.
DR   OMA; GHIHVEC; -.
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   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..594
FT                   /note="Adenine deaminase 1"
FT                   /id="PRO_0000142417"
SQ   SEQUENCE   594 AA;  64784 MW;  28D5BE1046AF2FC6 CRC64;
     MQVSKDALKQ LIRAGRGVIP ASKVLEGGYL VNVMSNEVYL ADVAIYEERI VAIGKVEEYK
     GPETEVIDVT GLYLLPGLID GHLHSECSKL SITSFAKAVV PCGTTSIVSG LDEYISVSGL
     EGLQEVFKEV KKSPLKVFWG APYKTPYTFP KSTVAFNFTE EVHQEVQQWP ECFGVWETVR
     EAVQEEDEDT LGALATAQNN RLPIFGCAPM ARGKELNGYL CAGVRLDHES YDHEEVVEKM
     RNGMHMLIRE SSVTHFLEEN IRAVTEVNPY LARRVSFCTD DVTATDILEK GHMDNVVRQA
     IKAGVEPITA IQMATINSAE AYRIDHLVGS ITPGKIADIV MVDSLEGFQV QAVLTDGKLV
     ARDKKMSYEL KAPARSSVLS CALKCATTTP EDFQYRVEIE QGTAEVLSMN VKGPFVRKRR
     DVTLQVANHI VQADTENDVL MVSVLERFGR NGNKSLAFCS GWKLKKGAMA SSAAPDDNNI
     IVMGADASDM SIAVNHLIEN GGGQVIVADG EILEFLALPV GGIVSDLEAE EIARQESLLT
     KAANSLGCDL PDPLMYMFFL PITAIPDYAI TDVGPVDCIA LTTFDPILAL NPGK