ID   ADEC_THEAB              Reviewed;         574 AA.
AC   B7IEM2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=THA_28;
OS   Thermosipho africanus (strain TCF52B).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=484019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCF52B;
RX   PubMed=19124572; DOI=10.1128/jb.01448-08;
RA   Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA   Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT   "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT   the Firmicutes and Archaea.";
RL   J. Bacteriol. 191:1974-1978(2009).
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; CP001185; ACJ74536.1; -; Genomic_DNA.
DR   RefSeq; WP_004103343.1; NC_011653.1.
DR   AlphaFoldDB; B7IEM2; -.
DR   SMR; B7IEM2; -.
DR   STRING; 484019.THA_28; -.
DR   EnsemblBacteria; ACJ74536; ACJ74536; THA_28.
DR   KEGG; taf:THA_28; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_0; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000002453; 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..574
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146246"
SQ   SEQUENCE   574 AA;  63466 MW;  B9147A1E7B1C8F42 CRC64;
     MKIYEIVPVA LGKKMPDVLI KNVNLVNVFT GKIEKTNIAL YKKRIAGIGD DYKVGKEVID
     AKGLFAIPGL IDAHVHIESS MLSPTEFAKL ILPFGTTTII ADPHEIANVL GVEGIEYMIK
     STEGIPLNVY FAIPSAVPAT NLETSGATLG AEDMVSLVEK YPFRIIALGE VMNYPGVLDC
     DRDLITKIEI LRHKYKKIDG HAPGLTGKEL NAYIDAFVRS DHECETKEEA LEKLSKGMQI
     FIREGTAARN LNALLPAVNE MNHFFFSFCT DDRDPNDIIE RGHINGIIKS AIDSGIDPII
     AIRMATINTA KYFNLRSMGA ISPGYKADIV FIDNLKDFNI KFVIKDSKIV VEDKRINMNV
     ESIIRNIPNT LGKINIVKNY SLSIKNRNRK IRVISVKSGT LLTDELIVEP NVEKGYVVSD
     IDRDIIKIAV FDRHKASGYS IGFVHGLSIK NGAVATTIGH DSHNLTVVGT NDEDMNYAIS
     RIKELNGGIV VVKNKKLIAS LSLPIAGLMS DKNYGFVVEE LRKLKNSLVE IGVNSDILMQ
     IHFLQLAVIP KLKITDKGLI DVEKQKIVDL FVEV