ID   ADEC_METBU              Reviewed;         584 AA.
AC   Q12XX8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=Mbur_0733;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(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; CP000300; ABE51698.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12XX8; -.
DR   SMR; Q12XX8; -.
DR   EnsemblBacteria; ABE51698; ABE51698; Mbur_0733.
DR   KEGG; mbu:Mbur_0733; -.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000001979; 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..584
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292402"
SQ   SEQUENCE   584 AA;  63335 MW;  60E4D2BAA7CD3506 CRC64;
     MNFFMDIRDK VFAATGKVKA DTIFFGGLLI NVNTKEMLYR DIAVKEGYIV GIGDVSSLKG
     DETEMIDVTG KHLCPGLMDG HVHFESSMVT LSQFAVPALA HGTTSVVIDP HEIANVLGRG
     GIELVLDEAA TLPLNAFVAV SSCVPATSFE TAGASIDVDD IVSLIANENV VGLGEMMDYP
     GVVFCDETKL SMIRTALKER LVVDGHCPAL SREQLFGYMC AGISTDHESI EYEEALEKLR
     LGMKLMIREG SAAKALDKFL PRLIGDGVSL ENVFFVTDDK HPSDLLKGYM DVIVRRAIEL
     GLSPLDAISM CTINAAKHYR VDHIVGSLSM GRKADIIVLE DLEKFIIDSV YASGRPVESF
     VPSYEYPDTV FNTVKFDAVT ATDLQIMSDA DKDHRVRVIK VVPDLIVTEN ETFVLHSDRH
     GILMPDVEND VLSVAVIERH GKNGNIGTGF IKGMGLRNGA IGQSIGHDSH NVVVTGVDHS
     DMALCANTIR SMNGGICVVS NGKVVEQLEL PFAGLLSTLP AEEVEKKLTD LHKAVKEIGC
     ALPAPFITHS FIALPVIPSL RLTDMGLFDV DKFSLVSPID EVME