ID   ADEC_MOOTA              Reviewed;         596 AA.
AC   Q2RL95;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Moth_0463;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC18794.1; -; Genomic_DNA.
DR   RefSeq; WP_011392001.1; NC_007644.1.
DR   RefSeq; YP_429337.1; NC_007644.1.
DR   AlphaFoldDB; Q2RL95; -.
DR   SMR; Q2RL95; -.
DR   STRING; 264732.Moth_0463; -.
DR   EnsemblBacteria; ABC18794; ABC18794; Moth_0463.
DR   GeneID; 61289114; -.
DR   KEGG; mta:Moth_0463; -.
DR   PATRIC; fig|264732.11.peg.498; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
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.
FT   CHAIN           1..596
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292388"
SQ   SEQUENCE   596 AA;  63030 MW;  BF57381721AAD503 CRC64;
     MLPTRRPLAE VTRELVAVAT GKLPADTVIK GGKVVNVFTG EILPWDIAIK NGRIASVGDV
     SAAVGPETEV IDASGYYLCP GFMDGHVHVE SSMVTVTQFA RAVLPGGTTA IFMDPHEIAN
     VLGMDGVKLM VDEGRELPLK VFATMPSCVP AAPGFEDAGA SFGPEEVAAA MQWPGICGLG
     EMMNFPGVLA GDPAVHGELR ATLAAGKPIT GHFAMPADFQ GLAGYTAAGI SSCHESTRTE
     DALNRLRLGM YAMMREGSAW HDIKATIKSL TETRVDSRRA MLVSDDTHPE TLLSTGHLNH
     VVRRAIEEGL NPIRAIQAVT INTAECFGVA QDLGAIAPGR YADILFLKDL ARVAIDKVMV
     DGRVVAAGGR LLVDLPAVAY PDRVRHSVHL KEPLTPWHFR INAPAGKSRV QVRVMEIIEA
     NVNTRHLTVT VPVVDGQVTA GVEADLAKVA VVERHGGNGS IGLGFVRGFG FKAGAVASTV
     AHDSHNLLIV GMNDADMALA GNTLAGCGGG MVAVRDGQVL ALLPLPIAGL MSDRPVEEVA
     ARLAAVHRAW QELGCRLVSP FMTMALLSLP VLPELRLTNR GLVDTLQFKM VDLITG