ID   ADEC_OCEIH              Reviewed;         582 AA.
AC   Q8CUS7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
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}; Synonyms=adeC;
GN   OrderedLocusNames=OB1030;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC12986.1; -; Genomic_DNA.
DR   RefSeq; WP_011065432.1; NC_004193.1.
DR   AlphaFoldDB; Q8CUS7; -.
DR   SMR; Q8CUS7; -.
DR   STRING; 221109.22776711; -.
DR   EnsemblBacteria; BAC12986; BAC12986; BAC12986.
DR   KEGG; oih:OB1030; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_9; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   PhylomeDB; Q8CUS7; -.
DR   Proteomes; UP000000822; 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..582
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142430"
SQ   SEQUENCE   582 AA;  63824 MW;  1D9A5B9F3445C273 CRC64;
     MNSTIEQLKH RIAVASKRKP AELVIKNAEV LNVFTGDWKK TDVAIADGYI AGLGNYEGLQ
     TVDATGKKIV PGLINGHIHI ESTMLTPREF SKVMLKHGVT TAITDPHEIA NVAGTDGLEY
     MLNASDALPM NIFVNMPSSV PATQFEHNGA QLDAKDISSY FQNPNVLGLA EVMDFPSVAN
     ADQKMLEKIV STIQHGGIID GHAAGLSKED LNIYMAAGIR NDHESVSAQE GKDRLEAGMY
     LMIREGTVAK DLEALLPIIN DKNARRCIFV TDDMLLDDLV ENGDIDHIIR KAIQLGLDPV
     MAYQMATLNT AECFGLRELG AVAPGYIADF LILNDENQVD IHQVYKNGKC VVDEGEINQS
     YFAASLTYDA TTLPKPRIQQ LKASDFSIDL TDDYCNIIEI VPNKIITNHV CERVEVKEGK
     FVPSVDKDQL LIAVVERHKG LGYIGKGIVK GFKMKEGAIA TSVAHDSHNF VVVGTSEEEM
     LSAIKKVEQL DGGLVVTKRK QVKAHLALPI GGLMSDKDYL DAYEEVLKLN HVAVENGIPS
     NFNPFLTLSF LTLPVIPTLK VTDQGLFDFK TFSHINVEVE EK