ID   ADEC_CERSK              Reviewed;         565 AA.
AC   B9KND1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=RSKD131_2377;
OS   Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=557760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD131 / KCTC 12085;
RX   PubMed=19028901; DOI=10.1128/jb.01565-08;
RA   Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT   "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL   J. Bacteriol. 191:1118-1119(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; CP001150; ACM02237.1; -; Genomic_DNA.
DR   RefSeq; WP_015921379.1; NC_011963.1.
DR   AlphaFoldDB; B9KND1; -.
DR   SMR; B9KND1; -.
DR   EnsemblBacteria; ACM02237; ACM02237; RSKD131_2377.
DR   GeneID; 67447757; -.
DR   KEGG; rsk:RSKD131_2377; -.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000001597; Chromosome 1.
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; 2.
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..565
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000185091"
SQ   SEQUENCE   565 AA;  60529 MW;  8F8CF5BDFD5DCF49 CRC64;
     MSRSLSECID QGRGLVPADL VLKHGRVFDL VTGELVQTDV AICGDRIVGT FGTYTGRREI
     DCRGRILVPG FIDTHLHVES SLVTPFEFDR CVTPRGITTA ICDPHEIANV CGLEGIRYFL
     EASAHLVMDL RVQLSSCVPS THMETAGAAL EAKDLAPLLD HPRVIGLAEF MNFPGVLMKD
     PGCMAKLEAF RGRHIDGHAP LLRGKDLNGY IAAGIRTEHE ATTADEALEK LRKGMRVLIR
     EGSVSKDLHA LVSILTERHA PYLCLCTDDR NPLDIAEHGH IDHMIRTAIR LGAPPLAVYR
     AASLSAAEAF GLKDRGLIAP GRRADIAVLD SLEGCHAALV LAGGVVADDA AFSARSGVEP
     VARASVKVAE IAPEAFRCPG NRAETPVIGI LPGKIITEHL TAEIEPVDGD KRPDPARDLA
     RIAVIERHGK TGGRATGFVQ GFGMARGAIA STVCHDHHNL AVVGIDYADM ALAANRLRAL
     EGGFAVAAGG EILAELALPV GGLMSLRPFE EVRDALVTLR EAARSLGVTL EEPFLQLAFL
     ALPVIPHLKI TDRGMVDVDR FEILP