ID   ADEC_CERS1              Reviewed;         565 AA.
AC   A3PN31;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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};
GN   OrderedLocusNames=Rsph17029_2645;
OS   Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17029 / ATH 2.4.9;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000577; ABN77747.1; -; Genomic_DNA.
DR   RefSeq; WP_011841799.1; NC_009049.1.
DR   AlphaFoldDB; A3PN31; -.
DR   SMR; A3PN31; -.
DR   EnsemblBacteria; ABN77747; ABN77747; Rsph17029_2645.
DR   GeneID; 57471317; -.
DR   KEGG; rsh:Rsph17029_2645; -.
DR   HOGENOM; CLU_027935_0_0_5; -.
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; 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_0000296730"
SQ   SEQUENCE   565 AA;  60603 MW;  65E24180EBDF886C CRC64;
     MSRSLSECID QGRGLVPADL VLKHGRVFDL VTGELVQTDV AICGDRIVGT FGTYAGRREI
     DCRGRILVPG FIDTHLHVES SLVTPFEFDR CVTPRGITTA ICDPHEIANV CGLEGIRYFL
     EASAHLVMDL RVQLSSCVPS THMETAGAAL EAKDLAPLMD HPRVIGLAEF MNFPGVLMKD
     PGCMAKLEAF RGRHIDGHAP LLRGKDLNGY IAAGIRTEHE ATTADEALEK LRKGMRVLIR
     EGSVSKDLHA LVSILTERHA PYLCLCTDDR NPLDIAEHGH IDHMIRTAIR LGAPPLAVYR
     AASLSAAEAF GLKDRGLIAP GRRADIAVLD SLEGCHAALV LAGGVVADDA AFSARSDVEP
     VARASVKVAE IAPEAFRCPG NRAETPVIGI LPGKIITEHL TAEIEPVDGD KRPDPARDLA
     RIAVIERHGK TGGRATGFVR GFGMARGAIA STVCHDHHNL AVVGIDYADM ALAANRLRAL
     EGGFAVAAGG EILAELALPV GGLMSLRPFE EVRDALVTLR EAARSLGVTL EEPFLQLAFL
     ALPVIPHLKI TDRGMVDVDR FEILP