ID   ADEC_CERS5              Reviewed;         565 AA.
AC   A4WP35;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Rsph17025_0239;
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3;
RG   US DOE Joint Genome Institute;
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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-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; CP000661; ABP69149.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WP35; -.
DR   SMR; A4WP35; -.
DR   STRING; 349102.Rsph17025_0239; -.
DR   EnsemblBacteria; ABP69149; ABP69149; Rsph17025_0239.
DR   KEGG; rsq:Rsph17025_0239; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   BioCyc; RSPH349102:G1G8M-245-MON; -.
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..565
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000068612"
SQ   SEQUENCE   565 AA;  60663 MW;  EB510265D1D0F6EC CRC64;
     MRRSLSDLID QGRGKAPADL VLKNGRIFDL VTGELVQTDV AICGDRIVGT FGTYEGRREI
     DCRGRILVPG FIDTHLHVES SLVTPFEFDR CVTPRGITTA ICDPHEIANV CGLEGIRYFL
     EAAEHLVMDL RVQLSSCVPS THMETAGATL EAADLVPLMD HPRVIGLAEF MNFPGVLAKD
     AGCLAKLEAF RGRHIDGHAP LLRGKDLNGY IAAGIRTEHE ATTAEEALEK LRKGMRVLIR
     EGSVSRDLEA LVPLLTERHS PYLCLCTDDR NPLDIAEHGH IDHMIRTAIR LGAPPLAVYR
     AASLSAAEAF GLKDRGLIAP GKRADVVALD SLEGCHAGLV VAGGVVVDAG AFAARGTVEP
     VARASVRVAP VEAAAFRCPG NRAETPVIGI LPGKIITEHL TDAIEPVDGD KRPDPSRDLA
     RIAVIERHGR NGGRAVGFVR GFGMRRGAIA STVCHDHHNL AVVGVDYADM ALAANRLREI
     EGGFAVAAEG EILAELALPV GGLMSLRPFE EVRDALVALR EAARGLGVTL EEPFLQLAFL
     ALPVIPHLKI TDRGIVDVDR FEILP