ID   ADEC_CERS4              Reviewed;         565 AA.
AC   Q3IZ66;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=RHOS4_26000;
GN   ORFNames=RSP_0985;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) 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; CP000143; ABA80168.1; -; Genomic_DNA.
DR   RefSeq; WP_011338640.1; NZ_CP030271.1.
DR   RefSeq; YP_354069.1; NC_007493.2.
DR   AlphaFoldDB; Q3IZ66; -.
DR   SMR; Q3IZ66; -.
DR   STRING; 272943.RSP_0985; -.
DR   DNASU; 3720739; -.
DR   EnsemblBacteria; ABA80168; ABA80168; RSP_0985.
DR   KEGG; rsp:RSP_0985; -.
DR   PATRIC; fig|272943.9.peg.2957; -.
DR   eggNOG; COG1001; Bacteria.
DR   OMA; TDHECFT; -.
DR   PhylomeDB; Q3IZ66; -.
DR   Proteomes; UP000002703; 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; 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..565
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000296729"
SQ   SEQUENCE   565 AA;  60661 MW;  5BB0398EF4251CB0 CRC64;
     MSRSLSECID QGRGLVPADL VLKHGRVFDL VTGELVQTDV AICGDRIVGT FGTYTGRREI
     DCRGRILVPG FIDTHLHVES SLVTPFEFDR CVTPRGITTA ICDPHEIANV CGLEGIRYFL
     EASAHLVMDL RVQLSSCVPS THMETAGAAL EAKDLAPLMD HPRVIGLAEF MNFPGVLMKD
     PGCMAKLEAF RGRHIDGHAP LLRGKDLNGY IAAGIRTEHE ATTAEEALEK LRKGMRVLIR
     EGSVSKDLHA LVSILTERHA PYLCLCTDDR NPLDIAEHGH IDHMIRTAIR LGAPPLAVYR
     AASLSAADAF GLKDRGLIAP GRRADIAVLD SLEGCHAALV LAGGVVADDA AFSARSDIEP
     VARASVKVAE IAPEAFRCPG NRADTPVIGI LPGKIITEHL TAEIEPVDGD KRPDPVRDLA
     RIAVIERHGK TGGRATGFVR GFGMARGAIA STVCHDHHNL AVVGIDYADM ALAANRLRAL
     EGGFAVAAGG EILAELALPV GGLMSLRPFE EVRDALVTLR EAARSLGVTL EEPFLQLAFL
     ALPVIPHLKI TDRGMVDVDR FEILP