ID   ADEC_ROSDO              Reviewed;         600 AA.
AC   Q16CI8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=RD1_0605;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG30305.1; -; Genomic_DNA.
DR   RefSeq; WP_011566927.1; NZ_FOOO01000001.1.
DR   AlphaFoldDB; Q16CI8; -.
DR   SMR; Q16CI8; -.
DR   STRING; 375451.RD1_0605; -.
DR   EnsemblBacteria; ABG30305; ABG30305; RD1_0605.
DR   KEGG; rde:RD1_0605; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000007029; 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..600
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292397"
SQ   SEQUENCE   600 AA;  63867 MW;  20F38F5439799AD7 CRC64;
     MTHSPFPSWP DTAADLIAVA TGRMAADMLI RGGKWVNVHT REVLDGYDVA IIRGRIACVV
     PDATNCTGPD THMIRANGRY MIPGLCDGHM HIESGMLTPA EFARAVIPHG TTSMFTDPHE
     IANVLGLEGV RMMHDEALMQ PVNIFTQMPS CAPSAPGLET TGFEITAADV ADAMAWPGIV
     GLGEMMNFPG VSNADPKMLA EIAATQRAGK TVGGHYASPD LGPAFAGYIA GGPADDHEGT
     CEADAIARMR QGMRSMIRLG SAWYDVESQI TAITEKGLDP RNMILCTDDC HSGTLVNDGH
     MNRVVRHAIE CGCDPLVALQ MATINTATHF GLEREIGSIT PGRRADIILT SDLRTLPIET
     VIARGQVVAE DGHCLVECPH FDWPAAARQT VHMGKTLGPD DFTINAPKGA NAVTANVIGV
     VENQAPTKAL KFELPVTEGR VQATGDVAQI ALVERHRATG SVTNAFVSGF GYQGRMAMAS
     TVAHDSHHMI VVGTDADDMA RAANRLGEVG GGIVLFKDGV ELALVELPIA GLMSDRPAAE
     VAAKADKMMQ AMRDCGCTLN NAYMQHSLLA LVVIPELRIS DLGLVDVRTF EFIPVIESPT