ID   ADEC_CHESB              Reviewed;         600 AA.
AC   Q11JE6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Meso_1082;
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNC1;
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., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) 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; CP000390; ABG62479.1; -; Genomic_DNA.
DR   RefSeq; WP_011580422.1; NC_008254.1.
DR   AlphaFoldDB; Q11JE6; -.
DR   SMR; Q11JE6; -.
DR   STRING; 266779.Meso_1082; -.
DR   EnsemblBacteria; ABG62479; ABG62479; Meso_1082.
DR   KEGG; mes:Meso_1082; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; MVTACAY; -.
DR   OrthoDB; 751534at2; -.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese.
FT   CHAIN           1..600
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000296728"
SQ   SEQUENCE   600 AA;  64391 MW;  1569B9FAD02D1C05 CRC64;
     MSTLTRFSVR PLATMTRHLA DVASGRAEPD LVIKGARVLS TYSERILPDR EVWISGGRIA
     AVKPAGSYRG SAATIYDAAG GLIAPGLVDP HIHIESSMVT ACSYAEAALL NGTTTIFCDS
     HEIGNVMDVA GVEAMLEDAR QAPSSIFLTV PSTVPATSPE LETAGGDLTA EKIAALFDKW
     PEAVALGEKM DFVQVAMGDE RSHAILAAAL ERGRPVSGHV YGREFVAAYA ASGVTDTHEA
     IDREIADDLL EAGIWLFLRG GPPTTPWHSL PQAIKTITEL GASHKRIAVC TDDRDADDLL
     LFGLDWVTRE AMKAGMKPEQ AWAMGSLHGA TRFGLEGDIG GLGGGRRADL VLLDDGFKPV
     NTWYGGELVV ENRKITPLLD TALSNRYRYP EAAYHTVKLP KAVKLTPELP TARVVAHTIR
     TELPGITLGH ERITLEPSNH WQDHFDRHGL CFVAVVERHG KSAGNVAHGL LSNFNLKRGA
     VASSVGHDSH NIIVAGTNEA DMQVALRAIE EAQGGVCVVM DGKVTAMVPL PIAGLLSDKR
     VTEVAEEVKA LKVEWEKAGC SIPYMGFNLI PLSVIPEIRI TDKGLVLVPE MEIVQLFEAA