ID   ADEC_RUBXD              Reviewed;         606 AA.
AC   Q1AZ25;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Rxyl_0377;
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
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; CP000386; ABG03353.1; -; Genomic_DNA.
DR   RefSeq; WP_011563371.1; NC_008148.1.
DR   AlphaFoldDB; Q1AZ25; -.
DR   SMR; Q1AZ25; -.
DR   STRING; 266117.Rxyl_0377; -.
DR   EnsemblBacteria; ABG03353; ABG03353; Rxyl_0377.
DR   KEGG; rxy:Rxyl_0377; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_11; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   PhylomeDB; Q1AZ25; -.
DR   Proteomes; UP000006637; Chromosome.
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; Reference proteome.
FT   CHAIN           1..606
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292398"
SQ   SEQUENCE   606 AA;  64643 MW;  7AC78CFFF79D5D9B CRC64;
     MEERGRRKPL YEMTRELAAT ARGDLPATLV IRDGTLVSVT SGEVLPGMSV AVRGPRIAYV
     GPDAGHTVGP QTTVIDAAGR YIAPGFLDGH CHIESSQITV TQFARAVLPL GTTGGFFDAH
     EITNVLGLRG LRLMLDEARS TPLAAYLEVA SCVPSTSTEL ETPGAVIGPE EVAEALSWGE
     DVIALGEVMN FPGVVFGDER MHAEISAALR AGKIADGHFC WPPDDHRLAA YAASGISGCH
     EGTTPEDTLW RLRQGMYAKL RRGSAWHDVA ATIKAHTERG LDPRRILLVT DDRSPESLLE
     EGHMDFVVRH AIAQGVNPVT AFQMATLNPA ERFRVSHDVG SVTPGRYADI LLLEGDLAEV
     RVSLTVAAGE VVAEGGRMVA ELEPYDYPAF CLDTVRVAGG LGPEDFDIPA PGGGERARVR
     AIRVVENHVE TRGEWVELPV EGGLVRLDPR KDVCKLFVIE RHGRGGGRGA GFVTGLGFER
     PAALASTVAH DSHNLMVLGN SEELMSRAAR EVVAARGGVA VAVGGETAVL PLPVAGLMSP
     EPYEEVARLS REIGRALRSA GCRMNYAFMT ISLLALVVLP ELHLSDRGLV EVGEEGFRLV
     GLAAEG