ID   ADEC_RUEST              Reviewed;         601 AA.
AC   Q1GCT5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=TM1040_2799;
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX   NCBI_TaxID=292414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040;
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   Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL   Submitted (MAY-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; CP000377; ABF65531.1; -; Genomic_DNA.
DR   RefSeq; WP_011540113.1; NC_008044.1.
DR   AlphaFoldDB; Q1GCT5; -.
DR   SMR; Q1GCT5; -.
DR   STRING; 292414.TM1040_2799; -.
DR   PRIDE; Q1GCT5; -.
DR   EnsemblBacteria; ABF65531; ABF65531; TM1040_2799.
DR   KEGG; sit:TM1040_2799; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000000636; 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..601
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292400"
SQ   SEQUENCE   601 AA;  63889 MW;  44A7A81EBE745C76 CRC64;
     MTHKTFPSWP DVAPQLIETA AGRSPADTVI RNGKWVNVHT REVLEGHDIA IKAGRIAYVG
     PDASYCTGPE TEVIDAEGRY MMPGLCDGHM HIESGMLTPA EFARAVIPHG TTTMFTDPHE
     IANVLGLEGV RLMHDEALLQ PVNIYTQMPS CAPSAPGLET TGYEISAEDV AEAMTWPGII
     GLGEMMNFPG VAHGDPKMLA EIAATQRSGK TVGGHYASPD LGPDFAAYVA GGPADDHEGT
     CEADAITRMR QGMRAMVRLG SAWYDVEAQI TAITEKGLDP RNFILCTDDC HSGTLVNEGH
     MNRAVRHAID CGCDPLIAIQ MATINTATHF GLEREIGSIT PGRRADIILT SDLKTLPIEV
     VIARGQIVAE SGSIKVECPH LDWPESARGT VHLGHTLAAT DFELAAPEGA NAVTANVIGV
     VENQAPTKAL KAELPVRDGL VEGEGDVCQI ALVERHRATG GVTNAFVSGF GYEGKMAMAS
     TVAHDSHHMI VVGTDRTQMA LAANRLAEVG GGITIFRDGA ELALVELPIA GLMSDSPASE
     VAANAQKLVE AMQACGCTLN NAYMQHSLLA LVVIPELRIS DLGLVDVRSF KKIPVIEPFN
     E