ID   ADEC_DEIDV              Reviewed;         558 AA.
AC   C1CZZ4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=Deide_04190;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO45246.1; -; Genomic_DNA.
DR   RefSeq; WP_012692369.1; NC_012526.1.
DR   AlphaFoldDB; C1CZZ4; -.
DR   SMR; C1CZZ4; -.
DR   STRING; 546414.Deide_04190; -.
DR   PaxDb; C1CZZ4; -.
DR   EnsemblBacteria; ACO45246; ACO45246; Deide_04190.
DR   KEGG; ddr:Deide_04190; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_0; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000002208; 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..558
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000215359"
SQ   SEQUENCE   558 AA;  58530 MW;  A297D304FB705BB6 CRC64;
     MTQWAMTESL EDRRRLVRVA RGLEEGDLLV RGARVAQPVT REILEADVLI ADGRVAVLGG
     TGDGLQAARV VEARGAFLAP GFIDGHVHIE SSLLTPAGFA RAVLLRGTTG VVAEPHEVVN
     VLGPQGLEWM LEAGRRSGLR VWASAPSCAP ASGFEAGGAR VGTAEVRQML GQPGVLGLAE
     MMNYPGVLGG DEEVWAVIQA GRATGRRLDG HAAGVRGRDL QAYAAAGLHS DHEATTPEEA
     RERLRAGLWL MVREGSAARN LQALLPVLRE RPRRAMLVSD DVSVDELLEL GHLDRLLRAC
     VAGGLDPLDA LALVTCNPAE YWGLHDVGLI APGHLADFVL LRDLQSFEVL ETFVGGAEAQ
     PGELTPPLSG GGVHLGQGWD AATFEVPPGW PVLGIHAEQI TTSREPEGSG DARLIVADRY
     GRGEWSACWT AGSGLTGGTL GISVLHDAHH AAFLGGSDTD VRMAGRALEA LGGGLVVVSD
     GEVRASLPLP FAGLMTGEAP QEAAAGLARV TAATRALGCT LPYPVTTLSF LGLTVIPSLK
     LTPRGLLDVE AWQLVPSR