ID   ADEC_DEHM1              Reviewed;         571 AA.
AC   Q3Z8C6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=DET0791;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS   (Dehalococcoides ethenogenes (strain 195)).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA   Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA   Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA   Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA   Zinder S.H., Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(2005).
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; CP000027; AAW39904.1; -; Genomic_DNA.
DR   RefSeq; WP_010936524.1; NC_002936.3.
DR   AlphaFoldDB; Q3Z8C6; -.
DR   SMR; Q3Z8C6; -.
DR   STRING; 243164.DET0791; -.
DR   PRIDE; Q3Z8C6; -.
DR   EnsemblBacteria; AAW39904; AAW39904; DET0791.
DR   KEGG; det:DET0791; -.
DR   PATRIC; fig|243164.10.peg.755; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_0; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000008289; 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..571
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142414"
SQ   SEQUENCE   571 AA;  61063 MW;  82F658B11AF088A8 CRC64;
     MQTNLSQLIK VARGEAKADL VLLNARVVNV FNAEIEPANV AVFGGQIAGV GDYTLGNRVL
     DLKGAYLLPG LINGHTHVES SMLDISQYAR AVIAHGTSAL ITDLHEISNV CGKEGIDYVL
     SASADLPLNI FLQVPSCVPA THLETAGAEI NSNDVTELLR LPNVTGLGEM MNFPGVLFGI
     PSVLDKIEAA SGKVLDGHAP GLSGKDLNAY ISAGIHSDHE CIQLDEAKEK LARGMYIMIR
     EGSSEKNLTE LLPLVTDKTY KRCIFVVDDR SCADLQRDGD IDAVVRKAIK LGLDPVRAIQ
     LASINTAEYF RLNGHGAIAP GYLANMIVCQ DLNQLDIDMV FHKGELVAEK GQVLFKPQSH
     VPKSLLSSMH IKPFDIKDLA IKGSSTQMPV IEVIPGQIVT RRLNLKIPAE NGVLTPDIEQ
     DLLKIVVLER HCQSGNIGRG LIKGFGLKKG AIASSVAHDS HNVIAVGTND ADIYTAVKEL
     ERINGGIALV VDGKISASVP LPVAGLLSTQ PLEKVVDALE EINKQAAGLG CKLSAPFATL
     SFMALPVIPE LRLTDLGLVD VNAFKLIPQE T