ID   ADEC_DEHMC              Reviewed;         571 AA.
AC   Q3ZXH1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-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=cbdbA769;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(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; AJ965256; CAI82924.1; -; Genomic_DNA.
DR   RefSeq; WP_011309275.1; NC_007356.1.
DR   AlphaFoldDB; Q3ZXH1; -.
DR   SMR; Q3ZXH1; -.
DR   KEGG; deh:cbdbA769; -.
DR   HOGENOM; CLU_027935_0_0_0; -.
DR   OMA; TDHECFT; -.
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.
FT   CHAIN           1..571
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142415"
SQ   SEQUENCE   571 AA;  61452 MW;  60199447D7B0CFD5 CRC64;
     MQTNLSQLIK VARGETEADL VLLNARVINV FNAEIEQANV AVFDGKIAGV GDYRHGKEVI
     DLKGAYLLPG LINGHTHVES SMLDIAQYAR AVVSHGTLAL ITDLHEISNV CGKEGIDYVL
     DASADLPLSI FLQVPSCVPA THLETAGAEI NSQDVADLLR LPNVTGLGEM MNFPGVLFGV
     PSVLDKIIAA AGKVLDGHAP GLSGKDLNAY ISAGIHSDHE CIHLAEAKEK LARGMYIMIR
     EGSSEKNLAE LLPLVTDQTY KRCLFVVDDR SCADLKSDGD IDAVVRKAIR LGLDPVRAIQ
     LASINTAEYF HLQGHGAIAP GYLANMIVCQ NLEQLDIDMV FHKGKLVAEK GQALFKPQSR
     IPKSLLNSIH IRPFDTKDLI LKTIQPQIPV IEVIPGQIVT RRLDLKIPAE NGVIKANTEL
     DLLKIVVMER HHQSGNMGHG LIRGFGLKKG AIASSVAHDS HNVVAVGTND ADLYTAIKEL
     ERINGGIALA VDGQVTASVS LPVAGLLSTK PLEEVVTELE EINNQVAKLG CKLSAPFATL
     SFMALPVIPE LRLTDLGLVD VKTFKLIPQE T