ID   ADEC_DEHMB              Reviewed;         571 AA.
AC   A5FR71;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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};
GN   OrderedLocusNames=DehaBAV1_0717;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 /
OS   BAV1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=216389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1;
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., Pitluck S., Lowry S., Clum A.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Ritalahti K.M., Loeffler F., Richardson P.;
RT   "Complete sequence of Dehalococcoides sp. BAV1.";
RL   Submitted (MAY-2007) 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; CP000688; ABQ17301.1; -; Genomic_DNA.
DR   RefSeq; WP_011929044.1; NC_009455.1.
DR   AlphaFoldDB; A5FR71; -.
DR   SMR; A5FR71; -.
DR   KEGG; deb:DehaBAV1_0717; -.
DR   PATRIC; fig|216389.18.peg.766; -.
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_1000087545"
SQ   SEQUENCE   571 AA;  61433 MW;  E4F742629731AF58 CRC64;
     MQTNLSQLIK VARGETEADL VLLNARVINV FNAEIEQTNV AVFDGKIAGV GDYRHGKEVI
     DLKGAYLLPG LINGHTHVES SMLDIAQYAR AVVSNGTLAL ITDLHEISNV CGKEGIDYVL
     DASADLPLSI FLQVPSCVPA THLETAGAEI NSQDVADLLR LPNVTGLGEM MNFPGVLFGV
     PSVLDKIIAA TGKVMDGHAP GLSGKDLNAY ISAGIHSDHE CIHLAEAKEK LARGMYIMIR
     EGSSEKNLAE LLPLVTDKTY KRCLFVVDDR SCADLKSDGD IDAVVRKAIR LGLDPVRAIQ
     LASINTAEYF HLQGHGAIAP GYLANMIVCQ NLEQLDIDMV FHKGKLVAEK GQALFKPQSR
     IPKSLLNSIH IKPFNTEDLV LKTIQPQIPV IEVIPGQIVT RRLDLKITAE NGVIKANTEL
     DLLKIVVLER HHQSGNIGHG LIRGFGLKKG AIASSVAHDS HNVVAVGTND ADLYTAIKEL
     ERINGGIALA VDGQVTASVS LPVAGLLSTK PLEEVVTELE EINNQVAKLG CKLSAPFATL
     SFMALPVIPE LRLTDLGLVD VKTFKLIPQE T