ID   ADEC_DESAL              Reviewed;         569 AA.
AC   B8FLT9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=Dalk_3756;
OS   Desulfatibacillum aliphaticivorans.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfatibacillum.
OX   NCBI_TaxID=218208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK-01;
RX   PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA   Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA   Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT   "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT   for anaerobic alkane oxidation.";
RL   Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL05443.1; -; Genomic_DNA.
DR   RefSeq; WP_015948494.1; NC_011768.1.
DR   AlphaFoldDB; B8FLT9; -.
DR   SMR; B8FLT9; -.
DR   PRIDE; B8FLT9; -.
DR   EnsemblBacteria; ACL05443; ACL05443; Dalk_3756.
DR   KEGG; dal:Dalk_3756; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_7; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000000739; 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..569
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146231"
SQ   SEQUENCE   569 AA;  60194 MW;  3722802EC88F7DD9 CRC64;
     MIDDQVIAAA RGDIPCDLVL KNAQIVNVFS GEIQKGDVAV QGGKVAALDS RDAKITVDLE
     GRFLTPGLID AHVHIESSMV SPYQYARTVI LHGTTAVIAD PHEIANVMGV DGVSYMIQAA
     EGAPVGIFYA VPSCVPATHL ETAGASLETK DILPFLEHPK IVGLAEMMNF PGVIYRDPEV
     LAKMNAAKSH RKTVDGHAPG LSGADLQAYL AAGAASDHEC TTPEEALEKL ASGMRIMIRQ
     GTGAKNLNDL LPIVTEQNSR RIMFCSDDRH PYDLLEKGHI NIMVARSIRQ GVDPVTAIRM
     ASLNTAEYFG LRDRGGIAPG MRADLLVVPD LVDFHVQDVY SGGVKVVEDG CGLPSPMDPP
     PRPQTSSMNV DVDGLDFTIK AGSGKARIIK LIPDQVVTAA MTGDVLQKNG EALSDPGNDI
     LKIAVVERHK GTGNIGLGFV NGFGLQKGAL ASSVAHDSHN IIVVGVDDAD MKAAVKAVAD
     MGGGLAAAAG GKALSVCPLP IAGLMSDQPM EQVRRQLDIL MQTAKELGAK AEDPFMSLSF
     LALPVIPELK ITDKGLVDVN LFNFVSLFE