ID   ADEC_METMA              Reviewed;         555 AA.
AC   Q8PT13;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=MM_2910;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM32606.1; -; Genomic_DNA.
DR   RefSeq; WP_011034812.1; NC_003901.1.
DR   AlphaFoldDB; Q8PT13; -.
DR   SMR; Q8PT13; -.
DR   STRING; 192952.MM_2910; -.
DR   DNASU; 1481252; -.
DR   EnsemblBacteria; AAM32606; AAM32606; MM_2910.
DR   GeneID; 24839510; -.
DR   KEGG; mma:MM_2910; -.
DR   PATRIC; fig|192952.21.peg.3363; -.
DR   eggNOG; arCOG00693; Archaea.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000000595; 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   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..555
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142442"
SQ   SEQUENCE   555 AA;  61369 MW;  12B85B52C53DF40F CRC64;
     MKKYMGIIVD AISRRQFKGE ITVENGKIIR VEEKEHDNEQ YILPGLVDAH VHIESSMTVP
     SVFARMAVAK GTVAVVSDPH EIANVMGEEG IEFMLEDSKK SPLKVYFGVP SCVPATPFES
     SGAVLDINAV DRLLAKDDLH YLSEMMNFPG VILEFPDVMA KLESARKHGK VIDGHAPGLR
     GADLQKYIGA GISTDHECFE YEEAREKIEL GMKILIREGS SARNFETLYP LIDEYPDHVM
     LCTDDSHPDT LIYEGHIDKL IRRGQEKGLD IYNLIRTAVF NPVEHYGLNV GLLREGDPAD
     FIIVDNLKSF NILSTFIDGE CVYENGKVLF PLEKVPAKNV FNRNKISIDD VKLVPPAGAI
     QEQTTEKGIK KIRVIVANDG ELVTGQELIV PKIENGNLVS DPERDILKMV VLSRYSDDPV
     RIGFIKNIGL EKGAIASSIA HDSHNIIAVG ATDEDIVETV NRLIKNKGGI AVGTAENLLD
     LPLEVAGLMS TLEGEEVASR YHLLNEEARK LGTSLESPFM TLAFMSLLVI PELKLGDKGL
     FDVTKFEFVD LFADE