ID   ADEC_DESVV              Reviewed;         575 AA.
AC   A1VGE5;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Dvul_2495;
OS   Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=391774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DP4;
RX   PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA   Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA   He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA   Stahl D.A.;
RT   "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT   plasticity.";
RL   Environ. Microbiol. 11:2244-2252(2009).
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; CP000527; ABM29511.1; -; Genomic_DNA.
DR   RefSeq; WP_011792891.1; NC_008751.1.
DR   AlphaFoldDB; A1VGE5; -.
DR   SMR; A1VGE5; -.
DR   PRIDE; A1VGE5; -.
DR   EnsemblBacteria; ABM29511; ABM29511; Dvul_2495.
DR   KEGG; dvl:Dvul_2495; -.
DR   HOGENOM; CLU_027935_0_0_7; -.
DR   OMA; TDHECFT; -.
DR   Proteomes; UP000009173; 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.
FT   CHAIN           1..575
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000296722"
SQ   SEQUENCE   575 AA;  60695 MW;  12B74EA01CFB6B47 CRC64;
     MTYRPLLNDL VDMAAGRAPV DLVVRNARIV DVFSQSIVEA PLAIGGGRFL GFFEAEAHAT
     LDAEGRYLLP GLIDGHVHIE SSLVSPAQFA RLVLARGTTA VIADPHEIAN VCGLAGLRYM
     LDATRDLPLD VRLALPSCVP ATPFENAGAV LDAAALATLM DDPRVAGLGE MMNFPGVLAG
     DADVLDKIAL ALDRGKTVDG HSPGLAGRDL ATYAAARIAT DHECTTVEEM HERIALGMYV
     LLREGSAARD MARLAPGITP GNARRCVFCT DDRQPADILR DGHIDNHLRI AVSHGVDPVT
     AVTIATLNAA ECFGLRDRGA VAPGRVADFV LVDDLTGFAV RKVYAAGRLV ARDGAVVVDL
     PDHADPAVRD TVNIRPLDDT AFRLPLPTGL ARVIGLQPHS LLTDALERDV PRDASGCFTP
     GDGLVKLAVV ERHKATGNVG VGIIEGYGLR GGAVATTVAH DSHNIVVAGD NDADMLVAVR
     ELERTGGGIT LCAGGRVLAS LPLPVAGLMS DRPATEVSET FAQMLSIAHE TLHISRDIEP
     FMTLSFLTLP VIPALKLTDR GLFDVRTFSF TTVGV