ID   ADEC_DESVH              Reviewed;         575 AA.
AC   Q72EX7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=DVU_0441;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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   -!- INTERACTION:
CC       Q72EX7; Q72EZ0: DVU_0428; NbExp=2; IntAct=EBI-10071496, EBI-10070754;
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; AE017285; AAS94924.1; -; Genomic_DNA.
DR   RefSeq; WP_010937748.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_009665.1; NC_002937.3.
DR   AlphaFoldDB; Q72EX7; -.
DR   SMR; Q72EX7; -.
DR   IntAct; Q72EX7; 1.
DR   STRING; 882.DVU_0441; -.
DR   PaxDb; Q72EX7; -.
DR   EnsemblBacteria; AAS94924; AAS94924; DVU_0441.
DR   KEGG; dvu:DVU_0441; -.
DR   PATRIC; fig|882.5.peg.419; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_7; -.
DR   OMA; TDHECFT; -.
DR   PhylomeDB; Q72EX7; -.
DR   Proteomes; UP000002194; 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   1: Evidence at protein level;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..575
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000142419"
SQ   SEQUENCE   575 AA;  60692 MW;  F00B188B80C45262 CRC64;
     MTYRPLLNDL VDMAAGRAPV DLVVRNARIV DVFSQRIVEA PLAIGGGRFL GFFEAEAHAT
     LDAEGRYLLP GLIDGHVHIE SSLVSPAQFA RLVLARGTTA VIADPHEIAN VCGLAGLRYM
     LDATRDLPLD VRLALPSCVP ATPFENAGAV LDAAALATLM DDPRVAGLGE MMNFPGVLAG
     DADVLDKIAL ALDRGKTVDG HSPGLAGRDL ATYAAARIAT DHECTTVDEM 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 DRPATEVSAT FAQMLSIAHE TLHISRDIEP
     FMTLSFLTLP VIPALKLTDR GLFDVRTFSF TTVGV