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ADEC_OLEA2
ID   ADEC_OLEA2              Reviewed;         570 AA.
AC   Q317F9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=Dde_0136;
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21685289; DOI=10.1128/jb.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
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; CP000112; ABB36937.1; -; Genomic_DNA.
DR   RefSeq; WP_011366306.1; NC_007519.1.
DR   AlphaFoldDB; Q317F9; -.
DR   SMR; Q317F9; -.
DR   STRING; 207559.Dde_0136; -.
DR   EnsemblBacteria; ABB36937; ABB36937; Dde_0136.
DR   KEGG; dde:Dde_0136; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_7; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000002710; 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..570
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000292381"
SQ   SEQUENCE   570 AA;  60480 MW;  81B399420402D5E3 CRC64;
     MKNNTMNTLI GAAQDESPVD LLVRNVRLVN VLSGEIHDAH IAVKDGIVVG FEEYEALHVV
     EGNGRHCIPG LIDGHIHIES TLLSPARFAA AAAPHGTAAV MCDPHEIANV MGAEGIEYML
     HASAGLPLSV YVMMPSCVPA THMETAGATL RAEDVQDFLS RYPDRMPGLA EMMNYPGVLF
     RDDEVMAKLE AAASHVIDGH APLLRGKALN AYVLGGPASD HETSDADEAR EKLRKGMHLM
     IREGGSQEHN LEELVTVLNE FNTQNVSFVS DDKVVNDLME SGHMDDILRK AMAAGIPPVR
     AVQMASINTA RYFRLHRRGA VAPGYRADFV LLDDLQTMRI SECYLGGRNV KEIDFTGHSA
     AFSANTVHVA GLNTDSLHVA AGNGNLRVIG IVPGQVITHA LELPPTLREG AAVADPSRDL
     AKLAVFERHK GTGNVGLGFT AGLGLHKGAL AGTVSHDSHN LIVAGMDDAD MITAAEEVQC
     IGGGLAVACD GRVLASLPLP IAGLMSDAPV EDVLAGLRGV NEALATLGYK LSSPFAALAF
     LSLAVIPSLK LTDKGLVDVH KFEIVPLWTA
 
 
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