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