DADD_METBF
ID DADD_METBF Reviewed; 432 AA.
AC Q466Q9;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=5'-deoxyadenosine deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE Short=5'-dA deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE EC=3.5.4.41 {ECO:0000255|HAMAP-Rule:MF_01281};
DE AltName: Full=5'-methylthioadenosine deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE Short=MTA deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE EC=3.5.4.31 {ECO:0000255|HAMAP-Rule:MF_01281};
DE AltName: Full=Adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE EC=3.5.4.4 {ECO:0000255|HAMAP-Rule:MF_01281};
DE AltName: Full=S-adenosylhomocysteine deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE Short=SAH deaminase {ECO:0000255|HAMAP-Rule:MF_01281};
DE EC=3.5.4.28 {ECO:0000255|HAMAP-Rule:MF_01281};
GN Name=dadD {ECO:0000255|HAMAP-Rule:MF_01281}; OrderedLocusNames=Mbar_A3252;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
CC -!- FUNCTION: Catalyzes the deamination of three SAM-derived enzymatic
CC products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-
CC methylthioadenosine, to produce the inosine analogs. Can also deaminate
CC adenosine. The preferred substrate for this enzyme is 5'-
CC deoxyadenosine, but all these substrates are efficiently deaminated.
CC Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway
CC from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent
CC methylation reactions. May also be involved in the recycling of 5'-
CC deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine
CC is further metabolized to deoxyhexoses used for the biosynthesis of
CC aromatic amino acids in methanogens. {ECO:0000255|HAMAP-Rule:MF_01281}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5'-deoxyadenosine + H(+) + H2O = 5'-deoxyinosine + NH4(+);
CC Xref=Rhea:RHEA:42892, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:28938, ChEBI:CHEBI:82775; EC=3.5.4.41;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42893;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-
CC homocysteine; Xref=Rhea:RHEA:20716, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:57985; EC=3.5.4.28; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20717;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + S-methyl-5'-thioadenosine = NH4(+) + S-methyl-5'-
CC thioinosine; Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:48595; EC=3.5.4.31; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25026;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01281};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01281};
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01281}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01281}.
CC -!- MISCELLANEOUS: SAH is a product of SAM methyltransferases and is known
CC to be a feedback inhibitor of these enzymes. As a result of this
CC inhibition, organisms have evolved efficient enzymes to metabolize SAH
CC via different pathways. The pathway found in methanogens differs from
CC the canonical pathway, it uses the deamination of S-adenosyl-L-
CC homocysteine to form S-inosyl-L-homocysteine for the regeneration of
CC SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM
CC enzyme reaction product which strongly inhibits radical SAM enzymes. A
CC pathway for removing this product must be present in methanogens where
CC the MTA/SAH nucleosidase which normally metabolizes this compound is
CC absent. {ECO:0000255|HAMAP-Rule:MF_01281}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC MTA/SAH deaminase family. {ECO:0000255|HAMAP-Rule:MF_01281}.
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DR EMBL; CP000099; AAZ72133.1; -; Genomic_DNA.
DR RefSeq; WP_011308173.1; NC_007355.1.
DR AlphaFoldDB; Q466Q9; -.
DR SMR; Q466Q9; -.
DR STRING; 269797.Mbar_A3252; -.
DR EnsemblBacteria; AAZ72133; AAZ72133; Mbar_A3252.
DR GeneID; 3627729; -.
DR KEGG; mba:Mbar_A3252; -.
DR eggNOG; arCOG00695; Archaea.
DR HOGENOM; CLU_012358_2_1_2; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 40873at2157; -.
DR UniPathway; UPA00315; -.
DR GO; GO:0090613; F:5'-deoxyadenosine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0090614; F:5'-methylthioadenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050270; F:S-adenosylhomocysteine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_01281; MTA_SAH_deamin; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR023512; Deaminase_MtaD/DadD.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..432
FT /note="5'-deoxyadenosine deaminase"
FT /id="PRO_0000312480"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ SEQUENCE 432 AA; 46970 MW; 2F7EEC103995037B CRC64;
MADIIVKNAY VMTMDPDEGD LKNGTVVIED GKITEIGEKT SESADTVIDA KHSVVMPGLV
NTHTHAAMTL FRGYADDLQL ADWLEGHIWP AEAKLTAEDV YKGSLLACLE MIRSGTTSFA
DMYFYMDETA KAVEASGLRA SLCHGLIELW NEEKGATDLK EGKRFVRAWQ GAADGRIKTM
YGPHAPNTCS EEFLAKVREE ANRDGAGIHI HLLETEAELL AMKERYGKCS VHLLEDIGFL
GPDVLAAHCV WLSDGDIEIL GKRGVNVSHN VISNMKLASG IAPVYKMLEK GVNVSLGTDG
CASNNNLDLF EEMKTAALLH KVNTFSPTAL PARQVLQMGT VNGAKALGTE TGMLKVGMKA
DLIVVDMKKA HLTPCFDVPS HLVYSAKGSD VRTTIVNGKV LMDDYKVLAL DEQKVMEDAQ
KAAEELVTRV NA
