DADD_METB6
ID DADD_METB6 Reviewed; 442 AA.
AC A7I6C5;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Mboo_0768;
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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; CP000780; ABS55286.1; -; Genomic_DNA.
DR RefSeq; WP_012106309.1; NC_009712.1.
DR AlphaFoldDB; A7I6C5; -.
DR SMR; A7I6C5; -.
DR STRING; 456442.Mboo_0768; -.
DR EnsemblBacteria; ABS55286; ABS55286; Mboo_0768.
DR GeneID; 5410708; -.
DR KEGG; mbn:Mboo_0768; -.
DR eggNOG; arCOG00695; Archaea.
DR HOGENOM; CLU_012358_2_1_2; -.
DR OMA; ALIGKVC; -.
DR OrthoDB; 40873at2157; -.
DR UniPathway; UPA00315; -.
DR Proteomes; UP000002408; Chromosome.
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; Reference proteome; Zinc.
FT CHAIN 1..442
FT /note="5'-deoxyadenosine deaminase"
FT /id="PRO_0000312477"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01281"
SQ SEQUENCE 442 AA; 47461 MW; 1F44C7460FDEB5AD CRC64;
MTTQESADIF GNNKSILITN VNDGTGPVDI FIDAEETISD IGCEIRKRHR GEAEFIVDGA
GALALPGLSN THTHAAMSLL RGYADDMILQ DWLAQKIWPL EAHLTADDVY WGTRLACLEM
IRTGTTAFND MYFFMESAAK AVDEAGIRAL LCYGFIDLGD AEKRERECRA TEALVAHIRG
LKNSRIHAAA GPHAPYTVSP EGLKWCGEFS REQDIPVHIH LSETEKEVND CVARHKKRPA
ALLDECGLLS PRTIAAHGCW LDDAECALLG KRGVSVSHNP ASNMKLATHR ALPYRELVAA
GANVCLGTDG CASNNNLDLF EEMKIAALLQ KFFWNDPTVL AAPEALGMAT ANGAKALGFG
DGALVAGAPA DLILVTTRTP ANTPLHNAAS NLVYACSGSA VETTICNGRV LMFDREIPGE
EKVLAEAAGA AARLVRRAQT PS
