HAMAP rule MF_01281

General rule information [?]

PURL	https://purl.expasy.org/hamap/rule/MF_01281
Accession	MF_01281
Dates	07-NOV-2007 (Created) 03-SEP-2024 (Last updated, Version 28)
Name	MTA_SAH_deamin
Scope(s)	Bacteria Archaea
Template(s)	Q9X034; Q58936; [ Recover all ]
Triggered by	HAMAP; MF_01281 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
Identifier	DADD
Protein name	RecName: Full=5'-deoxyadenosine deaminase; Short=5'-dA deaminase; EC=3.5.4.41; AltName: Full=5'-methylthioadenosine deaminase; Short=MTA deaminase; EC=3.5.4.31; AltName: Full=Adenosine deaminase; EC=3.5.4.4; AltName: Full=S-adenosylhomocysteine deaminase; Short=SAH deaminase; EC=3.5.4.28;
Gene name	Name=dadD;
else
Identifier	MTAD
Protein name	RecName: Full=5-methylthioadenosine/S-adenosylhomocysteine deaminase; Short=MTA/SAH deaminase; EC=3.5.4.28; EC=3.5.4.31;
Gene name	Name=mtaD;
end case

Comments [?]

case <OC:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
FUNCTION	Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'- methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'- deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'- deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
CATALYTIC ACTIVITY	Reaction=5'-deoxyadenosine + H2O + H(+) = 5'-deoxyinosine + NH4(+); Xref=Rhea:RHEA:42892, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:28938, ChEBI:CHEBI:82775; EC=3.5.4.41; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42893;
CATALYTIC ACTIVITY	Reaction=S-adenosyl-L-homocysteine + H2O + H(+) = S-inosyl-L- homocysteine + NH4(+); Xref=Rhea:RHEA:20716, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57856, ChEBI:CHEBI:57985; EC=3.5.4.28; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20717;
CATALYTIC ACTIVITY	Reaction=S-methyl-5'-thioadenosine + H2O + H(+) = S-methyl-5'- thioinosine + NH4(+); Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938, ChEBI:CHEBI:48595; EC=3.5.4.31; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25026;
CATALYTIC ACTIVITY	Reaction=adenosine + H2O + H(+) = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409;
PATHWAY	Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis.
SUBUNIT	Homotetramer.
MISCELLANEOUS	SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L- homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine. 5'-deoxyadenosine is a radical SAM enzyme reaction product which strongly inhibits radical SAM enzymes. A pathway for removing this product must be present in methanogens where the MTA/SAH nucleosidase which normally metabolizes this compound is absent.
else
FUNCTION	Catalyzes the deamination of 5-methylthioadenosine and S- adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L- homocysteine, respectively. Is also able to deaminate adenosine.
CATALYTIC ACTIVITY	Reaction=S-adenosyl-L-homocysteine + H2O + H(+) = S-inosyl-L- homocysteine + NH4(+); Xref=Rhea:RHEA:20716, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57856, ChEBI:CHEBI:57985; EC=3.5.4.28;
CATALYTIC ACTIVITY	Reaction=S-methyl-5'-thioadenosine + H2O + H(+) = S-methyl-5'- thioinosine + NH4(+); Xref=Rhea:RHEA:25025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:28938, ChEBI:CHEBI:48595; EC=3.5.4.31;
end case
COFACTOR	Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
SIMILARITY	Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.

Keywords [?]

Hydrolase

Metal-binding

Zinc

Gene Ontology [?]

case <OCellular component:Methanobacteria> or <OC:Methanococci> or <OC:Methanomicrobia> or <OC:Methanopyri>
GO:0090613; Molecular function:5'-deoxyadenosine deaminase activity
GO:0004000; Molecular function:adenosine deaminase activity
GO:0006556; Biological process:S-adenosylmethionine biosynthetic process
else; https://www.ebi.ac.uk/QuickGO/term/else
GO:0050270; Molecular function:S-adenosylhomocysteine deaminase activity
GO:0090614; Molecular function:5'-methylthioadenosine deaminase activity
end case

Cross-references [?]

Pfam	PF01979; Amidohydro_1; 1;

Features [?]

From: MTAD_THEMA (Q9X034)

Key

From

Description

Tag

Condition

FTGroup

BINDING

/ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"

BINDING

/ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"

BINDING

200

/ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"

BINDING

279

/ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"

BINDING

/ligand="substrate"

BINDING

136

/ligand="substrate"

BINDING

148

/ligand="substrate"

BINDING

173

/ligand="substrate"

BINDING

203

/ligand="substrate"

BINDING

279

/ligand="substrate"

Additional information [?]

Size range	406-449 amino acids
Related rules	None
Fusion	Nter: None Cter: None

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