HAMAP rule MF_01684
General rule information
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| Accession | MF_01684 |
| Dates | 19-NOV-2008 (Created)
1-JUN-2023 (Last updated, Version 23) |
| Name | Salvage_MtnN |
| Scope(s) |
Bacteria |
| Template(s) | P0AF12 (MTNN_ECOLI); O32028 (MTNN_BACSU); Q9R4A1 (MTNN_KLEPN); [ Recover all ] |
| Triggered by |
HAMAP; MF_01684 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | MTNN |
| Protein name | RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Short=MTA/SAH nucleosidase; Short=MTAN; EC=3.2.2.9; AltName: Full=5'-deoxyadenosine nucleosidase; Short=DOA nucleosidase; Short=dAdo nucleosidase; AltName: Full=5'-methylthioadenosine nucleosidase; Short=MTA nucleosidase; AltName: Full=S-adenosylhomocysteine nucleosidase; Short=AdoHcy nucleosidase; Short=SAH nucleosidase; Short=SRH nucleosidase; |
| Gene name | Name=mtnN; |
Comments
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| case <OC:Enterobacterales> | |
| FUNCTION | Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation. |
| else | |
| FUNCTION | Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. |
| end case | |
| CATALYTIC ACTIVITY | Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D- ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; |
| CATALYTIC ACTIVITY | Reaction=H2O + S-methyl-5'-thioadenosine = 5-(methylsulfanyl)-D-ribose + adenine; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:78440; EC=3.2.2.9; |
| CATALYTIC ACTIVITY | Reaction=5'-deoxyadenosine + H2O = 5-deoxy-D-ribose + adenine; Xref=Rhea:RHEA:29859, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:17319, ChEBI:CHEBI:149540; EC=3.2.2.9; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29860; |
| PATHWAY | Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'- thioadenosine (hydrolase route): step 1/2. |
| case <OC:Enterobacterales> | |
| SUBUNIT | Homodimer. |
| end case | |
| SIMILARITY | Belongs to the PNP/UDP phosphorylase family. MtnN subfamily. |
Keywords
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Gene Ontology
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| GO:0008782; Molecular function:adenosylhomocysteine nucleosidase activity | |
| GO:0008930; Molecular function:methylthioadenosine nucleosidase activity | |
| GO:0019284; Biological process:L-methionine salvage from S-adenosylmethionine | |
| case <OCellular component:Enterobacterales> | |
| GO:0046124; Biological process:purine deoxyribonucleoside catabolic process | |
| end case | |
Cross-references
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Features
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| From: MTNN_ECOLI (P0AF12) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 173 | 174 | /ligand="substrate" | M-[ED] | ||||||||
| ACT_SITE | 12 | 12 | /note="Proton acceptor" | E | ||||||||
| ACT_SITE | 197 | 197 | /note="Proton donor" | D | ||||||||
| BINDING | 78 | 78 | /ligand="substrate" | [GA] | ||||||||
| BINDING | 152 | 152 | /ligand="substrate" | [IVML] | ||||||||
Additional information
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| Size range | 221-251 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |