HAMAP rule MF_01682
General rule information
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Accession | MF_01682 |
Dates | 4-NOV-2008 (Created) 19-NOV-2022 (Last updated, Version 20) |
Name | Salvage_MtnD |
Scope | Bacteria |
Templates | Q9ZFE7 (MTND_KLEOX); O31669 (MTND_BACSU): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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Function | Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway. |
Catalytic activity | RHEA:14161: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + CO + formate + 2 H(+)
EC 1.13.11.53 |
RHEA:24504: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+)
EC 1.13.11.54 |
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Cofactor | Fe(2+) Note: Binds 1 Fe(2+) cation per monomer. |
Ni(2+) Note: Binds 1 nickel ion per monomer. |
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Pathway | Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6. |
Subunit | Monomer. |
Similarity | Belongs to the acireductone dioxygenase (ARD) family. |
Keywords
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Amino-acid biosynthesis
Dioxygenase
Iron
Metal-binding
Methionine biosynthesis
Nickel
Oxidoreductase
Dioxygenase
Iron
Metal-binding
Methionine biosynthesis
Nickel
Oxidoreductase
Gene Ontology
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GO:0005506; Molecular function: iron ion binding.
GO:0010308; Molecular function: acireductone dioxygenase (Ni2+-requiring) activity.
GO:0010309; Molecular function: acireductone dioxygenase [iron(II)-requiring] activity.
GO:0016151; Molecular function: nickel cation binding.
GO:0019284; Biological process: L-methionine salvage from S-adenosylmethionine.
GO:0010308; Molecular function: acireductone dioxygenase (Ni2+-requiring) activity.
GO:0010309; Molecular function: acireductone dioxygenase [iron(II)-requiring] activity.
GO:0016151; Molecular function: nickel cation binding.
GO:0019284; Biological process: L-methionine salvage from S-adenosylmethionine.
Cross-references
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Pfam | PF03079; ARD; 1; |
Features
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From: MTND_KLEOX (Q9ZFE7) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 97 | 97 | /ligand="Fe(2+)" /ligand_id="ChEBI:CHEBI:29033 | H | ||||||||
BINDING | 97 | 97 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786 | H | ||||||||
BINDING | 99 | 99 | /ligand="Fe(2+)" /ligand_id="ChEBI:CHEBI:29033 | H | ||||||||
BINDING | 99 | 99 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786 | H | ||||||||
BINDING | 103 | 103 | /ligand="Fe(2+)" /ligand_id="ChEBI:CHEBI:29033 | E | ||||||||
BINDING | 103 | 103 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786 | E | ||||||||
BINDING | 141 | 141 | /ligand="Fe(2+)" /ligand_id="ChEBI:CHEBI:29033 | H | ||||||||
BINDING | 141 | 141 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786 | H | ||||||||
SITE (Optional) | 96 | 96 | May play a role in metal incorporation in vivo | E | ||||||||
SITE (Optional) | 102 | 102 | May play a role in transmitting local conformational changes | D | ||||||||
SITE (Optional) | 105 | 105 | Important to generate the dianion | R |
Additional information
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Size range | 165-206 amino acids |
Related rules | None |
Fusion | None |