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HAMAP rule MF_03154

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General rule information [?]

Accession MF_03154
Dates 27-OCT-2011 (Created)
19-NOV-2022 (Last updated, Version 13)
Name Salvage_MtnD_euk
Scope(s) Eukaryota
Template(s) Q99JT9 (MTND_MOUSE); Q03677 (MTND_YEAST); Q9BV57 (MTND_HUMAN); [ Recover all ]
Triggered by HAMAP; MF_03154 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier MTND
case <FTGroup:1>
Protein name RecName: Full=Acireductone dioxygenase;
AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring);
                 Short=ARD';
                 Short=Fe-ARD;
                 EC=1.13.11.54;
AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring);
                 Short=ARD;
                 Short=Ni-ARD;
                 EC=1.13.11.53;
else
Protein name RecName: Full=Probable inactive acireductone dioxygenase;
end case
case <OC:Vertebrata>
Protein name + AltName: Full=Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1;
                 Short=MTCBP-1;
end case
case <OC:Vertebrata>
Gene name Name=ADI1; Synonyms=MTCBP1;
else case <OC:Fungi> or <OC:Dictyostelia>
Gene name Name=ADI1;
end case

Comments [?]

case <FTGroup:1> and <OC:Mammalia>
FUNCTIONCatalyzes 2 different reactions between oxygen 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. Also down- regulates cell migration mediated by MMP14.
else case <FTGroup:1> and not <OC:Mammalia>
FUNCTIONCatalyzes 2 different reactions between oxygen 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.
end case
case <FTGroup:1>
CATALYTIC ACTIVITY Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4- methylsulfanyl-2-oxobutanoate + formate + 2 H(+); Xref=Rhea:RHEA:24504, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:16723, ChEBI:CHEBI:49252; EC=1.13.11.54;
CATALYTIC ACTIVITY Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3- (methylsulfanyl)propanoate + CO + formate + 2 H(+); Xref=Rhea:RHEA:14161, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15740, ChEBI:CHEBI:17245, ChEBI:CHEBI:49016, ChEBI:CHEBI:49252; EC=1.13.11.53;
COFACTOR Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Note=Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4- methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.;
PATHWAYAmino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6.
end case
case <OC:Mammalia>
SUBUNITMonomer. Interacts with MMP14.
SUBCELLULAR LOCATIONCytoplasm. Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes to the plasma membrane when complexed to MMP14.
else case <OC:Vertebrata> and not <OC:Mammalia>
SUBUNITMonomer.
SUBCELLULAR LOCATIONCytoplasm. Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
else
SUBCELLULAR LOCATIONCytoplasm. Nucleus.
end case
SIMILARITYBelongs to the acireductone dioxygenase (ARD) family.
case not <FTGroup:1>
FUNCTIONProbable inactive acireductone dioxygenase.
CAUTIONThis enzyme lacks one or more conserved metal-binding sites. It may be non-functional.
end case

Keywords [?]


Gene Ontology [?]

GO:0005737; Cellular component:cytoplasm
GO:0005634; Cellular component:nucleus
case <FTGroup:1>
GO:0005506; Molecular function:iron ion binding
GO:0016151; Molecular function:nickel cation binding
GO:0010308; Molecular function:acireductone dioxygenase (Ni2+-requiring) activity
GO:0010309; Molecular function:acireductone dioxygenase [iron(II)-requiring] activity
GO:0019509; Biological process:L-methionine salvage from methylthioadenosine
end case

Cross-references [?]

Pfam PF03079; ARD; 1;

Features [?]

From: MTND_YEAST (Q03677)
Key From To Description Tag Condition FTGroup
BINDING 85 85 /ligand="Fe(2+)"
/ligand_id="ChEBI:CHEBI:29033"
/ligand_note="for iron-dependent acireductone dioxygenase activity"
H 1
BINDING 85 85 /ligand="Ni(2+)"
/ligand_id="ChEBI:CHEBI:49786"
/ligand_note="for nickel-dependent acireductone dioxygenase activity"
H 1
BINDING 87 87 /ligand="Fe(2+)"
/ligand_id="ChEBI:CHEBI:29033"
/ligand_note="for iron-dependent acireductone dioxygenase activity"
H 1
BINDING 87 87 /ligand="Ni(2+)"
/ligand_id="ChEBI:CHEBI:49786"
/ligand_note="for nickel-dependent acireductone dioxygenase activity"
H 1
BINDING 91 91 /ligand="Fe(2+)"
/ligand_id="ChEBI:CHEBI:29033"
/ligand_note="for iron-dependent acireductone dioxygenase activity"
E 1
BINDING 91 91 /ligand="Ni(2+)"
/ligand_id="ChEBI:CHEBI:49786"
/ligand_note="for nickel-dependent acireductone dioxygenase activity"
E 1
BINDING 132 132 /ligand="Fe(2+)"
/ligand_id="ChEBI:CHEBI:29033"
/ligand_note="for iron-dependent acireductone dioxygenase activity"
H 1
BINDING 132 132 /ligand="Ni(2+)"
/ligand_id="ChEBI:CHEBI:49786"
/ligand_note="for nickel-dependent acireductone dioxygenase activity"
H 1
From: MTND_HUMAN (Q03677)
Key From To Description Tag Condition FTGroup
case <OC:Mammalia>
INIT_MET 1 1 /note="Removed" M
end case

Additional information [?]

Size range 146-344 amino acids
Related rules None
Fusion Nter: None Cter: None



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