AC MF_03154; DC Protein; auto TR HAMAP; MF_03154; -; 1; level=0 XX Names: Salvage_MtnD_euk XX ID MTND case DE RecName: Full=Acireductone dioxygenase; DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring); DE Short=ARD'; DE Short=Fe-ARD; DE EC=1.13.11.54; DE AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring); DE Short=ARD; DE Short=Ni-ARD; DE EC=1.13.11.53; else DE RecName: Full=Probable inactive acireductone dioxygenase; end case case DE + AltName: Full=Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1; DE Short=MTCBP-1; end case case GN Name=ADI1; Synonyms=MTCBP1; else case or GN Name=ADI1; end case XX case and CC -!- FUNCTION: Catalyzes 2 different reactions between oxygen and the CC acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) CC depending upon the metal bound in the active site. Fe-containing CC acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4- CC methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine CC in the methionine recycle pathway. Ni-containing acireductone CC dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and CC formate, and does not lie on the methionine recycle pathway. Also down- CC regulates cell migration mediated by MMP14. else case and not CC -!- FUNCTION: Catalyzes 2 different reactions between oxygen and the CC acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) CC depending upon the metal bound in the active site. Fe-containing CC acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4- CC methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine CC in the methionine recycle pathway. Ni-containing acireductone CC dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and CC formate, and does not lie on the methionine recycle pathway. end case case CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4- CC methylsulfanyl-2-oxobutanoate + formate + 2 H(+); CC Xref=Rhea:RHEA:24504, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16723, ChEBI:CHEBI:49252; CC EC=1.13.11.54; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3- CC (methylsulfanyl)propanoate + CO + formate + 2 H(+); CC Xref=Rhea:RHEA:14161, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:17245, ChEBI:CHEBI:49016, CC ChEBI:CHEBI:49252; EC=1.13.11.53; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Note=Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes CC an acireductone dioxygenase reaction producing 2-keto-4- CC methylthiobutyrate, while nickel-binding promotes an acireductone CC dioxygenase reaction producing 3-(methylsulfanyl)propanoate.; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: CC step 5/6. end case case CC -!- SUBUNIT: Monomer. Interacts with MMP14. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Peripheral CC membrane protein; Cytoplasmic side. Note=Localizes to the plasma CC membrane when complexed to MMP14. else case and not CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Peripheral CC membrane protein; Cytoplasmic side. else CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. end case CC -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family. case not CC -!- FUNCTION: Probable inactive acireductone dioxygenase. CC -!- CAUTION: This enzyme lacks one or more conserved metal-binding sites. CC It may be non-functional. end case XX DR Pfam; PF03079; ARD; 1; trigger=no XX case KW Amino-acid biosynthesis KW Dioxygenase KW Methionine biosynthesis KW Oxidoreductase KW Metal-binding KW Iron KW Nickel end case case KW Cell membrane KW Membrane end case KW Cytoplasm KW Nucleus XX GO GO:0005737; C:cytoplasm GO GO:0005634; C:nucleus case GO GO:0005506; F:iron ion binding GO GO:0016151; F:nickel cation binding GO GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity GO GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity GO GO:0019509; P:L-methionine salvage from methylthioadenosine end case XX FT From: MTND_YEAST (Q03677) FT BINDING 85 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /ligand_note="for iron-dependent acireductone FT dioxygenase activity" FT Group: 1; Condition: H FT BINDING 85 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_note="for nickel-dependent acireductone FT dioxygenase activity" FT Group: 1; Condition: H FT BINDING 87 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /ligand_note="for iron-dependent acireductone FT dioxygenase activity" FT Group: 1; Condition: H FT BINDING 87 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_note="for nickel-dependent acireductone FT dioxygenase activity" FT Group: 1; Condition: H FT BINDING 91 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /ligand_note="for iron-dependent acireductone FT dioxygenase activity" FT Group: 1; Condition: E FT BINDING 91 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_note="for nickel-dependent acireductone FT dioxygenase activity" FT Group: 1; Condition: E FT BINDING 132 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /ligand_note="for iron-dependent acireductone FT dioxygenase activity" FT Group: 1; Condition: H FT BINDING 132 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_note="for nickel-dependent acireductone FT dioxygenase activity" FT Group: 1; Condition: H FT From: MTND_HUMAN (Q03677) case FT INIT_MET 1 FT /note="Removed" FT Condition: M end case XX Size: 146-344; Related: None; Template: Q99JT9; Q03677; Q9BV57; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in ARATH, CAEBR, CAEEL, COPC7, EMENI, ORYSI, ORYSJ, PHYPA, SORBI, VITVI, XENTR Plasmid: None Comments: None XX # Revision 1.13 2022/11/19 //