AC MF_01682; DC Protein; auto TR HAMAP; MF_01682; -; 1; level=0 XX Names: Salvage_MtnD XX ID MTND DE RecName: Full=Acireductone dioxygenase; DE AltName: Full=1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase; DE Short=DHK-MTPene 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; GN Name=mtnD; XX CC -!- FUNCTION: Catalyzes 2 different reactions between oxygene 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. 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 -!- 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 -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Note=Binds 1 Fe(2+) cation per monomer.; CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Note=Binds 1 nickel ion per monomer.; 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. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family. XX DR Pfam; PF03079; ARD; 1; trigger=no XX KW Amino-acid biosynthesis KW Dioxygenase KW Iron KW Metal-binding KW Methionine biosynthesis KW Nickel KW Oxidoreductase XX GO GO:0005506; F:iron ion binding GO GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity GO GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity GO GO:0016151; F:nickel cation binding GO GO:0019284; P:L-methionine salvage from S-adenosylmethionine XX FT From: MTND_KLEOX (Q9ZFE7) FT BINDING 97 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT Condition: H FT BINDING 97 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT Condition: H FT BINDING 99 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT Condition: H FT BINDING 99 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT Condition: H FT BINDING 103 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT Condition: E FT BINDING 103 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT Condition: E FT BINDING 141 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT Condition: H FT BINDING 141 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT Condition: H FT SITE 96 FT /note="May play a role in metal incorporation in vivo" FT Optional; Condition: E FT SITE 102 FT /note="May play a role in transmitting local conformational FT changes" FT Optional; Condition: D FT SITE 105 FT /note="Important to generate the dianion" FT Optional; Condition: R XX Size: 165-206; Related: None; Template: Q9ZFE7; O31669; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in PECAS, NOCFA, XANOP Plasmid: None Comments: None XX # Revision 1.20 2022/11/19 //