ID MTND_YEAST Reviewed; 179 AA. AC Q03677; D6VZI3; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 171. DE RecName: Full=Acireductone dioxygenase {ECO:0000255|HAMAP-Rule:MF_03154}; DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_03154}; DE Short=ARD' {ECO:0000255|HAMAP-Rule:MF_03154}; DE Short=Fe-ARD {ECO:0000255|HAMAP-Rule:MF_03154}; DE EC=1.13.11.54 {ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|PubMed:15938715}; DE AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_03154}; DE Short=ARD {ECO:0000255|HAMAP-Rule:MF_03154}; DE Short=Ni-ARD {ECO:0000255|HAMAP-Rule:MF_03154}; DE EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_03154}; GN Name=ADI1 {ECO:0000255|HAMAP-Rule:MF_03154}; GN OrderedLocusNames=YMR009W; ORFNames=YM8270.12; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [4] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PATHWAY, AND RP MUTAGENESIS OF GLU-24; GLU-45; GLU-91 AND GLU-151. RX PubMed=15938715; DOI=10.1111/j.1365-2443.2005.00859.x; RA Hirano W., Gotoh I., Uekita T., Seiki M.; RT "Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein- RT 1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the RT methionine salvage pathway."; RL Genes Cells 10:565-574(2005). RN [6] RP INDUCTION. RX PubMed=15967792; DOI=10.1074/jbc.m505913200; RA Zer C., Chanfreau G.; RT "Regulation and surveillance of normal and 3'-extended forms of the yeast RT aci-reductone dioxygenase mRNA by RNase III cleavage and exonucleolytic RT degradation."; RL J. Biol. Chem. 280:28997-29003(2005). RN [7] RP FUNCTION, AND PATHWAY. RX PubMed=18625006; DOI=10.1111/j.1742-4658.2008.06552.x; RA Pirkov I., Norbeck J., Gustafsson L., Albers E.; RT "A complete inventory of all enzymes in the eukaryotic methionine salvage RT pathway."; RL FEBS J. 275:4111-4120(2008). 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 (By similarity). Fe- CC containing acireductone dioxygenase (Fe-ARD) produces formate and 2- CC keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of CC methionine in the methionine recycle pathway (PubMed:15938715, CC PubMed:18625006). Ni-containing acireductone dioxygenase (Ni-ARD) CC produces methylthiopropionate, carbon monoxide and formate, and does CC not lie on the methionine recycle pathway (By similarity). CC {ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|PubMed:15938715, CC ECO:0000269|PubMed:18625006}. 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; Evidence={ECO:0000255|HAMAP-Rule:MF_03154, CC ECO:0000269|PubMed:15938715}; 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03154}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03154}; CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03154}; 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 {ECO:0000255|HAMAP-Rule:MF_03154}; 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. {ECO:0000255|HAMAP-Rule:MF_03154, CC ECO:0000269|PubMed:15938715, ECO:0000269|PubMed:18625006}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:15967792}. CC -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family. CC {ECO:0000255|HAMAP-Rule:MF_03154}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z48613; CAA88525.1; -; Genomic_DNA. DR EMBL; AY558584; AAS56910.1; -; Genomic_DNA. DR EMBL; BK006946; DAA09907.1; -; Genomic_DNA. DR PIR; S53039; S53039. DR RefSeq; NP_013722.1; NM_001182505.1. DR AlphaFoldDB; Q03677; -. DR SMR; Q03677; -. DR BioGRID; 35178; 98. DR DIP; DIP-877N; -. DR IntAct; Q03677; 1. DR STRING; 4932.YMR009W; -. DR MaxQB; Q03677; -. DR PaxDb; 4932-YMR009W; -. DR PeptideAtlas; Q03677; -. DR EnsemblFungi; YMR009W_mRNA; YMR009W; YMR009W. DR GeneID; 855021; -. DR KEGG; sce:YMR009W; -. DR AGR; SGD:S000004611; -. DR SGD; S000004611; ADI1. DR VEuPathDB; FungiDB:YMR009W; -. DR eggNOG; KOG2107; Eukaryota. DR GeneTree; ENSGT00390000008195; -. DR HOGENOM; CLU_090154_1_0_1; -. DR InParanoid; Q03677; -. DR OMA; MVRAWYM; -. DR OrthoDB; 130851at2759; -. DR BioCyc; YEAST:MONOMER3O-186; -. DR Reactome; R-SCE-1237112; Methionine salvage pathway. DR UniPathway; UPA00904; UER00878. DR BioGRID-ORCS; 855021; 0 hits in 10 CRISPR screens. DR PRO; PR:Q03677; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q03677; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity; IMP:SGD. DR GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule. DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IMP:SGD. DR GO; GO:0006555; P:methionine metabolic process; IBA:GO_Central. DR CDD; cd02232; cupin_ARD; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR HAMAP; MF_03154; Salvage_MtnD_euk; 1. DR InterPro; IPR004313; ARD. DR InterPro; IPR027496; ARD_euk. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR PANTHER; PTHR23418; ACIREDUCTONE DIOXYGENASE; 1. DR PANTHER; PTHR23418:SF0; ACIREDUCTONE DIOXYGENASE; 1. DR Pfam; PF03079; ARD; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Cytoplasm; Dioxygenase; Iron; Metal-binding; KW Methionine biosynthesis; Nickel; Nucleus; Oxidoreductase; KW Reference proteome. FT CHAIN 1..179 FT /note="Acireductone dioxygenase" FT /id="PRO_0000162946" FT BINDING 85 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /ligand_note="for iron-dependent acireductone dioxygenase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154" FT BINDING 85 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_note="for nickel-dependent acireductone dioxygenase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154" FT BINDING 87 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /ligand_note="for iron-dependent acireductone dioxygenase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154" FT BINDING 87 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_note="for nickel-dependent acireductone dioxygenase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154" FT BINDING 91 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /ligand_note="for iron-dependent acireductone dioxygenase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154" FT BINDING 91 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_note="for nickel-dependent acireductone dioxygenase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154" FT BINDING 132 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /ligand_note="for iron-dependent acireductone dioxygenase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154" FT BINDING 132 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_note="for nickel-dependent acireductone dioxygenase FT activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154" FT MUTAGEN 24 FT /note="E->A: No loss of acireductone dioxygenase activity." FT /evidence="ECO:0000269|PubMed:15938715" FT MUTAGEN 45 FT /note="E->A: No loss of acireductone dioxygenase activity." FT /evidence="ECO:0000269|PubMed:15938715" FT MUTAGEN 91 FT /note="E->A: Loss of acireductone dioxygenase activity." FT /evidence="ECO:0000269|PubMed:15938715" FT MUTAGEN 151 FT /note="E->A: No loss of acireductone dioxygenase activity." FT /evidence="ECO:0000269|PubMed:15938715" SQ SEQUENCE 179 AA; 20879 MW; E6629DC2E17E2109 CRC64; MVKVYIHDNK VDSDYRAPHN SGTELSLDEL AKLGVIYKYC ANEEEVNEIA RQREYKNRDV VNICEGSFKS EAEFNEKLAT FYQEHLHEDE EIRYCLEGAG YFDVRDASTP ENWIRCLVES GDLLILPPGI YHRFTLTTSN HIKALRLFKD EPKWQAINRS NQADSLPVRK DYIALINQY //