MTND_YEAST
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 03-AUG-2022, entry version 165.
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}; OrderedLocusNames=YMR009W;
GN 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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000255|HAMAP-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}.
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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; Q03677; -.
DR PRIDE; Q03677; -.
DR EnsemblFungi; YMR009W_mRNA; YMR009W; YMR009W.
DR GeneID; 855021; -.
DR KEGG; sce:YMR009W; -.
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; RGQEDEW; -.
DR BioCyc; YEAST:MON3O-186; -.
DR Reactome; R-SCE-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00878.
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: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; -; 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; PTHR23418; 1.
DR Pfam; PF03079; ARD; 1.
DR SUPFAM; SSF51182; SSF51182; 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
