1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (Q03677)

Identification
Name1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase
Synonyms
  • Acireductone dioxygenase
  • ARD
Gene NameADI1
Enzyme ClassNot Available
Biological Properties
General FunctionInvolved in metal ion binding
Specific FunctionCatalyzes the formation of formate and 2-keto-4- methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5- methylthiopentene (DHK-MTPene)
Cellular LocationCell membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus
SMPDB Pathways
Methionine metabolism and salvagePW002384 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG PathwaysNot Available
SMPDB Reactions
1,2-Dihydroxy-3-keto-5-methylthiopentene + oxygen → 4-Methylthio-2-oxobutanoate + hydron + Formic acid
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB001851,2-Dihydroxy-3-keto-5-methylthiopenteneShow
YMDB00385Formic acidShow
YMDB004214-Methylthio-2-oxobutanoateShow
YMDB00862hydronShow
YMDB00900oxygenShow
GO Classification
Function
metal ion binding
catalytic activity
oxidoreductase activity
dioxygenase activity
binding
ion binding
cation binding
Process
oxidation reduction
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular amino acid biosynthetic process
amino acid salvage
L-methionine salvage from methylthioadenosine
metabolic process
Gene Properties
Chromosome LocationNot Available
Locus
Gene Sequence>540 bp ATGGTTAAGGTATATATTCATGACAACAAGGTTGACTCCGATTATCGCGCACCCCACAAT TCTGGAACAGAACTTTCCCTGGATGAATTAGCCAAGTTAGGAGTGATTTATAAATACTGT GCAAATGAGGAAGAAGTGAATGAAATTGCTAGGCAAAGAGAATATAAAAATAGAGATGTG GTCAACATCTGCGAAGGTTCCTTCAAAAGTGAAGCAGAGTTTAATGAAAAACTAGCAACA TTCTACCAAGAGCATTTACATGAAGACGAAGAAATAAGATACTGTCTCGAGGGTGCTGGA TACTTTGACGTCAGGGATGCTTCCACACCAGAGAACTGGATTAGGTGTTTGGTAGAGTCA GGTGATTTACTGATTCTTCCACCAGGCATCTATCATCGTTTCACCTTGACAACTAGCAAC CACATCAAGGCCTTGAGACTGTTTAAGGACGAGCCCAAATGGCAAGCTATCAACAGGTCA AATCAGGCTGATTCATTGCCTGTACGCAAGGACTACATTGCCCTGATCAATCAGTACTAA
Protein Properties
Pfam Domain Function
Protein Residues179
Protein Molecular Weight20879.19922
Protein Theoretical pI4.98
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase MVKVYIHDNKVDSDYRAPHNSGTELSLDELAKLGVIYKYCANEEEVNEIARQREYKNRDV VNICEGSFKSEAEFNEKLATFYQEHLHEDEEIRYCLEGAGYFDVRDASTPENWIRCLVES GDLLILPPGIYHRFTLTTSNHIKALRLFKDEPKWQAINRSNQADSLPVRKDYIALINQY
References
External Links
ResourceLink
Saccharomyces Genome Database ADI1
Uniprot IDQ03677
Uniprot NameMTND_YEAST
GenBank Gene IDAY558584
Genebank Protein ID45271058
General Reference
  • Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Hirano, W., Gotoh, I., Uekita, T., Seiki, M. (2005). "Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the methionine salvage pathway." Genes Cells 10:565-574.15938715
  • Zer, C., Chanfreau, G. (2005). "Regulation and surveillance of normal and 3'-extended forms of the yeast aci-reductone dioxygenase mRNA by RNase III cleavage and exonucleolytic degradation." J Biol Chem 280:28997-29003.15967792