Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q03677 (MTND_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase

EC=1.13.11.54
Alternative name(s):
Acireductone dioxygenase (Fe(2+)-requiring)
Short name=ARD
Short name=Fe-ARD
Gene names
Name:ADI1
Ordered Locus Names:YMR009W
ORF Names:YM8270.12
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). Ref.5 Ref.7

Catalytic activity

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-(methylthio)-2-oxobutanoate + formate. Ref.5

Cofactor

Binds 1 iron ion per monomer. Can also use other divalent metal cations By similarity.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6. HAMAP-Rule MF_03154

Subcellular location

Cytoplasm. Nucleus Ref.4 Ref.5.

Induction

By heat shock. Ref.6

Sequence similarities

Belongs to the acireductone dioxygenase (ARD) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1791791,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase HAMAP-Rule MF_03154
PRO_0000162946

Sites

Metal binding851Iron or nickel By similarity
Metal binding871Iron or nickel By similarity
Metal binding911Iron or nickel By similarity
Metal binding1321Iron or nickel By similarity

Experimental info

Mutagenesis241E → A: No loss of acireductone dioxygenase activity. Ref.5
Mutagenesis451E → A: No loss of acireductone dioxygenase activity. Ref.5
Mutagenesis911E → A: Loss of acireductone dioxygenase activity. Ref.5
Mutagenesis1511E → A: No loss of acireductone dioxygenase activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q03677 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: E6629DC2E17E2109

FASTA17920,879
        10         20         30         40         50         60 
MVKVYIHDNK VDSDYRAPHN SGTELSLDEL AKLGVIYKYC ANEEEVNEIA RQREYKNRDV 

        70         80         90        100        110        120 
VNICEGSFKS EAEFNEKLAT FYQEHLHEDE EIRYCLEGAG YFDVRDASTP ENWIRCLVES 

       130        140        150        160        170 
GDLLILPPGI YHRFTLTTSN HIKALRLFKD EPKWQAINRS NQADSLPVRK DYIALINQY 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., 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.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., 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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"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."
Hirano W., Gotoh I., Uekita T., Seiki M.
Genes Cells 10:565-574(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-24; GLU-45; GLU-91 AND GLU-151.
[6]"Regulation and surveillance of normal and 3'-extended forms of the yeast aci-reductone dioxygenase mRNA by RNase III cleavage and exonucleolytic degradation."
Zer C., Chanfreau G.
J. Biol. Chem. 280:28997-29003(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"A complete inventory of all enzymes in the eukaryotic methionine salvage pathway."
Pirkov I., Norbeck J., Gustafsson L., Albers E.
FEBS J. 275:4111-4120(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z48613 Genomic DNA. Translation: CAA88525.1.
AY558584 Genomic DNA. Translation: AAS56910.1.
BK006946 Genomic DNA. Translation: DAA09907.1.
PIRS53039.
RefSeqNP_013722.1. NM_001182505.1.

3D structure databases

ProteinModelPortalQ03677.
SMRQ03677. Positions 1-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35178. 40 interactions.
DIPDIP-877N.
MINTMINT-565090.
STRING4932.YMR009W.

Proteomic databases

PaxDbQ03677.
PeptideAtlasQ03677.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR009W; YMR009W; YMR009W.
GeneID855021.
KEGGsce:YMR009W.

Organism-specific databases

CYGDYMR009w.
SGDS000004611. ADI1.

Phylogenomic databases

eggNOGCOG1791.
GeneTreeENSGT00390000008195.
HOGENOMHOG000201071.
KOK08967.
OMAGFFDVRE.
OrthoDBEOG7M0P3P.

Enzyme and pathway databases

BioCycYEAST:G3O-32717-MONOMER.
YEAST:MONOMER3O-186.
UniPathwayUPA00904; UER00878.

Gene expression databases

GenevestigatorQ03677.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
HAMAPMF_03154. Salvage_MtnD_euk.
InterProIPR004313. Acireductn_dOase_family.
IPR027496. MTCBP-1_eukaryotes.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERPTHR23418. PTHR23418. 1 hit.
PfamPF03079. ARD. 1 hit.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Other

NextBio978207.
PROQ03677.

Entry information

Entry nameMTND_YEAST
AccessionPrimary (citable) accession number: Q03677
Secondary accession number(s): D6VZI3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 19, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways