Q03677 (MTND_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	179 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-methionine salvage from methylthioadenosine Inferred from mutant phenotype Ref.5Ref.7. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.4. Source: SGD nucleus Inferred from direct assay Ref.4. Source: SGD
Molecular_function	acireductone dioxygenase (Ni2+-requiring) activity Inferred from mutant phenotype Ref.5. Source: SGD acireductone dioxygenase [iron(II)-requiring] activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 179	179	1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase HAMAP-Rule MF_03154		PRO_0000162946
Sites
	Metal binding	85	1	Iron or nickel By similarity
	Metal binding	87	1	Iron or nickel By similarity
	Metal binding	91	1	Iron or nickel By similarity
	Metal binding	132	1	Iron or nickel By similarity
Experimental info
	Mutagenesis	24	1	E → A: No loss of acireductone dioxygenase activity. Ref.5
	Mutagenesis	45	1	E → A: No loss of acireductone dioxygenase activity. Ref.5
	Mutagenesis	91	1	E → A: Loss of acireductone dioxygenase activity. Ref.5
	Mutagenesis	151	1	E → A: No loss of acireductone dioxygenase activity. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q03677 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: E6629DC2E17E2109	FASTA	179	20,879
	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

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[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. , 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.
PIR	S53039.
RefSeq	NP_013722.1. NM_001182505.1.
3D structure databases
ProteinModelPortal	Q03677.
SMR	Q03677. Positions 1-176.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-877N.
MINT	MINT-565090.
STRING	4932.YMR009W.
Proteomic databases
PaxDb	Q03677.
PeptideAtlas	Q03677.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR009W; YMR009W; YMR009W.
GeneID	855021.
KEGG	sce:YMR009W.
Organism-specific databases
CYGD	YMR009w.
SGD	S000004611. ADI1.
Phylogenomic databases
eggNOG	COG1791.
GeneTree	ENSGT00390000008195.
HOGENOM	HOG000201071.
KO	K08967.
OMA	KWTPLNR.
OrthoDB	EOG498Z95.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32717-MONOMER. YEAST:MONOMER3O-186.
UniPathway	UPA00904; UER00878.
Gene expression databases
Genevestigator	Q03677.
GermOnline	YMR009W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.60.120.10. 1 hit.
HAMAP	MF_03154. Salvage_MtnD_euk.
InterPro	IPR004313. Acireductn_dOase_family. IPR027496. MTCBP-1_eukaryotes. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
PANTHER	PTHR23418. PTHR23418. 1 hit.
Pfam	PF03079. ARD. 1 hit. [Graphical view]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
ProtoNet	Search...
Other
NextBio	978207.

Entry information

Entry name

MTND_YEAST

Accession

Primary (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:	May 29, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program