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Reviewed, UniProtKB/Swiss-Prot Q06489 (MTNA_YEAST)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Methylthioribose-1-phosphate isomerase
      Short name=MTR-1-P isomerase
      Short name=M1Pi
    EC=5.3.1.23
Alternative name(s):
    S-methyl-5-thioribose-1-phosphate isomerase
Gene names
Name: MRI1
Ordered Locus Names: YPR118W
ORF Names: P9642.7
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). Ref.4

Catalytic activity

S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate.

Pathway

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

Subunit structure

Homodimer. Ref.4

Miscellaneous

Present with 922 molecules/cell in log phase SD medium. Ref.2

Sequence similarities

Belongs to the EIF-2B alpha/beta/delta subunits family. MtnA subfamily.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

SVF1Q055151EBI-29371,EBI-38400

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411Methylthioribose-1-phosphate isomerase
PRO_0000156110

Amino acid modifications

Modified residue3511Phosphoserine Ref.3

Secondary structure

1 ....................................................................... 411
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q06489-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 369B2114E12E11D8

FASTA41145,020
        10         20         30         40         50         60 
MSLEAIVFDR SEPENVSVKV LDQLLLPYTT KYVPIHTIDD GYSVIKSMQV RGAPAIAIVG 

        70         80         90        100        110        120 
SLSVLTEVQL IKHNPTSDVA TLYSLVNWES TKTVLNKRLD FLLSSRPTAV NLSNSLVEIK 

       130        140        150        160        170        180 
NILKSSSDLK AFDGSLYNYV CELIDEDLAN NMKMGDNGAK YLIDVLQKDG FKDEFAVLTI 

       190        200        210        220        230        240 
CNTGSLATSG YGTALGVIRS LWKDSLAKTD KADSGLDNEK CPRMGHVFPL ETRPYNQGSR 

       250        260        270        280        290        300 
LTAYELVYDK IPSTLITDSS IAYRIRTSPI PIKAAFVGAD RIVRNGDTAN KIGTLQLAVI 

       310        320        330        340        350        360 
CKQFGIKFFV VAPKTTIDNV TETGDDIIVE ERNPEEFKVV TGTVINPENG SLILNESGEP 

       370        380        390        400        410 
ITGKVGIAPL EINVWNPAFD ITPHELIDGI ITEEGVFTKN SSGEFQLESL F

« Hide

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References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[3]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, MASS SPECTROMETRY.
[4]"Crystal structure of yeast Ypr118w, a methylthioribose-1-phosphate isomerase related to regulatory eIF2B subunits."
Bumann M., Djafarzadeh S., Oberholzer A.E., Bigler P., Altmann M., Trachsel H., Baumann U.
J. Biol. Chem. 279:37087-37094(2004) [PubMed: 15215245] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), SUBUNIT, FUNCTION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U40828 Genomic DNA. Translation: AAB68059.1.
PIRS69011.
RefSeqNP_015443.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1W2WX-ray1.75A/E/I/M1-211[»]
B/F/J/N221-411[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:4685N.
IntActQ06489. 3 interactions.

Proteomic databases

PeptideAtlasQ06489.

Genome annotation databases

EnsemblYPR118W. Saccharomyces cerevisiae. [Contig view]
GeneID856234.
GenomeReviewsGene locus YPR118W in contig U00094_GR.
KEGGsce:YPR118W.
NMPDRfig|4932.3.peg.6580.

Organism-specific databases

CYGDYPR118w.
SGDS000006322. MRI1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMQ06489.
OMAQ06489. GDNILTI.

Enzyme and pathway databases

BRENDA5.3.1.23. 250.

Gene expression databases

GermOnlineYPR118W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000649. IF-2B_related.
IPR005251. IF-2BI_MTNA.
IPR011559. Initiation_fac_2B_a/b/d.
[Graphical view]
PANTHERPTHR10233. IF-2B_related. 1 hit.
PfamPF01008. IF-2B. 1 hit.
[Graphical view]
TIGRFAMsTIGR00524. eIF-2B_rel. 1 hit.
TIGR00512. salvage_mtnA. 1 hit.
ProtoNetSearch...

Other Resources

NextBio981488.

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Entry information

Entry nameMTNA_YEAST
AccessionPrimary (citable) accession number: Q06489
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents