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Protein

Methylthioribose-1-phosphate isomerase

Gene

MRI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).UniRule annotation2 Publications

Catalytic activityi

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

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (MRI1)
  2. Methylthioribulose-1-phosphate dehydratase (MDE1)
  3. Enolase-phosphatase E1 (UTR4)
  4. Enolase-phosphatase E1 (UTR4)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (ADI1)
  6. Aromatic amino acid aminotransferase 2 (ARO9), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1), Aromatic/aminoadipate aminotransferase 1 (ARO8)
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei181 – 1811Transition state stabilizerUniRule annotation
Active sitei280 – 2801Proton donorUniRule annotation

GO - Molecular functioni

  • S-methyl-5-thioribose-1-phosphate isomerase activity Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Enzyme and pathway databases

BioCyciYEAST:G3O-34257-MONOMER.
ReactomeiR-SCE-1237112. Methionine salvage pathway.
UniPathwayiUPA00904; UER00874.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylthioribose-1-phosphate isomeraseUniRule annotation (EC:5.3.1.23UniRule annotation)
Short name:
M1PiUniRule annotation
Short name:
MTR-1-P isomeraseUniRule annotation
Alternative name(s):
S-methyl-5-thioribose-1-phosphate isomeraseUniRule annotation
Translation initiation factor eIF-2B subunit alpha/beta/delta-like proteinUniRule annotation
Gene namesi
Name:MRI1UniRule annotation
Ordered Locus Names:YPR118W
ORF Names:P9642.7
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR118W.
SGDiS000006322. MRI1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 411410Methylthioribose-1-phosphate isomerasePRO_0000156110Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei351 – 3511PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ06489.
PeptideAtlasiQ06489.

PTM databases

iPTMnetiQ06489.

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi36285. 25 interactions.
DIPiDIP-4685N.
IntActiQ06489. 1 interaction.
MINTiMINT-505844.

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Beta strandi17 – 215Combined sources
Turni23 – 286Combined sources
Beta strandi32 – 343Combined sources
Helixi38 – 469Combined sources
Helixi53 – 7321Combined sources
Helixi79 – 824Combined sources
Helixi88 – 10316Combined sources
Helixi111 – 12414Combined sources
Helixi129 – 16840Combined sources
Beta strandi173 – 1797Combined sources
Helixi185 – 1873Combined sources
Beta strandi188 – 1914Combined sources
Helixi194 – 21017Combined sources
Beta strandi223 – 2308Combined sources
Turni233 – 2364Combined sources
Helixi237 – 2404Combined sources
Helixi242 – 2498Combined sources
Beta strandi253 – 2564Combined sources
Helixi258 – 2603Combined sources
Helixi261 – 2677Combined sources
Beta strandi272 – 2776Combined sources
Beta strandi280 – 2823Combined sources
Beta strandi288 – 2914Combined sources
Helixi294 – 30411Combined sources
Beta strandi307 – 3115Combined sources
Helixi314 – 3163Combined sources
Helixi324 – 3263Combined sources
Helixi335 – 3384Combined sources
Beta strandi339 – 3457Combined sources
Turni347 – 3493Combined sources
Beta strandi362 – 3665Combined sources
Beta strandi377 – 3826Combined sources
Helixi384 – 3863Combined sources
Beta strandi388 – 3925Combined sources
Beta strandi395 – 3973Combined sources
Helixi408 – 4103Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W2WX-ray1.75A/E/I/M1-211[»]
B/F/J/N221-411[»]
ProteinModelPortaliQ06489.
SMRiQ06489. Positions 1-211, 221-411.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06489.

Family & Domainsi

Sequence similaritiesi

Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000013732.
HOGENOMiHOG000224730.
InParanoidiQ06489.
KOiK08963.
OMAiAIPGGDH.
OrthoDBiEOG76QFST.

Family and domain databases

Gene3Di1.20.120.420. 1 hit.
HAMAPiMF_01678. Salvage_MtnA.
InterProiIPR000649. IF-2B-related.
IPR005251. IF-M1Pi.
IPR011559. Initiation_fac_2B_a/b/d.
IPR027363. M1Pi_N.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00524. eIF-2B_rel. 1 hit.
TIGR00512. salvage_mtnA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q06489-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLEAIVFDR SEPENVSVKV LDQLLLPYTT KYVPIHTIDD GYSVIKSMQV
60 70 80 90 100
RGAPAIAIVG SLSVLTEVQL IKHNPTSDVA TLYSLVNWES TKTVLNKRLD
110 120 130 140 150
FLLSSRPTAV NLSNSLVEIK NILKSSSDLK AFDGSLYNYV CELIDEDLAN
160 170 180 190 200
NMKMGDNGAK YLIDVLQKDG FKDEFAVLTI CNTGSLATSG YGTALGVIRS
210 220 230 240 250
LWKDSLAKTD KADSGLDNEK CPRMGHVFPL ETRPYNQGSR LTAYELVYDK
260 270 280 290 300
IPSTLITDSS IAYRIRTSPI PIKAAFVGAD RIVRNGDTAN KIGTLQLAVI
310 320 330 340 350
CKQFGIKFFV VAPKTTIDNV TETGDDIIVE ERNPEEFKVV TGTVINPENG
360 370 380 390 400
SLILNESGEP ITGKVGIAPL EINVWNPAFD ITPHELIDGI ITEEGVFTKN
410
SSGEFQLESL F
Length:411
Mass (Da):45,020
Last modified:November 1, 1996 - v1
Checksum:i369B2114E12E11D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40828 Genomic DNA. Translation: AAB68059.1.
BK006949 Genomic DNA. Translation: DAA11533.1.
PIRiS69011.
RefSeqiNP_015443.1. NM_001184215.1.

Genome annotation databases

EnsemblFungiiYPR118W; YPR118W; YPR118W.
GeneIDi856234.
KEGGisce:YPR118W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40828 Genomic DNA. Translation: AAB68059.1.
BK006949 Genomic DNA. Translation: DAA11533.1.
PIRiS69011.
RefSeqiNP_015443.1. NM_001184215.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W2WX-ray1.75A/E/I/M1-211[»]
B/F/J/N221-411[»]
ProteinModelPortaliQ06489.
SMRiQ06489. Positions 1-211, 221-411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36285. 25 interactions.
DIPiDIP-4685N.
IntActiQ06489. 1 interaction.
MINTiMINT-505844.

PTM databases

iPTMnetiQ06489.

Proteomic databases

MaxQBiQ06489.
PeptideAtlasiQ06489.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR118W; YPR118W; YPR118W.
GeneIDi856234.
KEGGisce:YPR118W.

Organism-specific databases

EuPathDBiFungiDB:YPR118W.
SGDiS000006322. MRI1.

Phylogenomic databases

GeneTreeiENSGT00390000013732.
HOGENOMiHOG000224730.
InParanoidiQ06489.
KOiK08963.
OMAiAIPGGDH.
OrthoDBiEOG76QFST.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00874.
BioCyciYEAST:G3O-34257-MONOMER.
ReactomeiR-SCE-1237112. Methionine salvage pathway.

Miscellaneous databases

EvolutionaryTraceiQ06489.
PROiQ06489.

Family and domain databases

Gene3Di1.20.120.420. 1 hit.
HAMAPiMF_01678. Salvage_MtnA.
InterProiIPR000649. IF-2B-related.
IPR005251. IF-M1Pi.
IPR011559. Initiation_fac_2B_a/b/d.
IPR027363. M1Pi_N.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00524. eIF-2B_rel. 1 hit.
TIGR00512. salvage_mtnA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "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.
  6. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), SUBUNIT, FUNCTION.

Entry informationi

Entry nameiMTNA_YEAST
AccessioniPrimary (citable) accession number: Q06489
Secondary accession number(s): D6W4B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 922 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.