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Protein

Free methionine-R-sulfoxide reductase

Gene

YKL069W

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

Functioni

Catalyzes the reversible oxidation-reduction of the R-enantiomer of free methionine sulfoxide to methionine. Does not act on S-enantiomer of free methionine sulfoxide or R-enantiomer of dabsylated methionine sulfoxide. Involved in protection against oxidative stress.1 Publication

Miscellaneous

Present with 2610 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

L-methionine + thioredoxin disulfide + H2O = L-methionine (R)-S-oxide + thioredoxin.1 Publication

Kineticsi

  1. KM=230 µM for free methionine-R-sulfoxide1 Publication
  1. Vmax=443 nmol/min/mg enzyme1 Publication

GO - Molecular functioni

GO - Biological processi

  • cellular response to oxidative stress Source: SGD

Keywordsi

Molecular functionOxidoreductase
Biological processStress response

Enzyme and pathway databases

BioCyciYEAST:G3O-31865-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Free methionine-R-sulfoxide reductase (EC:1.8.4.14)
Short name:
fRMsr
Alternative name(s):
GAF domain-containing protein YKL069W
Gene namesi
Ordered Locus Names:YKL069W
ORF Names:YKL340
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL069W
SGDiS000001552 YKL069W

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Single deletion of fRMsr has complete growth inhibition on methionine-R-sulfoxide medium and fRMsr and MXR1 double deletion completely blocks the growth on both methionine-R-sulfoxide and methionine-S-sulfoxide medium. FRMsr and MXR2 double deletion has no effect on growth on methionine-S-sulfoxide medium. Single mutant or any of the double mutants show no growth defects in methionine medium, even the fRMsr, MXR1 and MXR2 triple deletion mutant is viable and grows similarly to wild-type. Single deletion of fRMsr has an increased sensitivity to oxidative stress and a decreased life span of 18% compared to wild-type. FRMsr and MXR1, as well as fRMsr and MXR2 double mutants, and fRMsr, MXR1 and MXR2 triple mutant show 20% reduction in life span compared with wild-type cells.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi91C → S: Dramatic reduction in enzyme activity. 1 Publication1
Mutagenesisi101C → S: Dramatic reduction in enzyme activity. 1 Publication1
Mutagenesisi125C → S: Dramatic reduction in enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001715521 – 180Free methionine-R-sulfoxide reductaseAdd BLAST180

Proteomic databases

MaxQBiP36088
PaxDbiP36088
PRIDEiP36088

Interactioni

Protein-protein interaction databases

BioGridi34063, 330 interactors
DIPiDIP-4301N
IntActiP36088, 11 interactors
MINTiP36088
STRINGi4932.YKL069W

Structurei

Secondary structure

1180
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 13Combined sources5
Helixi21 – 36Combined sources16
Helixi42 – 59Combined sources18
Beta strandi64 – 72Combined sources9
Beta strandi74 – 77Combined sources4
Beta strandi79 – 88Combined sources10
Beta strandi92 – 95Combined sources4
Helixi99 – 107Combined sources9
Beta strandi111 – 114Combined sources4
Helixi116 – 118Combined sources3
Beta strandi131 – 138Combined sources8
Beta strandi144 – 154Combined sources11
Helixi160 – 176Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F5MX-ray1.90A/B1-180[»]
3KO6X-ray2.55A/B1-180[»]
ProteinModelPortaliP36088
SMRiP36088
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36088

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini99 – 177GAFAdd BLAST79

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000022909
InParanoidiP36088
KOiK08968
OMAiGICGQVA
OrthoDBiEOG092C4PVO

Family and domain databases

Gene3Di3.30.450.40, 1 hit
InterProiView protein in InterPro
IPR000614 FRMsr_CS
IPR003018 GAF
IPR029016 GAF-like_dom_sf
PfamiView protein in Pfam
PF13185 GAF_2, 1 hit
PROSITEiView protein in PROSITE
PS01320 UPF0067, 1 hit

Sequencei

Sequence statusi: Complete.

P36088-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSSTGFHHA DHVNYSSNLN KEEILEQLLL SYEGLSDGQV NWVCNLSNAS
60 70 80 90 100
SLIWHAYKSL AVDINWAGFY VTQASEENTL ILGPFQGKVA CQMIQFGKGV
110 120 130 140 150
CGTAASTKET QIVPDVNKYP GHIACDGETK SEIVVPIISN DGKTLGVIDI
160 170 180
DCLDYEGFDH VDKEFLEKLA KLINKSCVFK
Length:180
Mass (Da):19,734
Last modified:June 1, 1994 - v1
Checksum:i911158E8C0F2B0A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75780 Genomic DNA Translation: CAA53405.1
Z28069 Genomic DNA Translation: CAA81906.1
BK006944 Genomic DNA Translation: DAA09087.1
PIRiS37891
RefSeqiNP_012854.1, NM_001179635.1

Genome annotation databases

EnsemblFungiiYKL069W; YKL069W; YKL069W
GeneIDi853794
KEGGisce:YKL069W

Similar proteinsi

Entry informationi

Entry nameiFRMSR_YEAST
AccessioniPrimary (citable) accession number: P36088
Secondary accession number(s): D6VXL7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: March 28, 2018
This is version 143 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health