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Protein

Glutathione reductase

Gene

GLR1

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

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei472 – 4721Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi53 – 619FADBy similarity

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: SGD
  • cellular response to oxidative stress Source: SGD
  • glutathione metabolic process Source: SGD
  • protein glutathionylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciYEAST:YPL091W-MONOMER.
BRENDAi1.8.1.7. 984.
ReactomeiREACT_275578. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_310793. Detoxification of Reactive Oxygen Species.
REACT_362040. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:GLR1
Ordered Locus Names:YPL091W
ORF Names:LPG17W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XVI

Organism-specific databases

CYGDiYPL091w.
EuPathDBiFungiDB:YPL091W.
SGDiS000006012. GLR1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Glutathione reductasePRO_0000067972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Disulfide bondi61 ↔ 66Redox-activeBy similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP41921.
PaxDbiP41921.
PeptideAtlasiP41921.

2D gel databases

COMPLUYEAST-2DPAGEP41921.

Interactioni

Protein-protein interaction databases

BioGridi36090. 64 interactions.
DIPiDIP-4020N.
IntActiP41921. 3 interactions.
MINTiMINT-484403.
STRINGi4932.YPL091W.

Structurei

Secondary structure

1
483
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 297Combined sources
Helixi33 – 4412Combined sources
Beta strandi49 – 557Combined sources
Helixi59 – 646Combined sources
Helixi66 – 8217Combined sources
Turni83 – 897Combined sources
Helixi98 – 1003Combined sources
Helixi105 – 12925Combined sources
Beta strandi132 – 14110Combined sources
Beta strandi147 – 1548Combined sources
Beta strandi157 – 16610Combined sources
Beta strandi170 – 1723Combined sources
Helixi181 – 1833Combined sources
Helixi187 – 1926Combined sources
Beta strandi198 – 2036Combined sources
Helixi207 – 21812Combined sources
Beta strandi222 – 2265Combined sources
Beta strandi228 – 2325Combined sources
Helixi238 – 25114Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi261 – 2666Combined sources
Beta strandi273 – 2775Combined sources
Beta strandi282 – 29110Combined sources
Beta strandi295 – 2973Combined sources
Helixi303 – 3064Combined sources
Beta strandi329 – 3313Combined sources
Helixi333 – 3353Combined sources
Helixi342 – 35716Combined sources
Helixi360 – 3623Combined sources
Beta strandi374 – 3763Combined sources
Beta strandi382 – 3865Combined sources
Helixi389 – 3968Combined sources
Helixi398 – 4003Combined sources
Beta strandi401 – 4088Combined sources
Helixi411 – 4155Combined sources
Beta strandi422 – 4298Combined sources
Turni430 – 4334Combined sources
Beta strandi434 – 4429Combined sources
Helixi445 – 45713Combined sources
Helixi462 – 4665Combined sources
Helixi476 – 4805Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HQMX-ray2.40A/B17-483[»]
ProteinModelPortaliP41921.
SMRiP41921. Positions 22-483.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41921.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00390000007578.
HOGENOMiHOG000276712.
InParanoidiP41921.
KOiK00383.
OMAiHKEPTVY.
OrthoDBiEOG79W9F2.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41921-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSATKQTFR SLQIRTMSTN TKHYDYLVIG GGSGGVASAR RAASYGAKTL
60 70 80 90 100
LVEAKALGGT CVNVGCVPKK VMWYASDLAT RVSHANEYGL YQNLPLDKEH
110 120 130 140 150
LTFNWPEFKQ KRDAYVHRLN GIYQKNLEKE KVDVVFGWAR FNKDGNVEVQ
160 170 180 190 200
KRDNTTEVYS ANHILVATGG KAIFPENIPG FELGTDSDGF FRLEEQPKKV
210 220 230 240 250
VVVGAGYIGI ELAGVFHGLG SETHLVIRGE TVLRKFDECI QNTITDHYVK
260 270 280 290 300
EGINVHKLSK IVKVEKNVET DKLKIHMNDS KSIDDVDELI WTIGRKSHLG
310 320 330 340 350
MGSENVGIKL NSHDQIIADE YQNTNVPNIY SLGDVVGKVE LTPVAIAAGR
360 370 380 390 400
KLSNRLFGPE KFRNDKLDYE NVPSVIFSHP EAGSIGISEK EAIEKYGKEN
410 420 430 440 450
IKVYNSKFTA MYYAMLSEKS PTRYKIVCAG PNEKVVGLHI VGDSSAEILQ
460 470 480
GFGVAIKMGA TKADFDNCVA IHPTSAEELV TMR
Length:483
Mass (Da):53,441
Last modified:October 1, 1996 - v2
Checksum:i203BBB770120504A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti315 – 3151Q → E in BAA07109 (Ref. 4) Curated
Sequence conflicti428 – 4281C → G in BAA07109 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35342 Genomic DNA. Translation: AAA92575.1.
U43281 Genomic DNA. Translation: AAB68208.1.
D37871 mRNA. Translation: BAA07109.1.
BK006949 Genomic DNA. Translation: DAA11342.1.
PIRiS61975.
RefSeqiNP_015234.1. NM_001183905.1.

Genome annotation databases

EnsemblFungiiYPL091W; YPL091W; YPL091W.
GeneIDi856014.
KEGGisce:YPL091W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35342 Genomic DNA. Translation: AAA92575.1.
U43281 Genomic DNA. Translation: AAB68208.1.
D37871 mRNA. Translation: BAA07109.1.
BK006949 Genomic DNA. Translation: DAA11342.1.
PIRiS61975.
RefSeqiNP_015234.1. NM_001183905.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HQMX-ray2.40A/B17-483[»]
ProteinModelPortaliP41921.
SMRiP41921. Positions 22-483.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36090. 64 interactions.
DIPiDIP-4020N.
IntActiP41921. 3 interactions.
MINTiMINT-484403.
STRINGi4932.YPL091W.

Chemistry

BindingDBiP41921.
ChEMBLiCHEMBL4119.

2D gel databases

COMPLUYEAST-2DPAGEP41921.

Proteomic databases

MaxQBiP41921.
PaxDbiP41921.
PeptideAtlasiP41921.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL091W; YPL091W; YPL091W.
GeneIDi856014.
KEGGisce:YPL091W.

Organism-specific databases

CYGDiYPL091w.
EuPathDBiFungiDB:YPL091W.
SGDiS000006012. GLR1.

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00390000007578.
HOGENOMiHOG000276712.
InParanoidiP41921.
KOiK00383.
OMAiHKEPTVY.
OrthoDBiEOG79W9F2.

Enzyme and pathway databases

BioCyciYEAST:YPL091W-MONOMER.
BRENDAi1.8.1.7. 984.
ReactomeiREACT_275578. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_310793. Detoxification of Reactive Oxygen Species.
REACT_362040. TP53 Regulates Metabolic Genes.

Miscellaneous databases

EvolutionaryTraceiP41921.
NextBioi980908.
PROiP41921.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, characterization and overexpression of the yeast gene, GLR1, encoding glutathione reductase."
    Collinson L.P., Dawes I.W.
    Gene 156:123-127(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-483.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Aono M., Nakajima N.
    Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 20-483.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGSHR_YEAST
AccessioniPrimary (citable) accession number: P41921
Secondary accession number(s): D6W3S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.
Present with 7600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.