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Protein

Glutaredoxin-1

Gene

GRX1

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

Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX1 is less active as an oxidoreductase than GRX2.5 Publications

Kineticsi

  1. KM=0.88 mM for H2O22 Publications
  2. KM=0.52 mM for cumene hydroperoxide2 Publications
  3. KM=0.37 mM for tert-butyl hydroperoxide2 Publications
  4. KM=4.2 mM for 1-chloro-2,4-dinitrobenzene2 Publications
  5. KM=1.3 mM for 1,2-dichloro-4-nitrobenzene2 Publications
  6. KM=6.2 mM for reduced glutathione1 Publication
  1. Vmax=110 µmol/min/mg enzyme for H2O22 Publications
  2. Vmax=32.5 µmol/min/mg enzyme for cumene hydroperoxide2 Publications
  3. Vmax=7.5 µmol/min/mg enzyme for tert-butyl hydroperoxide2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631Glutathione2 Publications
Binding sitei75 – 751Glutathione; via amide nitrogen and carbonyl oxygen2 Publications

GO - Molecular functioni

  • disulfide oxidoreductase activity Source: SGD
  • electron carrier activity Source: InterPro
  • glutathione peroxidase activity Source: SGD
  • glutathione transferase activity Source: SGD
  • protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular oxidant detoxification Source: GOC
  • cellular response to oxidative stress Source: SGD
  • protein glutathionylation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

ReactomeiR-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP25373.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-1
Alternative name(s):
Glutathione-dependent oxidoreductase 1
Gene namesi
Name:GRX1
Ordered Locus Names:YCL035C
ORF Names:YCL35C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCL035C.
SGDiS000000540. GRX1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301C → S: Leads to increased oxidoreductase activity. 1 Publication
Mutagenesisi89 – 891D → S: Leads to increased oxidoreductase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 110110Glutaredoxin-1PRO_0000141613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 30Redox-active; alternate1 Publication
Modified residuei27 – 271S-glutathionyl cysteine; alternate2 Publications

Keywords - PTMi

Disulfide bond, Glutathionylation

Proteomic databases

MaxQBiP25373.
PeptideAtlasiP25373.

Expressioni

Inductioni

In response to heat shock and osmotic stress.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi30948. 37 interactions.
DIPiDIP-5646N.
IntActiP25373. 2 interactions.
MINTiMINT-556392.

Structurei

Secondary structure

1
110
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1613Combined sources
Beta strandi17 – 237Combined sources
Helixi28 – 3811Combined sources
Turni39 – 413Combined sources
Helixi45 – 473Combined sources
Beta strandi48 – 525Combined sources
Helixi53 – 553Combined sources
Helixi59 – 7012Combined sources
Beta strandi77 – 804Combined sources
Beta strandi83 – 875Combined sources
Helixi88 – 969Combined sources
Helixi99 – 10810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JACX-ray2.02A1-110[»]
2JADX-ray2.70A1-110[»]
3C1RX-ray2.00A1-110[»]
3C1SX-ray2.50A1-110[»]
ProteinModelPortaliP25373.
SMRiP25373. Positions 1-92.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25373.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 110104GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 296Glutathione binding2 Publications
Regioni88 – 892Glutathione binding2 Publications

Sequence similaritiesi

Belongs to the glutaredoxin family.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
InParanoidiP25373.
KOiK03676.
OMAiHTINSHK.
OrthoDBiEOG75F4SQ.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSQETIKHV KDLIAENEIF VASKTYCPYC HAALNTLFEK LKVPRSKVLV
60 70 80 90 100
LQLNDMKEGA DIQAALYEIN GQRTVPNIYI NGKHIGGNDD LQELRETGEL
110
EELLEPILAN
Length:110
Mass (Da):12,380
Last modified:May 1, 1992 - v1
Checksum:i8E69BC80BF40F2DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42381.1.
BK006937 Genomic DNA. Translation: DAA07449.1.
PIRiS19363.
RefSeqiNP_009895.1. NM_001178680.1.

Genome annotation databases

EnsemblFungiiCAA42381; CAA42381; CAA42381.
YCL035C; YCL035C; YCL035C.
GeneIDi850322.
KEGGisce:YCL035C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42381.1.
BK006937 Genomic DNA. Translation: DAA07449.1.
PIRiS19363.
RefSeqiNP_009895.1. NM_001178680.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JACX-ray2.02A1-110[»]
2JADX-ray2.70A1-110[»]
3C1RX-ray2.00A1-110[»]
3C1SX-ray2.50A1-110[»]
ProteinModelPortaliP25373.
SMRiP25373. Positions 1-92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30948. 37 interactions.
DIPiDIP-5646N.
IntActiP25373. 2 interactions.
MINTiMINT-556392.

Proteomic databases

MaxQBiP25373.
PeptideAtlasiP25373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42381; CAA42381; CAA42381.
YCL035C; YCL035C; YCL035C.
GeneIDi850322.
KEGGisce:YCL035C.

Organism-specific databases

EuPathDBiFungiDB:YCL035C.
SGDiS000000540. GRX1.

Phylogenomic databases

GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
InParanoidiP25373.
KOiK03676.
OMAiHTINSHK.
OrthoDBiEOG75F4SQ.

Enzyme and pathway databases

ReactomeiR-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP25373.

Miscellaneous databases

EvolutionaryTraceiP25373.
NextBioi965736.
PROiP25373.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [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. "The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species."
    Luikenhuis S., Perrone G., Dawes I.W., Grant C.M.
    Mol. Biol. Cell 9:1081-1091(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  4. "Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae."
    Grant C.M., Luikenhuis S., Beckhouse A., Soderbergh M., Dawes I.W.
    Biochim. Biophys. Acta 1490:33-42(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  6. "Role of yeast glutaredoxins as glutathione S-transferases."
    Collinson E.J., Grant C.M.
    J. Biol. Chem. 278:22492-22497(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae."
    Discola K.F., de Oliveira M.A., Rosa Cussiol J.R., Monteiro G., Barcena J.A., Porras P., Padilla C.A., Guimaraes B.G., Netto L.E.
    J. Mol. Biol. 385:889-901(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-30.
  9. "Structural basis for the different activities of yeast Grx1 and Grx2."
    Li W.F., Yu J., Ma X.X., Teng Y.B., Luo M., Tang Y.J., Zhou C.Z.
    Biochim. Biophys. Acta 1804:1542-1547(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-89.
  10. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structure of glutaredoxin Grx1p C30S mutant from yeast."
    Hakansson K.O., Winther J.R.
    Acta Crystallogr. D 63:288-294(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, MUTAGENESIS OF CYS-30.
  12. "Glutathionylation-triggered conformational changes of glutaredoxin Grx1 from the yeast Saccharomyces cerevisiae."
    Yu J., Zhang N.N., Yin P.D., Cui P.X., Zhou C.Z.
    Proteins 72:1077-1083(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, DISULFIDE BOND.

Entry informationi

Entry nameiGLRX1_YEAST
AccessioniPrimary (citable) accession number: P25373
Secondary accession number(s): D6VQY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 11, 2016
This is version 134 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 3030 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 III
    Yeast (Saccharomyces cerevisiae) chromosome III: 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.