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Protein

Glutaredoxin-8

Gene

GRX8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Glutathione-dependent oxidoreductase with lower activity compared to the other members of the glutaredoxin family. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32435-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-8
Alternative name(s):
Glutathione-dependent oxidoreductase 8
Gene namesi
Name:GRX8
Ordered Locus Names:YLR364W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR364W.
SGDiS000004356. GRX8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi25C → S: Impairs activity. 1 Publication1
Mutagenesisi28C → S: Impairs activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002681921 – 109Glutaredoxin-8Add BLAST109

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi25 ↔ 28Redox-activeCurated

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ05926.
PRIDEiQ05926.

Expressioni

Inductioni

Strongly induced by the exposure to arsenic which causes glutathione depletion.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi31626. 3 interactors.
IntActiQ05926. 1 interactor.
MINTiMINT-4496129.

Structurei

Secondary structure

1109
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 14Combined sources10
Beta strandi17 – 21Combined sources5
Helixi28 – 38Combined sources11
Turni41 – 43Combined sources3
Beta strandi44 – 48Combined sources5
Helixi54 – 67Combined sources14
Beta strandi72 – 78Combined sources7
Beta strandi81 – 84Combined sources4
Helixi86 – 95Combined sources10
Helixi98 – 104Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M80NMR-A1-109[»]
ProteinModelPortaliQ05926.
SMRiQ05926.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 109GlutaredoxinPROSITE-ProRule annotationAdd BLAST105

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

InParanoidiQ05926.
OMAiRKWVPTI.
OrthoDBiEOG092C5IZN.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05926-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAFVTKAEE MIKSHPYFQL SASWCPDCVY ANSIWNKLNV QDKVFVFDIG
60 70 80 90 100
SLPRNEQEKW RIAFQKVVGS RNLPTIVVNG KFWGTESQLH RFEAKGTLEE

ELTKIGLLP
Length:109
Mass (Da):12,519
Last modified:November 1, 1996 - v1
Checksum:i3353EFB47A61574A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19103 Genomic DNA. Translation: AAB67570.1.
AY558221 Genomic DNA. Translation: AAS56547.1.
BK006945 Genomic DNA. Translation: DAA09669.1.
PIRiS51382.
RefSeqiNP_013468.3. NM_001182253.3.

Genome annotation databases

EnsemblFungiiYLR364W; YLR364W; YLR364W.
GeneIDi851079.
KEGGisce:YLR364W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19103 Genomic DNA. Translation: AAB67570.1.
AY558221 Genomic DNA. Translation: AAS56547.1.
BK006945 Genomic DNA. Translation: DAA09669.1.
PIRiS51382.
RefSeqiNP_013468.3. NM_001182253.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M80NMR-A1-109[»]
ProteinModelPortaliQ05926.
SMRiQ05926.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31626. 3 interactors.
IntActiQ05926. 1 interactor.
MINTiMINT-4496129.

Proteomic databases

MaxQBiQ05926.
PRIDEiQ05926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR364W; YLR364W; YLR364W.
GeneIDi851079.
KEGGisce:YLR364W.

Organism-specific databases

EuPathDBiFungiDB:YLR364W.
SGDiS000004356. GRX8.

Phylogenomic databases

InParanoidiQ05926.
OMAiRKWVPTI.
OrthoDBiEOG092C5IZN.

Enzyme and pathway databases

BioCyciYEAST:G3O-32435-MONOMER.

Miscellaneous databases

PROiQ05926.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLRX8_YEAST
AccessioniPrimary (citable) accession number: Q05926
Secondary accession number(s): D6VZ03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 111 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 573 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.