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Q05926

- GLRX8_YEAST

UniProt

Q05926 - GLRX8_YEAST

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Protein

Glutaredoxin-8

Gene

GRX8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

  1. electron carrier activity Source: InterPro
  2. glutathione-disulfide reductase activity Source: SGD
  3. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
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
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR364w.
SGDiS000004356. GRX8.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251C → S: Impairs activity. 1 Publication
Mutagenesisi28 – 281C → S: Impairs activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 109109Glutaredoxin-8PRO_0000268192Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 28Redox-activeCurated

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ05926.
PaxDbiQ05926.
PeptideAtlasiQ05926.

Expressioni

Inductioni

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

Gene expression databases

GenevestigatoriQ05926.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi31626. 2 interactions.
IntActiQ05926. 1 interaction.
MINTiMINT-4496129.
STRINGi4932.YLR364W.

Structurei

Secondary structure

1
109
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410
Beta strandi17 – 215
Helixi28 – 3811
Turni41 – 433
Beta strandi44 – 485
Helixi54 – 6714
Beta strandi72 – 787
Beta strandi81 – 844
Helixi86 – 9510
Helixi98 – 1047

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M80NMR-A1-109[»]
ProteinModelPortaliQ05926.
SMRiQ05926. Positions 1-109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 109105GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0695.
InParanoidiQ05926.
OMAiRKWVPTI.
OrthoDBiEOG7JMGSQ.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U19103 Genomic DNA. Translation: AAB67570.1 .
AY558221 Genomic DNA. Translation: AAS56547.1 .
BK006945 Genomic DNA. Translation: DAA09669.1 .
PIRi S51382.
RefSeqi NP_013468.3. NM_001182253.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2M80 NMR - A 1-109 [» ]
ProteinModelPortali Q05926.
SMRi Q05926. Positions 1-109.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31626. 2 interactions.
IntActi Q05926. 1 interaction.
MINTi MINT-4496129.
STRINGi 4932.YLR364W.

Proteomic databases

MaxQBi Q05926.
PaxDbi Q05926.
PeptideAtlasi Q05926.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR364W ; YLR364W ; YLR364W .
GeneIDi 851079.
KEGGi sce:YLR364W.

Organism-specific databases

CYGDi YLR364w.
SGDi S000004356. GRX8.

Phylogenomic databases

eggNOGi COG0695.
InParanoidi Q05926.
OMAi RKWVPTI.
OrthoDBi EOG7JMGSQ.

Enzyme and pathway databases

BioCyci YEAST:G3O-32435-MONOMER.

Miscellaneous databases

NextBioi 967738.

Gene expression databases

Genevestigatori Q05926.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00462. Glutaredoxin. 1 hit.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Integrating phenotypic and expression profiles to map arsenic-response networks."
    Haugen A.C., Kelley R., Collins J.B., Tucker C.J., Deng C., Afshari C.A., Brown J.M., Ideker T., Van Houten B.
    Genome Biol. 5:R95.1-R95.18(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance."
    Mesecke N., Spang A., Deponte M., Herrmann J.M.
    Mol. Biol. Cell 19:2673-2680(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux."
    Eckers E., Bien M., Stroobant V., Herrmann J.M., Deponte M.
    Biochemistry 48:1410-1423(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-25 AND CYS-28.

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: October 29, 2014
This is version 98 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

External Data

Dasty 3