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Protein

Monothiol glutaredoxin-6

Gene

GRX6

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi136 – 1361Iron-sulfur (2Fe-2S); shared with dimeric partnerSequence analysis

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: SGD
  • electron carrier activity Source: InterPro
  • glutathione-disulfide reductase activity Source: SGD
  • iron ion binding Source: SGD
  • protein disulfide oxidoreductase activity Source: InterPro
  • protein homodimerization activity Source: SGD

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular response to oxidative stress Source: SGD
Complete GO annotation...

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29441-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Monothiol glutaredoxin-6
Gene namesi
Name:GRX6
Ordered Locus Names:YDL010W
ORF Names:D2890
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL010W.
SGDiS000002168. GRX6.

Subcellular locationi

GO - Cellular componenti

  • cis-Golgi network Source: SGD
  • endoplasmic reticulum membrane Source: SGD
  • fungal-type vacuole Source: SGD
  • Golgi apparatus Source: SGD
  • Golgi lumen Source: SGD
  • integral component of membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence analysisAdd
BLAST
Chaini30 – 231202Monothiol glutaredoxin-6PRO_0000042988Add
BLAST

Proteomic databases

MaxQBiQ12438.

PTM databases

iPTMnetiQ12438.

Interactioni

GO - Molecular functioni

  • protein homodimerization activity Source: SGD

Protein-protein interaction databases

BioGridi32043. 15 interactions.
MINTiMINT-4478768.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi115 – 1239Combined sources
Beta strandi127 – 1326Combined sources
Helixi137 – 14913Combined sources
Beta strandi150 – 1545Combined sources
Beta strandi157 – 1604Combined sources
Helixi161 – 1633Combined sources
Helixi167 – 17812Combined sources
Beta strandi185 – 1884Combined sources
Helixi196 – 2049Combined sources
Helixi208 – 2147Combined sources
Beta strandi221 – 2244Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4NX-ray1.50A113-231[»]
ProteinModelPortaliQ12438.
SMRiQ12438. Positions 113-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12438.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 219104GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00550000075735.
HOGENOMiHOG000208731.
InParanoidiQ12438.
OMAiLENEYQF.
OrthoDBiEOG75F4SQ.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. 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.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12438-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPSNKRNAR ILSITTLLLL LVFFVAQNAN FLTVEIKEET SKAFSTNMDN
60 70 80 90 100
MAGGSSREYA AMPTSTTNKG SSEVDEEINE IKQKVGLQQP IASVDDSLSA
110 120 130 140 150
IKNDKGSRIT KAFNVQKEYS LILDLSPIII FSKSTCSYSK GMKELLENEY
160 170 180 190 200
QFIPNYYIIE LDKHGHGEEL QEYIKLVTGR GTVPNLLVNG VSRGGNEEIK
210 220 230
KLHTQGKLLE SLQVWSDGKF SVEQREKPSN N
Length:231
Mass (Da):25,783
Last modified:November 1, 1996 - v1
Checksum:iC76DD4E2A6E16744
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48432 Genomic DNA. Translation: CAA88349.1.
Z74059 Genomic DNA. Translation: CAA98567.1.
BK006938 Genomic DNA. Translation: DAA11838.1.
PIRiS52509.
RefSeqiNP_010274.1. NM_001180069.1.

Genome annotation databases

EnsemblFungiiYDL010W; YDL010W; YDL010W.
GeneIDi851551.
KEGGisce:YDL010W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48432 Genomic DNA. Translation: CAA88349.1.
Z74059 Genomic DNA. Translation: CAA98567.1.
BK006938 Genomic DNA. Translation: DAA11838.1.
PIRiS52509.
RefSeqiNP_010274.1. NM_001180069.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4NX-ray1.50A113-231[»]
ProteinModelPortaliQ12438.
SMRiQ12438. Positions 113-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32043. 15 interactions.
MINTiMINT-4478768.

PTM databases

iPTMnetiQ12438.

Proteomic databases

MaxQBiQ12438.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL010W; YDL010W; YDL010W.
GeneIDi851551.
KEGGisce:YDL010W.

Organism-specific databases

EuPathDBiFungiDB:YDL010W.
SGDiS000002168. GRX6.

Phylogenomic databases

GeneTreeiENSGT00550000075735.
HOGENOMiHOG000208731.
InParanoidiQ12438.
OMAiLENEYQF.
OrthoDBiEOG75F4SQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29441-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12438.
PROiQ12438.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. 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.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(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. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 70-82; 85-102; 144-175; 181-193 AND 208-219, IDENTIFICATION BY MASS SPECTROMETRY.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLRX6_YEAST
AccessioniPrimary (citable) accession number: Q12438
Secondary accession number(s): D6VRX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 117 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 1643 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.