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Protein

Monothiol glutaredoxin-3

Gene

GRX3

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

Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable).By similarityCurated1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi176 – 1761Iron-sulfur (2Fe-2S); shared with dimeric partnerBy similarity

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: SGD
  • cell redox homeostasis Source: InterPro
  • cellular iron ion homeostasis Source: SGD
  • cellular response to oxidative stress Source: SGD
  • negative regulation of transcription regulatory region DNA binding Source: SGD
Complete GO annotation...

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciYEAST:G3O-29701-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Monothiol glutaredoxin-3
Gene namesi
Name:GRX3
Ordered Locus Names:YDR098C
ORF Names:YD8557.05C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR098C.
SGDiS000002505. GRX3.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Monothiol glutaredoxin-3PRO_0000102249Add
BLAST

Interactioni

Subunit structurei

Homodimer. Heterodimer with FRA2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AFT1P221494EBI-22178,EBI-2332

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi32153. 33 interactions.
DIPiDIP-1350N.
IntActiQ03835. 9 interactions.
MINTiMINT-402040.

Structurei

Secondary structure

1
250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Helixi9 – 168Combined sources
Turni17 – 226Combined sources
Beta strandi25 – 306Combined sources
Helixi37 – 4913Combined sources
Helixi51 – 533Combined sources
Beta strandi56 – 627Combined sources
Turni63 – 653Combined sources
Helixi67 – 726Combined sources
Beta strandi77 – 859Combined sources
Beta strandi88 – 936Combined sources
Helixi98 – 11215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D6IX-ray1.50A/B2-113[»]
ProteinModelPortaliQ03835.
SMRiQ03835. Positions 2-113, 150-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03835.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 110110ThioredoxinPROSITE-ProRule annotationAdd
BLAST
Domaini151 – 250100GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 glutaredoxin domain.PROSITE-ProRule annotation
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00550000075030.
HOGENOMiHOG000165751.
InParanoidiQ03835.
OMAiMIFMKGD.
OrthoDBiEOG7WMCX0.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10293. PTHR10293. 1 hit.
PfamiPF00462. Glutaredoxin. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 2 hits.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03835-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVIEINDQE QFTYLTTTAA GDKLIVLYFH TSWAEPCKAL KQVFEAISNE
60 70 80 90 100
PSNSNVSFLS IDADENSEIS ELFEISAVPY FIIIHKGTIL KELSGADPKE
110 120 130 140 150
YVSLLEDCKN SVNSGSSQTH TMENANVNEG SHNDEDDDDE EEEEETEEQI
160 170 180 190 200
NARLTKLVNA APVMLFMKGS PSEPKCGFSR QLVGILREHQ VRFGFFDILR
210 220 230 240 250
DESVRQNLKK FSEWPTFPQL YINGEFQGGL DIIKESLEED PDFLQHALQS
Length:250
Mass (Da):28,261
Last modified:October 14, 2015 - v2
Checksum:i8CC1A04EC1E7DAB3
GO

Sequence cautioni

The sequence CAA87672.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47746 Genomic DNA. Translation: CAA87672.1. Different initiation.
BK006938 Genomic DNA. Translation: DAA11943.2.
PIRiS51247.
RefSeqiNP_010383.4. NM_001180406.4.

Genome annotation databases

EnsemblFungiiYDR098C; YDR098C; YDR098C.
GeneIDi851672.
KEGGisce:YDR098C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47746 Genomic DNA. Translation: CAA87672.1. Different initiation.
BK006938 Genomic DNA. Translation: DAA11943.2.
PIRiS51247.
RefSeqiNP_010383.4. NM_001180406.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D6IX-ray1.50A/B2-113[»]
ProteinModelPortaliQ03835.
SMRiQ03835. Positions 2-113, 150-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32153. 33 interactions.
DIPiDIP-1350N.
IntActiQ03835. 9 interactions.
MINTiMINT-402040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR098C; YDR098C; YDR098C.
GeneIDi851672.
KEGGisce:YDR098C.

Organism-specific databases

EuPathDBiFungiDB:YDR098C.
SGDiS000002505. GRX3.

Phylogenomic databases

GeneTreeiENSGT00550000075030.
HOGENOMiHOG000165751.
InParanoidiQ03835.
OMAiMIFMKGD.
OrthoDBiEOG7WMCX0.

Enzyme and pathway databases

BioCyciYEAST:G3O-29701-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ03835.
PROiQ03835.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10293. PTHR10293. 1 hit.
PfamiPF00462. Glutaredoxin. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 2 hits.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
PS51352. THIOREDOXIN_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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  4. "Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis."
    Kumanovics A., Chen O.S., Li L., Bagley D., Adkins E.M., Lin H., Dingra N.N., Outten C.E., Keller G., Winge D., Ward D.M., Kaplan J.
    J. Biol. Chem. 283:10276-10286(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FRA2.
  5. "The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation."
    Li H., Mapolelo D.T., Dingra N.N., Naik S.G., Lees N.S., Hoffman B.M., Riggs-Gelasco P.J., Huynh B.H., Johnson M.K., Outten C.E.
    Biochemistry 48:9569-9581(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FRA2, IDENTIFICATION OF PROBABLE INITIATION SITE.
  6. "Structure of the thioredoxin-like domain of yeast glutaredoxin 3."
    Gibson L.M., Dingra N.N., Outten C.E., Lebioda L.
    Acta Crystallogr. D 64:927-932(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-113.

Entry informationi

Entry nameiGLRX3_YEAST
AccessioniPrimary (citable) accession number: Q03835
Secondary accession number(s): D6VS83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 14, 2015
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 11000 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 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.