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Protein

Glutaredoxin-2, mitochondrial

Gene

GRX2

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. GRX2 is more active as an oxidoreductase than GRX1.5 Publications

Kineticsi

  1. KM=2.0 mM for H2O22 Publications
  2. KM=2.2 mM for tert-butyl hydroperoxide2 Publications
  3. KM=0.87 mM for cumene hydroperoxide2 Publications
  4. KM=0.17 mM for 1-chloro-2,4-dinitrobenzene2 Publications
  5. KM=0.27 mM for 1,2-dichloro-4-nitrobenzene2 Publications
  6. KM=0.9 mM for reduced glutathione1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

    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
    • glutathione metabolic process Source: SGD
    Complete GO annotation...

    Keywords - Biological processi

    Electron transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:MONOMER3O-490.
    ReactomeiR-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
    SABIO-RKP17695.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaredoxin-2, mitochondrial
    Alternative name(s):
    Glutathione-dependent oxidoreductase 2
    Thioltransferase
    Gene namesi
    Name:GRX2
    Synonyms:TTR, TTR1
    Ordered Locus Names:YDR513W
    ORF Names:D9719.17
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome IV

    Organism-specific databases

    EuPathDBiFungiDB:YDR513W.
    SGDiS000002921. GRX2.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641C → S: Leads to 30 percent decreased oxidoreductase activity. 1 Publication
    Mutagenesisi123 – 1231S → D: Leads to decreased oxidoreductase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3535Mitochondrion1 PublicationAdd
    BLAST
    Chaini36 – 143108Glutaredoxin-2, mitochondrialPRO_0000141612Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei37 – 371PhosphoserineCombined sources
    Disulfide bondi61 ↔ 64Redox-active; alternate1 Publication
    Modified residuei61 – 611S-glutathionyl cysteine; alternate1 Publication
    Modified residuei91 – 911PhosphoserineCombined sources

    Keywords - PTMi

    Disulfide bond, Glutathionylation, Phosphoprotein

    Proteomic databases

    MaxQBiP17695.
    PeptideAtlasiP17695.
    PRIDEiP17695.
    TopDownProteomicsiP17695.

    PTM databases

    iPTMnetiP17695.

    Expressioni

    Inductioni

    In response to exposure to reactive oxygen species (ROS) and upon entry into stationary phase.2 Publications

    Interactioni

    Protein-protein interaction databases

    BioGridi32563. 40 interactions.
    DIPiDIP-5271N.
    IntActiP17695. 1 interaction.
    MINTiMINT-568234.

    Structurei

    Secondary structure

    1
    143
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 5013Combined sources
    Beta strandi51 – 577Combined sources
    Helixi62 – 7211Combined sources
    Helixi79 – 813Combined sources
    Beta strandi82 – 865Combined sources
    Helixi87 – 893Combined sources
    Helixi93 – 10412Combined sources
    Beta strandi111 – 1144Combined sources
    Beta strandi117 – 1215Combined sources
    Helixi122 – 1309Combined sources
    Helixi133 – 1375Combined sources
    Turni138 – 1414Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CTFX-ray2.10A35-143[»]
    3CTGX-ray1.50A35-143[»]
    3D4MX-ray2.05A35-143[»]
    3D5JX-ray1.91A/B35-143[»]
    ProteinModelPortaliP17695.
    SMRiP17695. Positions 36-143.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17695.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 143103GlutaredoxinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 636Glutathione binding1 Publication
    Regioni122 – 1232Glutathione binding1 Publication

    Sequence similaritiesi

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

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    GeneTreeiENSGT00390000003677.
    HOGENOMiHOG000095204.
    InParanoidiP17695.
    OMAiYCKATLS.
    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.

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

    P17695-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    METNFSFDSN LIVIIIITLF ATRIIAKRFL STPKMVSQET VAHVKDLIGQ
    60 70 80 90 100
    KEVFVAAKTY CPYCKATLST LFQELNVPKS KALVLELDEM SNGSEIQDAL
    110 120 130 140
    EEISGQKTVP NVYINGKHIG GNSDLETLKK NGKLAEILKP VFQ
    Length:143
    Mass (Da):15,861
    Last modified:February 21, 2006 - v3
    Checksum:i99A79B87695B2266
    GO

    Sequence cautioni

    The sequence AAB23389.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S45268 Genomic DNA. Translation: AAB23389.1. Different initiation.
    U33057 Genomic DNA. Translation: AAB64953.1.
    AY692896 Genomic DNA. Translation: AAT92915.1.
    BK006938 Genomic DNA. Translation: DAA12344.1.
    PIRiS69570. GDBY.
    RefSeqiNP_010801.1. NM_001180821.1.

    Genome annotation databases

    EnsemblFungiiYDR513W; YDR513W; YDR513W.
    GeneIDi852124.
    KEGGisce:YDR513W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S45268 Genomic DNA. Translation: AAB23389.1. Different initiation.
    U33057 Genomic DNA. Translation: AAB64953.1.
    AY692896 Genomic DNA. Translation: AAT92915.1.
    BK006938 Genomic DNA. Translation: DAA12344.1.
    PIRiS69570. GDBY.
    RefSeqiNP_010801.1. NM_001180821.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CTFX-ray2.10A35-143[»]
    3CTGX-ray1.50A35-143[»]
    3D4MX-ray2.05A35-143[»]
    3D5JX-ray1.91A/B35-143[»]
    ProteinModelPortaliP17695.
    SMRiP17695. Positions 36-143.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32563. 40 interactions.
    DIPiDIP-5271N.
    IntActiP17695. 1 interaction.
    MINTiMINT-568234.

    PTM databases

    iPTMnetiP17695.

    Proteomic databases

    MaxQBiP17695.
    PeptideAtlasiP17695.
    PRIDEiP17695.
    TopDownProteomicsiP17695.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDR513W; YDR513W; YDR513W.
    GeneIDi852124.
    KEGGisce:YDR513W.

    Organism-specific databases

    EuPathDBiFungiDB:YDR513W.
    SGDiS000002921. GRX2.

    Phylogenomic databases

    GeneTreeiENSGT00390000003677.
    HOGENOMiHOG000095204.
    InParanoidiP17695.
    OMAiYCKATLS.
    OrthoDBiEOG75F4SQ.

    Enzyme and pathway databases

    BioCyciYEAST:MONOMER3O-490.
    ReactomeiR-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
    SABIO-RKP17695.

    Miscellaneous databases

    EvolutionaryTraceiP17695.
    NextBioi970510.
    PROiP17695.

    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. "Cloning and sequencing of a gene encoding yeast thioltransferase."
      Gan Z.-R.
      Biochem. Biophys. Res. Commun. 187:949-955(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DMY6.
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Complete amino acid sequence of yeast thioltransferase (glutaredoxin)."
      Gan Z.-R., Polokoff M.A., Jacobs J.W., Sardana M.K.
      Biochem. Biophys. Res. Commun. 168:944-951(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 36-141.
    6. "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.
    7. "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.
    8. "Two isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in vivo and localize to different subcellular compartments."
      Pedrajas J.R., Porras P., Martinez-Galisteo E., Padilla C.A., Miranda-Vizuete A., Barcena J.A.
      Biochem. J. 364:617-623(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "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.
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 35-143 IN COMPLEX WITH GLUTATHIONE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-64.
    15. "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: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 35-143 IN COMPLEX WITH GLUTATHIONE, DISULFIDE BOND, MUTAGENESIS OF SER-123, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiGLRX2_YEAST
    AccessioniPrimary (citable) accession number: P17695
    Secondary accession number(s): D6VTD4, Q6B234
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: February 21, 2006
    Last modified: May 11, 2016
    This is version 151 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 31400 molecules/cell in log phase SD medium.1 Publication
    It is unclear whether the long polypeptide observed in mitochondria represents the immature form of the protein before cleavage of the transit peptide and release of the short form into the cytoplasm or whether two mature isoforms exists.

    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.