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Protein

Glutaredoxin-C5, chloroplastic

Gene

GRXC5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. Can assemble a [2Fe-2S] cluster, but cannot transfer it to an apoferredoxin.1 Publication

Kineticsi

kcat is 1.21 sec(-1) with glutathionylated beta-mercaptoethanol as substrate. kcat is 0.23 sec(-1) with dehydroascorbate as substrate. kcat is 0.69 sec(-1) with reduced glutathione as substrate.1 Publication

  1. KM=0.20 mM for glutathionylated beta-mercaptoethanol1 Publication
  2. KM=0.21 mM for dehydroascorbate1 Publication
  3. KM=3.6 mM for reduced glutathione1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei135 – 1351Glutathione; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei148 – 1481Glutathione; via amide nitrogen1 Publication
    Binding sitei149 – 1491Glutathione; via amide nitrogen1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • cell redox homeostasis Source: InterPro
    • cellular oxidant detoxification Source: GOC
    • iron-sulfur cluster assembly Source: TAIR
    Complete GO annotation...

    Keywords - Biological processi

    Electron transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaredoxin-C5, chloroplastic1 Publication
    Short name:
    AtGrxC51 Publication
    Gene namesi
    Name:GRXC51 Publication
    Ordered Locus Names:At4g28730Imported
    ORF Names:F16A16.160Imported
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G28730.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi90 – 901C → S: Loss of Fe-S cluster incorporation and loss of glutaredoxin activity. 1 Publication
    Mutagenesisi93 – 931C → S: Loss of Fe-S cluster incorporation, but increased glutaredoxin activity. 1 Publication
    Mutagenesisi141 – 1411C → S: No effect on Fe-S cluster incorporation or on glutaredoxin activity. 1 Publication
    Mutagenesisi148 – 1481C → S: No effect on Fe-S cluster incorporation or on glutaredoxin activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6363Chloroplast1 PublicationAdd
    BLAST
    Chaini64 – 174111Glutaredoxin-C5, chloroplasticPRO_0000268712Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi90 ↔ 93Redox-activeBy similarity
    Modified residuei90 – 901S-glutathionyl cysteine; partial1 Publication
    Modified residuei148 – 1481S-glutathionyl cysteine; partial1 Publication

    Post-translational modificationi

    Glutathionylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glutathionylation

    Proteomic databases

    PaxDbiQ8GWS0.
    PRIDEiQ8GWS0.

    Expressioni

    Inductioni

    Up-regulated by cold treatment.1 Publication

    Interactioni

    Subunit structurei

    Monomeric apoprotein and homodimeric holoprotein containing a [2Fe-2S] cluster (PubMed:21632542). No in vitro interactions with SUFE1, BOLA1, BOLA2 or BOLA4 (PubMed:24203231).2 Publications

    Protein-protein interaction databases

    BioGridi14281. 5 interactions.
    IntActiQ8GWS0. 2 interactions.
    STRINGi3702.AT4G28730.1.

    Structurei

    Secondary structure

    1
    174
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi68 – 7912Combined sources
    Beta strandi80 – 867Combined sources
    Helixi91 – 10212Combined sources
    Beta strandi108 – 1114Combined sources
    Helixi112 – 1143Combined sources
    Helixi118 – 13013Combined sources
    Beta strandi137 – 1404Combined sources
    Beta strandi143 – 1475Combined sources
    Helixi148 – 1569Combined sources
    Helixi159 – 1646Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RHBX-ray1.20A64-174[»]
    3RHCX-ray2.40A/B64-174[»]
    ProteinModelPortaliQ8GWS0.
    SMRiQ8GWS0. Positions 67-166.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8GWS0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini93 – 17179GlutaredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiKOG1752. Eukaryota.
    COG0695. LUCA.
    HOGENOMiHOG000095204.
    InParanoidiQ8GWS0.
    OMAiSCSVRAM.
    PhylomeDBiQ8GWS0.

    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.

    Q8GWS0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAVTAFNTLK LVSSSLDPIP SVSCSSYSFS LIYVGSPYKR CLKQSCSVRA
    60 70 80 90 100
    MTSSSSAASS SSSSFGSRME ESIRKTVTEN TVVIYSKTWC SYCTEVKTLF
    110 120 130 140 150
    KRLGVQPLVV ELDQLGPQGP QLQKVLERLT GQHTVPNVFV CGKHIGGCTD
    160 170
    TVKLNRKGDL ELMLAEANGK NGQS
    Length:174
    Mass (Da):18,814
    Last modified:March 1, 2003 - v1
    Checksum:iD7912FC4FBB01743
    GO

    Sequence cautioni

    The sequence CAA22979.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence CAB81461.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL035353 Genomic DNA. Translation: CAA22979.1. Sequence problems.
    AL161573 Genomic DNA. Translation: CAB81461.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE85535.1.
    AK118672 mRNA. Translation: BAC43267.1.
    BT003703 mRNA. Translation: AAO39931.1.
    PIRiT04526.
    RefSeqiNP_194602.2. NM_119017.4.
    UniGeneiAt.31993.

    Genome annotation databases

    EnsemblPlantsiAT4G28730.1; AT4G28730.1; AT4G28730.
    GeneIDi828994.
    GrameneiAT4G28730.1; AT4G28730.1; AT4G28730.
    KEGGiath:AT4G28730.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL035353 Genomic DNA. Translation: CAA22979.1. Sequence problems.
    AL161573 Genomic DNA. Translation: CAB81461.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE85535.1.
    AK118672 mRNA. Translation: BAC43267.1.
    BT003703 mRNA. Translation: AAO39931.1.
    PIRiT04526.
    RefSeqiNP_194602.2. NM_119017.4.
    UniGeneiAt.31993.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RHBX-ray1.20A64-174[»]
    3RHCX-ray2.40A/B64-174[»]
    ProteinModelPortaliQ8GWS0.
    SMRiQ8GWS0. Positions 67-166.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi14281. 5 interactions.
    IntActiQ8GWS0. 2 interactions.
    STRINGi3702.AT4G28730.1.

    Proteomic databases

    PaxDbiQ8GWS0.
    PRIDEiQ8GWS0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G28730.1; AT4G28730.1; AT4G28730.
    GeneIDi828994.
    GrameneiAT4G28730.1; AT4G28730.1; AT4G28730.
    KEGGiath:AT4G28730.

    Organism-specific databases

    TAIRiAT4G28730.

    Phylogenomic databases

    eggNOGiKOG1752. Eukaryota.
    COG0695. LUCA.
    HOGENOMiHOG000095204.
    InParanoidiQ8GWS0.
    OMAiSCSVRAM.
    PhylomeDBiQ8GWS0.

    Miscellaneous databases

    EvolutionaryTraceiQ8GWS0.
    PROiQ8GWS0.

    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. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Plant glutaredoxins: still mysterious reducing systems."
      Rouhier N., Gelhaye E., Jacquot J.-P.
      Cell. Mol. Life Sci. 61:1266-1277(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    6. "Genome-wide analysis of plant glutaredoxin systems."
      Rouhier N., Couturier J., Jacquot J.-P.
      J. Exp. Bot. 57:1685-1696(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY.
    7. "Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis thaliana BolA2 and SufE1."
      Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D., Gualberto J.M., Jacquot J.P., Gaymard F., Vignols F., Rouhier N.
      Mol. Plant 7:187-205(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4.
    8. "Arabidopsis chloroplastic glutaredoxin C5 as a model to explore molecular determinants for iron-sulfur cluster binding into glutaredoxins."
      Couturier J., Stroher E., Albetel A.N., Roret T., Muthuramalingam M., Tarrago L., Seidel T., Tsan P., Jacquot J.P., Johnson M.K., Dietz K.J., Didierjean C., Rouhier N.
      J. Biol. Chem. 286:27515-27527(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 64-174 OF APO- AND HOLOFORMS IN COMPLEX WITH GLUTATHIONE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION BY COLD, SUBUNIT, MUTAGENESIS OF CYS-90; CYS-93; CYS-141 AND CYS-148, GLUTATHIONYLATION AT CYS-90 AND CYS-148.

    Entry informationi

    Entry nameiGRXC5_ARATH
    AccessioniPrimary (citable) accession number: Q8GWS0
    Secondary accession number(s): Q9SVU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: March 1, 2003
    Last modified: February 17, 2016
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    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.