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P42770

- GSHRP_ARATH

UniProt

P42770 - GSHRP_ARATH

Protein

Glutathione reductase, chloroplastic

Gene

EMB2360

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Maintains high levels of reduced glutathione in the chloroplast.

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei291 – 2911NADPBy similarity
    Binding sitei297 – 2971NADPBy similarity
    Active sitei529 – 5291Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi126 – 13510FADBy similarity

    GO - Molecular functioni

    1. ATP binding Source: TAIR
    2. copper ion binding Source: TAIR
    3. flavin adenine dinucleotide binding Source: InterPro
    4. glutathione-disulfide reductase activity Source: UniProtKB-EC
    5. NADP binding Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. glutathione metabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciRETL1328306-WGS:GSTH-2390-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione reductase, chloroplastic (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Alternative name(s):
    Protein EMBRYO DEFECTIVE 2360
    Gene namesi
    Name:EMB2360
    Ordered Locus Names:At3g54660
    ORF Names:T5N23_20
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G54660.

    Subcellular locationi

    Plastidchloroplast Curated

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast stroma Source: TAIR
    3. mitochondrion Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7474ChloroplastSequence AnalysisAdd
    BLAST
    Chaini75 – 565491Glutathione reductase, chloroplasticPRO_0000030280Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi135 ↔ 140Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP42770.
    PRIDEiP42770.

    Expressioni

    Gene expression databases

    GenevestigatoriP42770.

    Interactioni

    Protein-protein interaction databases

    IntActiP42770. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP42770.
    SMRiP42770. Positions 86-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiCOG1249.
    HOGENOMiHOG000276712.
    InParanoidiP42770.
    KOiK00383.
    OMAiLAKTLFQ.
    PhylomeDBiP42770.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006324. Glut-diS_reduct.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR01424. gluta_reduc_2. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P42770-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASTPKLTST ISSSSPSLQF LCKKLPIAIH LPSSSSSSFL SLPKTLTSLY    50
    SLRPRIALLS NHRYYHSRRF SVCASTDNGA ESDRHYDFDL FTIGAGSGGV 100
    RASRFATSFG ASAAVCELPF STISSDTAGG VGGTCVLRGC VPKKLLVYAS 150
    KYSHEFEDSH GFGWKYETEP SHDWTTLIAN KNAELQRLTG IYKNILSKAN 200
    VKLIEGRGKV IDPHTVDVDG KIYTTRNILI AVGGRPFIPD IPGKEFAIDS 250
    DAALDLPSKP KKIAIVGGGY IALEFAGIFN GLNCEVHVFI RQKKVLRGFD 300
    EDVRDFVGEQ MSLRGIEFHT EESPEAIIKA GDGSFSLKTS KGTVEGFSHV 350
    MFATGRKPNT KNLGLENVGV KMAKNGAIEV DEYSQTSVPS IWAVGDVTDR 400
    INLTPVALME GGALAKTLFQ NEPTKPDYRA VPCAVFSQPP IGTVGLTEEQ 450
    AIEQYGDVDV YTSNFRPLKA TLSGLPDRVF MKLIVCANTN KVLGVHMCGE 500
    DSPEIIQGFG VAVKAGLTKA DFDATVGVHP TAAEEFVTMR APTRKFRKDS 550
    SEGKASPEAK TAAGV 565
    Length:565
    Mass (Da):60,852
    Last modified:November 1, 1995 - v1
    Checksum:i29C2CD0E68ED4E4A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14049 mRNA. Translation: BAA03137.1.
    D89620 Genomic DNA. Translation: BAA19653.1.
    AL138650 Genomic DNA. Translation: CAB77586.1.
    CP002686 Genomic DNA. Translation: AEE79262.1.
    PIRiT47625.
    RefSeqiNP_191026.1. NM_115323.3.
    UniGeneiAt.21776.

    Genome annotation databases

    EnsemblPlantsiAT3G54660.1; AT3G54660.1; AT3G54660.
    GeneIDi824631.
    KEGGiath:AT3G54660.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14049 mRNA. Translation: BAA03137.1 .
    D89620 Genomic DNA. Translation: BAA19653.1 .
    AL138650 Genomic DNA. Translation: CAB77586.1 .
    CP002686 Genomic DNA. Translation: AEE79262.1 .
    PIRi T47625.
    RefSeqi NP_191026.1. NM_115323.3.
    UniGenei At.21776.

    3D structure databases

    ProteinModelPortali P42770.
    SMRi P42770. Positions 86-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P42770. 1 interaction.

    Proteomic databases

    PaxDbi P42770.
    PRIDEi P42770.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G54660.1 ; AT3G54660.1 ; AT3G54660 .
    GeneIDi 824631.
    KEGGi ath:AT3G54660.

    Organism-specific databases

    GeneFarmi 2285. 251.
    TAIRi AT3G54660.

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276712.
    InParanoidi P42770.
    KOi K00383.
    OMAi LAKTLFQ.
    PhylomeDBi P42770.

    Enzyme and pathway databases

    BioCyci RETL1328306-WGS:GSTH-2390-MONOMER.

    Miscellaneous databases

    PROi P42770.

    Gene expression databases

    Genevestigatori P42770.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006324. Glut-diS_reduct.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    TIGRFAMsi TIGR01424. gluta_reduc_2. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and properties of glutathione reductase from Arabidopsis thaliana."
      Kubo A., Sano T., Saji H., Tanaka K., Kondo N., Tanaka K.
      Plant Cell Physiol. 34:1259-1266(1993)
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: cv. Columbia.
    2. Kubo A.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiGSHRP_ARATH
    AccessioniPrimary (citable) accession number: P42770
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3