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Q43621

- GSHRC_PEA

UniProt

Q43621 - GSHRC_PEA

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Protein

Glutathione reductase, cytosolic

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Maintains high levels of reduced glutathione in the cytosol. May play a role in the restoration of the post-stress redox state of the cytosolic glutathione pool.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei233 – 2331NADPBy similarity
Binding sitei239 – 2391NADPBy similarity
Active sitei471 – 4711Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi63 – 7210FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. glutathione-disulfide reductase activity Source: UniProtKB-EC
  3. NADP binding Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase, cytosolic (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Alternative name(s):
GOR2
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Glutathione reductase, cytosolicPRO_0000067964Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi72 ↔ 77Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ43621.

Expressioni

Inductioni

Increased expression in the recovery (post-stress) phases of both drought and chilling.

Structurei

3D structure databases

ProteinModelPortaliQ43621.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

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.

Q43621-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARKMLNDGE PDLKKGEEQG KVYDFDLFII GAGSGGVRAA RFSSNFGAKV
60 70 80 90 100
GICELPFHPI SSETIGGVGG TCVIRGCVPK KILVYGASYG GELQDARNFG
110 120 130 140 150
WELNENVDFN WKKLLQKKTD EINRLNGIYK RLLSNAGVKL FEGEGKIASP
160 170 180 190 200
NEVEVTQLDG TKLSYSAKHI LIATGSRAQR PNIPGQELGI TSDEALSLEE
210 220 230 240 250
FPKRAVILGG GYIAVEFASI WRGMGSSVNL VFRKELPLRG FDDEMRAVVA
260 270 280 290 300
RNLEGRGINL HPRTNLAQLI KTEDGIKVIT DHGEELIADV VLFATGRSPN
310 320 330 340 350
SKRLNLEKVG VEFDKAGAIV VDEYSRTNIP SIWAVGDVTN RLNLTPVALM
360 370 380 390 400
EASLFAKTVF GGQASKPDYN DIPYAVFCIP PLSVVGLSEE QAVEQTKGDV
410 420 430 440 450
LIFTSTFNPM KNTISGRQEK TVMKLVVDAQ TDKVLGASMC GPDAPEIVQG
460 470 480 490
IAIAIKCGAT KAQFDSTVGI HPSSAEEFVT MRSETRRVTG GVKPKTNL
Length:498
Mass (Da):53,897
Last modified:November 1, 1997 - v1
Checksum:i19AD08959764C6D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98274 mRNA. Translation: CAA66924.1.
PIRiT06442.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98274 mRNA. Translation: CAA66924.1 .
PIRi T06442.

3D structure databases

ProteinModelPortali Q43621.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q43621.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Cloning and characterisation of a cytosolic glutathione reductase cDNA from pea (Pisum sativum L.) and its expression in response to stress."
    Stevens R.G., Greissen G.P., Mullineaux P.M.
    Plant Mol. Biol. 35:641-654(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Birte.
    Tissue: Leaf.

Entry informationi

Entry nameiGSHRC_PEA
AccessioniPrimary (citable) accession number: Q43621
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 91 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.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3