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Q43621 (GSHRC_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione reductase, cytosolic

Short name=GR
Short name=GRase
EC=1.8.1.7
Alternative name(s):
GOR2
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subcellular location

Cytoplasm.

Induction

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

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Glutathione reductase, cytosolic
PRO_0000067964

Regions

Nucleotide binding63 – 7210FAD By similarity

Sites

Active site4711Proton acceptor By similarity
Binding site2331NADP By similarity
Binding site2391NADP By similarity

Amino acid modifications

Disulfide bond72 ↔ 77Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q43621 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 19AD08959764C6D0

FASTA49853,897
        10         20         30         40         50         60 
MARKMLNDGE PDLKKGEEQG KVYDFDLFII GAGSGGVRAA RFSSNFGAKV GICELPFHPI 

        70         80         90        100        110        120 
SSETIGGVGG TCVIRGCVPK KILVYGASYG GELQDARNFG WELNENVDFN WKKLLQKKTD 

       130        140        150        160        170        180 
EINRLNGIYK RLLSNAGVKL FEGEGKIASP NEVEVTQLDG TKLSYSAKHI LIATGSRAQR 

       190        200        210        220        230        240 
PNIPGQELGI TSDEALSLEE FPKRAVILGG GYIAVEFASI WRGMGSSVNL VFRKELPLRG 

       250        260        270        280        290        300 
FDDEMRAVVA RNLEGRGINL HPRTNLAQLI KTEDGIKVIT DHGEELIADV VLFATGRSPN 

       310        320        330        340        350        360 
SKRLNLEKVG VEFDKAGAIV VDEYSRTNIP SIWAVGDVTN RLNLTPVALM EASLFAKTVF 

       370        380        390        400        410        420 
GGQASKPDYN DIPYAVFCIP PLSVVGLSEE QAVEQTKGDV LIFTSTFNPM KNTISGRQEK 

       430        440        450        460        470        480 
TVMKLVVDAQ TDKVLGASMC GPDAPEIVQG IAIAIKCGAT KAQFDSTVGI HPSSAEEFVT 

       490 
MRSETRRVTG GVKPKTNL 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98274 mRNA. Translation: CAA66924.1.
PIRT06442.

3D structure databases

ProteinModelPortalQ43621.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ43621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. 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]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. SSF55424. 1 hit.
TIGRFAMsTIGR01424. gluta_reduc_2. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHRC_PEA
AccessionPrimary (citable) accession number: Q43621
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 19, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families