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Reviewed, UniProtKB/Swiss-Prot O04955 (GSHRC_BRARP)

Last modified September 22, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutathione reductase, cytosolic
      Short name=GRase
      Short name=GR
    EC=1.8.1.7
Gene names
Name: GR1
OrganismBrassica rapa subsp. pekinensis (Chinese cabbage)
Taxonomic identifier51351 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeBrassica

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Maintains high levels of reduced glutathione in the cytosol By similarity.

Catalytic activity

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subcellular location

Cytoplasm Potential.

Induction

By paraquat and ozone. Ref.1

Miscellaneous

The active site is a redox-active disulfide bond By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Glutathione reductase, cytosolic
PRO_0000067962

Regions

Nucleotide binding67 – 7610FAD By similarity

Sites

Active site4751Proton acceptor By similarity
Binding site2371NADP By similarity
Binding site2431NADP By similarity

Amino acid modifications

Disulfide bond76 ↔ 81Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O04955-1 [UniParc].

Last modified October 1, 2000. Version 2.
Checksum: 397D978EE114B6BE

FASTA50254,059
        10         20         30         40         50         60 
MARKMLSDGE LNKAAAAGEE ATTETHYDFD LFVIGAGSGG VRAARFSANN GAKVGICELP 

        70         80         90        100        110        120 
FHPISSEEIG GVGGTCVIRG CVPKKILVYG ATYGGELEDA RNYGWEINGN VDFNWKKLLQ 

       130        140        150        160        170        180 
KKTDEILRLN NIYKRLLANA AVKLYEGEGR IVGPNEVEVR QIDGTKISYT AKHILIATGS 

       190        200        210        220        230        240 
RAQKPNIPGH ELAITSDEAL SLEEFPKRAI VLGGGYIAVE FASIWRGMGA TVDLFFRKEL 

       250        260        270        280        290        300 
PLRGFDDEMR ALVARNLEGR GINLHPQTSL AELIKTDDGI KVISSHGEEF VADVVLFATG 

       310        320        330        340        350        360 
RIPNTKRLNL EAVGVELDQA GAVKVDEYSR TNIPSIWAVG DATNRINLTP VALMEATCFA 

       370        380        390        400        410        420 
NTVFGGKPAK ADYTNVACAV FCIPPLAVVG LSEEEAVEKA TGDILVFTSG FNPMKNTISG 

       430        440        450        460        470        480 
RQEKSLMKLI VDEKTDKVIG ASMCGPDAAE IMQGIAIALK CGATKAQFDS TVGIHPSSAE 

       490        500 
EFVTMRTVTR RIAYKAKPQT SL 

« Hide

References

[1]"Molecular cloning and characterization of the gene encoding glutathione reductase in Brassica campestris."
Lee H.S., Jo J.K., Son D.Y.
Biochim. Biophys. Acta 1395:309-314(1998) [PubMed: 9512665] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Strain: cv. Seoul.
Tissue: Leaf.
[2]Lee H.S., Chung M.S., Jo J.K., Son D.Y.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Genomic cloning and its expression analysis of glutathione reductase from Brassica campestris var. Pekinensis."
Lee H.S., Lee B., Won S., Jo J.K.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Seoul.

Cross-references

Sequence databases

AF008441 mRNA. Translation: AAC49980.2.
AF255651 Genomic DNA. Translation: AAF67753.1.
PIRT14394.

3D structure databases

HSSPHSSP built from PDB template 1ONF based on UniProtKB Q94655.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.8.1.7. 142183.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006324. Glut_reduct_pln.
IPR000815. Hg_reductase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01424. gluta_reduc_2. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHRC_BRARP
AccessionPrimary (citable) accession number: O04955
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2000
Last modified: September 22, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents