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Protein

Glutathione reductase, cytosolic

Gene

GR1

Organism
Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

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 sitei237 – 2371NADPBy similarity
Binding sitei243 – 2431NADPBy similarity
Active sitei475 – 4751Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi67 – 7610FADBy similarity

GO - Molecular functioni

GO - Biological processi

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
Gene namesi
Name:GR1
OrganismiBrassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis)
Taxonomic identifieri51351 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica
ProteomesiUP000011750 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Glutathione reductase, cytosolicPRO_0000067962Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi76 ↔ 81Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By paraquat and ozone.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO04955.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

InParanoidiO04955.
KOiK00383.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
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]
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01424. gluta_reduc_2. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O04955-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKMLSDGE LNKAAAAGEE ATTETHYDFD LFVIGAGSGG VRAARFSANN
60 70 80 90 100
GAKVGICELP FHPISSEEIG GVGGTCVIRG CVPKKILVYG ATYGGELEDA
110 120 130 140 150
RNYGWEINGN VDFNWKKLLQ KKTDEILRLN NIYKRLLANA AVKLYEGEGR
160 170 180 190 200
IVGPNEVEVR QIDGTKISYT AKHILIATGS RAQKPNIPGH ELAITSDEAL
210 220 230 240 250
SLEEFPKRAI VLGGGYIAVE FASIWRGMGA TVDLFFRKEL PLRGFDDEMR
260 270 280 290 300
ALVARNLEGR GINLHPQTSL AELIKTDDGI KVISSHGEEF VADVVLFATG
310 320 330 340 350
RIPNTKRLNL EAVGVELDQA GAVKVDEYSR TNIPSIWAVG DATNRINLTP
360 370 380 390 400
VALMEATCFA NTVFGGKPAK ADYTNVACAV FCIPPLAVVG LSEEEAVEKA
410 420 430 440 450
TGDILVFTSG FNPMKNTISG RQEKSLMKLI VDEKTDKVIG ASMCGPDAAE
460 470 480 490 500
IMQGIAIALK CGATKAQFDS TVGIHPSSAE EFVTMRTVTR RIAYKAKPQT

SL
Length:502
Mass (Da):54,059
Last modified:October 1, 2000 - v2
Checksum:i397D978EE114B6BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008441 mRNA. Translation: AAC49980.2.
AF255651 Genomic DNA. Translation: AAF67753.1.
PIRiT14394.
RefSeqiNP_001288954.1. NM_001302025.1.

Genome annotation databases

GeneIDi103828679.
KEGGibrp:103828679.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008441 mRNA. Translation: AAC49980.2.
AF255651 Genomic DNA. Translation: AAF67753.1.
PIRiT14394.
RefSeqiNP_001288954.1. NM_001302025.1.

3D structure databases

ProteinModelPortaliO04955.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi103828679.
KEGGibrp:103828679.

Phylogenomic databases

InParanoidiO04955.
KOiK00383.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
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]
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01424. gluta_reduc_2. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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.

Entry informationi

Entry nameiGSHRC_BRARP
AccessioniPrimary (citable) accession number: O04955
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 98 of the entry and version 2 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.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.