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O04955

- GSHRC_BRARP

UniProt

O04955 - GSHRC_BRARP

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Protein

Glutathione reductase, cytosolic

Gene
GR1
Organism
Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis)
Status
Reviewed - 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

Binds 1 FAD per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei237 – 2371NADP By similarity
Binding sitei243 – 2431NADP By similarity
Active sitei475 – 4751Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi67 – 7610FAD By 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
Gene namesi
Name:GR1
OrganismiBrassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis)
Taxonomic identifieri51351 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica
ProteomesiUP000011750: Unplaced

Subcellular locationi

Cytoplasm Reviewed prediction

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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-active By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By paraquat and ozone.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO04955.

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.

O04955-1 [UniParc]FASTAAdd to Basket

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MARKMLSDGE LNKAAAAGEE ATTETHYDFD LFVIGAGSGG VRAARFSANN    50
GAKVGICELP FHPISSEEIG GVGGTCVIRG CVPKKILVYG ATYGGELEDA 100
RNYGWEINGN VDFNWKKLLQ KKTDEILRLN NIYKRLLANA AVKLYEGEGR 150
IVGPNEVEVR QIDGTKISYT AKHILIATGS RAQKPNIPGH ELAITSDEAL 200
SLEEFPKRAI VLGGGYIAVE FASIWRGMGA TVDLFFRKEL PLRGFDDEMR 250
ALVARNLEGR GINLHPQTSL AELIKTDDGI KVISSHGEEF VADVVLFATG 300
RIPNTKRLNL EAVGVELDQA GAVKVDEYSR TNIPSIWAVG DATNRINLTP 350
VALMEATCFA NTVFGGKPAK ADYTNVACAV FCIPPLAVVG LSEEEAVEKA 400
TGDILVFTSG FNPMKNTISG RQEKSLMKLI VDEKTDKVIG ASMCGPDAAE 450
IMQGIAIALK CGATKAQFDS TVGIHPSSAE EFVTMRTVTR RIAYKAKPQT 500
SL 502
Length:502
Mass (Da):54,059
Last modified:October 1, 2000 - v2
Checksum:i397D978EE114B6BE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF008441 mRNA. Translation: AAC49980.2.
AF255651 Genomic DNA. Translation: AAF67753.1.
PIRiT14394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF008441 mRNA. Translation: AAC49980.2 .
AF255651 Genomic DNA. Translation: AAF67753.1 .
PIRi T14394.

3D structure databases

ProteinModelPortali O04955.
ModBasei Search...
MobiDBi Search...

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. "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: February 19, 2014
This is version 88 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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