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Q6BPI1

- GSHR_DEBHA

UniProt

Q6BPI1 - GSHR_DEBHA

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Protein

Glutathione reductase

Gene
GLR1, DEHA2E13442g
Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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
Active sitei479 – 4791Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 4911FAD By similarityAdd
BLAST

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 (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:GLR1
Ordered Locus Names:DEHA2E13442g
OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic identifieri284592 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
ProteomesiUP000000599: Chromosome E

Subcellular locationi

Cytoplasm By similarity

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 – 490490Glutathione reductasePRO_0000067967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 54Redox-active By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi4959.Q6BPI1.

Structurei

3D structure databases

ProteinModelPortaliQ6BPI1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
KOiK00383.
OrthoDBiEOG79W9F2.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006322. Glutathione_Rdtase_euk/bac.
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.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6BPI1-1 [UniParc]FASTAAdd to Basket

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MAPLQAIRKY DYLVIGGGSG GVASARRAAS YGAKVLLIES KFNKMGGTCV    50
NVGCVPKKVM WYAGDLAEKR HHLKSYGLST TDDKVKYGDF DWSTFKDKRD 100
AYVKRLNGIY ERNLKNEGVD YIYGFAHFAN SNGDVEVTLT GDQELSFLEE 150
GKEFKKDEKL VFAGSKTLIA TGGYAINPPN VEGHELGTTS DGFFELQKQP 200
KSVAVVGAGY IGVELSGIFK ALGSETHLVI RGDTVLRSFD ESIQNSITDY 250
YTDKLGVNII KQSGSVSKVE KIDGDRKKIT LGNGQVLEVD ELIWTMGRKS 300
LINIGLDKVG VTLNDKQQVD VDQFQQTANP NIFSLGDVIG KVELTPVAIA 350
AGRRLSNRLF SGDKAFENDH LDYSNVPSVI FSHPEAGSIG LSCKEAKEKY 400
GEDQIKIYKS KFNAMYYAMM EDDSLKSPTS YKVVCAGEDE KVVGLHIVGD 450
SSAEILQGFG VAIKMGATKK DFDSCVAIHP TSAEELVTMK 490
Length:490
Mass (Da):53,520
Last modified:December 16, 2008 - v3
Checksum:i1076F6EDB4389EAE
GO

Sequence cautioni

The sequence CAG88130.2 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR382137 Genomic DNA. Translation: CAG88130.2. Different initiation.
RefSeqiXP_459889.2. XM_459889.2.

Genome annotation databases

GeneIDi2902393.
KEGGidha:DEHA2E13442g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR382137 Genomic DNA. Translation: CAG88130.2 . Different initiation.
RefSeqi XP_459889.2. XM_459889.2.

3D structure databases

ProteinModelPortali Q6BPI1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 4959.Q6BPI1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2902393.
KEGGi dha:DEHA2E13442g.

Phylogenomic databases

eggNOGi COG1249.
HOGENOMi HOG000276712.
KOi K00383.
OrthoDBi EOG79W9F2.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006322. Glutathione_Rdtase_euk/bac.
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 TIGR01421. gluta_reduc_1. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Entry informationi

Entry nameiGSHR_DEBHA
AccessioniPrimary (citable) accession number: Q6BPI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: December 16, 2008
Last modified: November 13, 2013
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

Similar proteinsi