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Q6BPI1

- GSHR_DEBHA

UniProt

Q6BPI1 - GSHR_DEBHA

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Protein

Glutathione reductase

Gene

GLR1

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

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei479 – 4791Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 4911FADBy 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-KW
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-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi4959.Q6BPI1.

Structurei

3D structure databases

ProteinModelPortaliQ6BPI1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
InParanoidiQ6BPI1.
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

« Hide

        10         20         30         40         50
MAPLQAIRKY DYLVIGGGSG GVASARRAAS YGAKVLLIES KFNKMGGTCV
60 70 80 90 100
NVGCVPKKVM WYAGDLAEKR HHLKSYGLST TDDKVKYGDF DWSTFKDKRD
110 120 130 140 150
AYVKRLNGIY ERNLKNEGVD YIYGFAHFAN SNGDVEVTLT GDQELSFLEE
160 170 180 190 200
GKEFKKDEKL VFAGSKTLIA TGGYAINPPN VEGHELGTTS DGFFELQKQP
210 220 230 240 250
KSVAVVGAGY IGVELSGIFK ALGSETHLVI RGDTVLRSFD ESIQNSITDY
260 270 280 290 300
YTDKLGVNII KQSGSVSKVE KIDGDRKKIT LGNGQVLEVD ELIWTMGRKS
310 320 330 340 350
LINIGLDKVG VTLNDKQQVD VDQFQQTANP NIFSLGDVIG KVELTPVAIA
360 370 380 390 400
AGRRLSNRLF SGDKAFENDH LDYSNVPSVI FSHPEAGSIG LSCKEAKEKY
410 420 430 440 450
GEDQIKIYKS KFNAMYYAMM EDDSLKSPTS YKVVCAGEDE KVVGLHIVGD
460 470 480 490
SSAEILQGFG VAIKMGATKK DFDSCVAIHP TSAEELVTMK
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi Q6BPI1.
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 26, 2014
This is version 75 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3