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Protein

Glutathione reductase

Gene

GLR1

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei459 – 4591Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 449FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. glutathione-disulfide reductase activity Source: UniProtKB-EC
  3. mercury (II) reductase activity Source: InterPro
  4. mercury ion binding Source: InterPro
  5. NADP binding Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to hydrogen peroxide Source: EnsemblFungi
  3. cellular response to menadione Source: EnsemblFungi
  4. detoxification of mercury ion Source: InterPro
  5. glutathione metabolic process Source: EnsemblFungi
  6. protein glutathionylation Source: EnsemblFungi
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:YALI0E18029g
OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic identifieri284591 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
ProteomesiUP000001300 Componenti: Chromosome E

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: EnsemblFungi
  2. mitochondrion Source: EnsemblFungi
  3. nucleus Source: EnsemblFungi
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Glutathione reductasePRO_0000067971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 49Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi4952.Q6C5H4.

Structurei

3D structure databases

ProteinModelPortaliQ6C5H4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
InParanoidiQ6C5H4.
KOiK00383.
OMAiHKEPTVY.
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.

Q6C5H4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASIPHYDYL VIGGGSGGVA SARRAASYGA KTLLIEGKAL GGTCVNVGCV
60 70 80 90 100
PKKVMWNASD LAGRIRQAKE YGFPDVDPKY ADNFDWSGFK AKRDAYVKRL
110 120 130 140 150
NGIYERNLQK EGVEYVFGWA TLYKQEGQEF PLVHVKSDDG NTKLYSAKKI
160 170 180 190 200
MIATGGKPRL PDVPGAEYGI DSDGFFALET QPKRVAVVGG GYIGVELAGV
210 220 230 240 250
FHGLNSETTL FCRGQTVLRA FDIMIQDTIT DYYVKEGINV LKGSGVKKIV
260 270 280 290 300
KKDNGELLVT YEQDGAEKDI TLDSLIWTIG REPLKDTLNL GEFGIKTNKR
310 320 330 340 350
GYIEVDEYQR SSVDNIYSLG DVCGKVELTP MAIAAGRKLS NRLFGPTEFK
360 370 380 390 400
NQKQDYTDVP SAVFSHPEVG SIGITEAAAK EQYGEENVKV YTSKFVAMYY
410 420 430 440 450
AMLEEKAPTA YKLVCAGKDE KVVGLHIVGA DSAEILQGFG VAIRMGATKA
460 470
DFDNVVAIHP TSAEELVTMR
Length:470
Mass (Da):51,302
Last modified:August 15, 2004 - v1
Checksum:iB9E4760F181DD143
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382131 Genomic DNA. Translation: CAG79681.1.
RefSeqiXP_504088.1. XM_504088.1.

Genome annotation databases

EnsemblFungiiCAG79681; CAG79681; YALI0_E18029g.
GeneIDi2911696.
KEGGiyli:YALI0E18029g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382131 Genomic DNA. Translation: CAG79681.1.
RefSeqiXP_504088.1. XM_504088.1.

3D structure databases

ProteinModelPortaliQ6C5H4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4952.Q6C5H4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG79681; CAG79681; YALI0_E18029g.
GeneIDi2911696.
KEGGiyli:YALI0E18029g.

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
InParanoidiQ6C5H4.
KOiK00383.
OMAiHKEPTVY.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiGSHR_YARLI
AccessioniPrimary (citable) accession number: Q6C5H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2004
Last sequence update: August 15, 2004
Last modified: March 31, 2015
This is version 82 of the entry and version 1 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

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.