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Protein

Glutathione reductase

Gene

GR2

Organism
Plasmodium falciparum (isolate K1 / Thailand)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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)DescriptionActionsGraphical viewLength
Active sitei485Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 40FADBy similarity9

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 (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:GR2
OrganismiPlasmodium falciparum (isolate K1 / Thailand)
Taxonomic identifieri5839 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1741261.
DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000679592 – 500Glutathione reductaseAdd BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi40 ↔ 45Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1500
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi12 – 23Combined sources12
Beta strandi28 – 35Combined sources8
Helixi38 – 42Combined sources5
Helixi45 – 63Combined sources19
Helixi64 – 67Combined sources4
Helixi77 – 101Combined sources25
Beta strandi105 – 109Combined sources5
Beta strandi142 – 147Combined sources6
Helixi161 – 163Combined sources3
Helixi167 – 170Combined sources4
Beta strandi177 – 182Combined sources6
Helixi186 – 196Combined sources11
Turni197 – 199Combined sources3
Beta strandi201 – 205Combined sources5
Beta strandi207 – 211Combined sources5
Helixi217 – 229Combined sources13
Beta strandi233 – 235Combined sources3
Beta strandi240 – 247Combined sources8
Beta strandi251 – 255Combined sources5
Beta strandi260 – 269Combined sources10
Turni276 – 279Combined sources4
Turni283 – 286Combined sources4
Beta strandi289 – 292Combined sources4
Beta strandi294 – 296Combined sources3
Beta strandi303 – 309Combined sources7
Beta strandi314 – 316Combined sources3
Helixi354 – 369Combined sources16
Beta strandi383 – 385Combined sources3
Beta strandi391 – 395Combined sources5
Helixi398 – 404Combined sources7
Helixi407 – 409Combined sources3
Beta strandi410 – 417Combined sources8
Helixi420 – 422Combined sources3
Helixi429 – 431Combined sources3
Beta strandi435 – 442Combined sources8
Turni443 – 446Combined sources4
Beta strandi447 – 455Combined sources9
Helixi458 – 470Combined sources13
Helixi475 – 479Combined sources5
Helixi491 – 494Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ONFX-ray2.60A1-500[»]
ProteinModelPortaliQ94655.
SMRiQ94655.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ94655.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 4 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q94655-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVYDLIVIGG GSGGMAAARR AARHNAKVAL VEKSRLGGTC VNVGCVPKKI
60 70 80 90 100
MFNAASVHDI LENSRHYGFD TKFSFNLPLL VERRDKYIQR LNNIYRQNLS
110 120 130 140 150
KDKVDLYEGT ASFLSENRIL IKGTKDNNNK DNGPLNEEIL EGRNILIAVG
160 170 180 190 200
NKPVFPPVKG IENTISSDEF FNIKESKKIG IVGSGYIAVE LINVIKRLGI
210 220 230 240 250
DSYIFARGNR ILRKFDESVI NVLENDMKKN NINIVTFADV VEIKKVSDKN
260 270 280 290 300
LSIHLSDGRI YEHFDHVIYC VGRSPDTENL KLEKLNVETN NNYIVVDENQ
310 320 330 340 350
RTSVNNIYAV GDCCMVKKSK EIEDLNLLKL YNEERYLNKK ENVTEDIFYN
360 370 380 390 400
VQLTPVAINA GRLLADRLFL KKTRKTNYKL IPTVIFSHPP IGTIGLSEEA
410 420 430 440 450
AIQIYGKENV KIYESKFTNL FFSVYDIEPE LKEKTYLKLV CVGKDELIKG
460 470 480 490 500
LHIIGLNADE IVQGFAVALK MNATKKDFDE TIPIHPTAAE EFLTLQPWMK
Length:500
Mass (Da):56,561
Last modified:January 23, 2007 - v3
Checksum:iAB2299144002FCD3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93462 Genomic DNA. Translation: CAA63747.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93462 Genomic DNA. Translation: CAA63747.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ONFX-ray2.60A1-500[»]
ProteinModelPortaliQ94655.
SMRiQ94655.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL1741261.
DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ94655.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 4 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSHR_PLAFK
AccessioniPrimary (citable) accession number: Q94655
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.