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Protein

Glutathione reductase

Gene

GR3

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed-Annotation score: 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

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei485 – 4851Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 409FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. glutathione-disulfide reductase activity Source: GeneDB_Pfalciparum

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. response to oxidative stress Source: GeneDB_Pfalciparum
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:GR3
ORF Names:PF14_0192
OrganismiPlasmodium falciparum (isolate 3D7)
Taxonomic identifieri36329 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)
ProteomesiUP000001450 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_1419800.2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. apicoplast Source: GeneDB_Pfalciparum
  2. cytoplasm Source: GeneDB_Pfalciparum
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 500499Glutathione reductasePRO_0000067960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 45Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi5833.PF14_0192-1.

Structurei

3D structure databases

ProteinModelPortaliO15770.
SMRiO15770. Positions 2-496.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000276712.
InParanoidiO15770.
KOiK00383.
OMAiNHYHGIG.
PhylomeDBiO15770.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

O15770-1 [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 NLEKLNVETN NNYIVVDENQ
310 320 330 340 350
RTSVNNIYAV GDCCMVKKSK EIEDLNLLKL YNEETYLNKK 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):56,492
Last modified:October 5, 2010 - v4
Checksum:iEFFBA1668599EA37
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti283 – 2831E → G in AAB84117 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027825 mRNA. Translation: AAB84117.1.
AE014187 Genomic DNA. Translation: AAN36804.1.
RefSeqiXP_001348365.1. XM_001348329.1.

Genome annotation databases

EnsemblProtistsiPF14_0192:mRNA; PF14_0192:pep; PF14_0192.
GeneIDi811773.
KEGGipfa:PF14_0192.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027825 mRNA. Translation: AAB84117.1.
AE014187 Genomic DNA. Translation: AAN36804.1.
RefSeqiXP_001348365.1. XM_001348329.1.

3D structure databases

ProteinModelPortaliO15770.
SMRiO15770. Positions 2-496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5833.PF14_0192-1.

Chemistry

ChEMBLiCHEMBL5061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiPF14_0192:mRNA; PF14_0192:pep; PF14_0192.
GeneIDi811773.
KEGGipfa:PF14_0192.

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_1419800.2.

Phylogenomic databases

HOGENOMiHOG000276712.
InParanoidiO15770.
KOiK00383.
OMAiNHYHGIG.
PhylomeDBiO15770.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
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.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Glutathione reductase from Plasmodium falciparum."
    Gilberger T.-W., Walter R.D., Mueller S.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Isolate 3D7.

Entry informationi

Entry nameiGSHR_PLAF7
AccessioniPrimary (citable) accession number: O15770
Secondary accession number(s): Q8ILQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 5, 2010
Last modified: January 7, 2015
This is version 101 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

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.