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O15770

- GSHR_PLAF7

UniProt

O15770 - GSHR_PLAF7

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Protein
Glutathione reductase
Gene
GR3, PF14_0192
Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed - 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

Binds 1 FAD per subunit By similarity.

Sites

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

Regions

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

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. glutathione-disulfide reductase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiREACT_191640. Detoxification of Reactive Oxygen Species.

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: Chromosome 14

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_1419800.2.

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
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 500499Glutathione reductase
PRO_0000067960Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi5833.PF14_0192-1.

Structurei

3D structure databases

ProteinModelPortaliO15770.
SMRiO15770. Positions 2-496.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000276712.
KOiK00383.
OMAiGTNSDGF.
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

MVYDLIVIGG GSGGMAAARR AARHNAKVAL VEKSRLGGTC VNVGCVPKKI    50
MFNAASVHDI LENSRHYGFD TKFSFNLPLL VERRDKYIQR LNNIYRQNLS 100
KDKVDLYEGT ASFLSENRIL IKGTKDNNNK DNGPLNEEIL EGRNILIAVG 150
NKPVFPPVKG IENTISSDEF FNIKESKKIG IVGSGYIAVE LINVIKRLGI 200
DSYIFARGNR ILRKFDESVI NVLENDMKKN NINIVTFADV VEIKKVSDKN 250
LSIHLSDGRI YEHFDHVIYC VGRSPDTENL NLEKLNVETN NNYIVVDENQ 300
RTSVNNIYAV GDCCMVKKSK EIEDLNLLKL YNEETYLNKK ENVTEDIFYN 350
VQLTPVAINA GRLLADRLFL KKTRKTNYKL IPTVIFSHPP IGTIGLSEEA 400
AIQIYGKENV KIYESKFTNL FFSVYDIEPE LKEKTYLKLV CVGKDELIKG 450
LHIIGLNADE IVQGFAVALK MNATKKDFDE TIPIHPTAAE EFLTLQPWMK 500
Length:500
Mass (Da):56,492
Last modified:October 5, 2010 - v4
Checksum:iEFFBA1668599EA37
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF027825 mRNA. Translation: AAB84117.1 .
AE014187 Genomic DNA. Translation: AAN36804.1 .
RefSeqi XP_001348365.1. XM_001348329.1.

3D structure databases

ProteinModelPortali O15770.
SMRi O15770. Positions 2-496.
ModBasei Search...

Protein-protein interaction databases

STRINGi 5833.PF14_0192-1.

Chemistry

BindingDBi O15770.
ChEMBLi CHEMBL5061.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblProtistsi PF14_0192:mRNA ; PF14_0192:pep ; PF14_0192 .
GeneIDi 811773.
KEGGi pfa:PF14_0192.

Organism-specific databases

EuPathDBi PlasmoDB:PF3D7_1419800.2.

Phylogenomic databases

HOGENOMi HOG000276712.
KOi K00383.
OMAi GTNSDGF.
PhylomeDBi O15770.

Enzyme and pathway databases

Reactomei REACT_191640. Detoxification of Reactive Oxygen Species.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. 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 ]
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.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Glutathione reductase from Plasmodium falciparum."
    Gilberger T.-W., Walter R.D., Mueller S.
    Submitted (OCT-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: September 3, 2014
This is version 97 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