Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q94655

- GSHR_PLAFK

UniProt

Q94655 - GSHR_PLAFK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutathione reductase

Gene

GR2

Organism
Plasmodium falciparum (isolate K1 / Thailand)
Status
Reviewed - 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

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: UniProtKB-EC

GO - Biological processi

  1. cell redox homeostasis 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:GR2
OrganismiPlasmodium falciparum (isolate K1 / Thailand)
Taxonomic identifieri5839 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 500499Glutathione reductasePRO_0000067959Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86
Helixi12 – 2312
Beta strandi28 – 358
Helixi38 – 425
Helixi45 – 6319
Helixi64 – 674
Helixi77 – 10125
Beta strandi105 – 1095
Beta strandi142 – 1476
Helixi161 – 1633
Helixi167 – 1704
Beta strandi177 – 1826
Helixi186 – 19611
Turni197 – 1993
Beta strandi201 – 2055
Beta strandi207 – 2115
Helixi217 – 22913
Beta strandi233 – 2353
Beta strandi240 – 2478
Beta strandi251 – 2555
Beta strandi260 – 26910
Turni276 – 2794
Turni283 – 2864
Beta strandi289 – 2924
Beta strandi294 – 2963
Beta strandi303 – 3097
Beta strandi314 – 3163
Helixi354 – 36916
Beta strandi383 – 3853
Beta strandi391 – 3955
Helixi398 – 4047
Helixi407 – 4093
Beta strandi410 – 4178
Helixi420 – 4223
Helixi429 – 4313
Beta strandi435 – 4428
Turni443 – 4464
Beta strandi447 – 4559
Helixi458 – 47013
Helixi475 – 4795
Helixi491 – 4944

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONFX-ray2.60A1-500[»]
ProteinModelPortaliQ94655.
SMRiQ94655. Positions 2-496.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ94655.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.

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.

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:
EMBL
GenBank
DDBJ
Links Updated
X93462 Genomic DNA. Translation: CAA63747.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X93462 Genomic DNA. Translation: CAA63747.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ONF X-ray 2.60 A 1-500 [» ]
ProteinModelPortali Q94655.
SMRi Q94655. Positions 2-496.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL1741261.
DrugBanki DB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG1249.

Miscellaneous databases

EvolutionaryTracei Q94655.

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

  1. "Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum."
    Faerber P.M., Becker K., Mueller S.
    Eur. J. Biochem. 239:655-661(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria."
    Krauth-Siegel R.L., Muller J.G., Lottspeich F., Schirmer R.H.
    Eur. J. Biochem. 235:345-350(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16, CHARACTERIZATION.

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: October 29, 2014
This is version 94 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

External Data

Dasty 3