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Protein

Glutathione S-transferase

Gene

GST

Organism
Plasmodium falciparum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin).3 Publications

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.4 Publications

Enzyme regulationi

Inhibited by chloroquine, cibacron blue, ferriprotoporphyrin IX (hemin) and S-hexylglutathione.3 Publications

Kineticsi

  1. KM=0.156 mM for bromosulphophthalein4 Publications
  2. KM=10 mM for 1-chloro-2,4-dinitrobenzene4 Publications
  3. KM=2.5 mM for 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole4 Publications
  4. KM=0.96 mM for ethacrynic acid4 Publications
  5. KM=0.164 mM for reduced glutathione4 Publications

    pH dependencei

    Optimum pH is 8.1.4 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei105GlutathioneCombined sources1
    Binding sitei117Glutathione; via carbonyl oxygen1 Publication1
    Binding sitei121Glutathione1 Publication1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 4889.
    SABIO-RKQ8MU52.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase (EC:2.5.1.18)
    Alternative name(s):
    PfGST
    Gene namesi
    Name:GST
    OrganismiPlasmodium falciparum
    Taxonomic identifieri5833 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi9Y → F: Greater than 10-fold decrease in activity. 1 Publication1
    Mutagenesisi15K → E: 10-fold decrease in substrate affinity and 20-fold decrease in activity. 1 Publication1
    Mutagenesisi71Q → E: 3-fold decrease in substrate affinity and 2-fold decrease in activity. 1 Publication1
    Mutagenesisi101C → A: 2-fold decrease in substrate affinity. 1 Publication1
    Mutagenesisi211Y → F: 2-fold increase in activity. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL1697656.
    DrugBankiDB00608. Chloroquine.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002599661 – 211Glutathione S-transferaseAdd BLAST211

    Proteomic databases

    PaxDbiQ8MU52.

    Interactioni

    Subunit structurei

    Homodimer. In the absence of ligands two homodimers may interact to form a tetramer.2 Publications

    Protein-protein interaction databases

    STRINGi5833.PF14_0187.

    Chemistry databases

    BindingDBiQ8MU52.

    Structurei

    Secondary structure

    1211
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 12Combined sources8
    Turni14 – 16Combined sources3
    Helixi17 – 26Combined sources10
    Beta strandi31 – 35Combined sources5
    Beta strandi37 – 39Combined sources3
    Helixi41 – 51Combined sources11
    Beta strandi55 – 57Combined sources3
    Beta strandi61 – 64Combined sources4
    Beta strandi67 – 70Combined sources4
    Helixi72 – 82Combined sources11
    Helixi90 – 111Combined sources22
    Turni115 – 118Combined sources4
    Helixi120 – 126Combined sources7
    Helixi128 – 141Combined sources14
    Turni142 – 144Combined sources3
    Helixi160 – 175Combined sources16
    Turni179 – 182Combined sources4
    Helixi184 – 194Combined sources11
    Helixi197 – 205Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1OKTX-ray1.90A/B1-211[»]
    1PA3X-ray2.70A/B1-211[»]
    1Q4JX-ray2.20A/B1-211[»]
    2AAWX-ray2.40A/C1-211[»]
    3FR3X-ray1.90A/B1-211[»]
    3FR6X-ray2.60A/B1-211[»]
    3FR9X-ray2.40A/B1-211[»]
    3FRCX-ray2.00A/B1-211[»]
    4ZXGX-ray1.70A/B3-207[»]
    ProteinModelPortaliQ8MU52.
    SMRiQ8MU52.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8MU52.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini3 – 87GST N-terminalSequence analysisAdd BLAST85
    Domaini89 – 211GST C-terminalSequence analysisAdd BLAST123

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni58 – 59Glutathione binding1 Publication2
    Regioni71 – 72Glutathione binding1 Publication2

    Sequence similaritiesi

    Belongs to the GST superfamily.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiENOG410IN5F. Eukaryota.
    ENOG41127WC. LUCA.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF14497. GST_C_3. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8MU52-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGDNIVLYYF DARGKAELIR LIFAYLGIEY TDKRFGVNGD AFVEFKNFKK
    60 70 80 90 100
    EKDTPFEQVP ILQIGDLILA QSQAIVRYLS KKYNICGESE LNEFYADMIF
    110 120 130 140 150
    CGVQDIHYKF NNTNLFKQNE TTFLNEDLPK WSGYFEKLLK KNHTNNNNDK
    160 170 180 190 200
    YYFVGNNLTY ADLAVFNLYD DIETKYPSSL KNFPLLKAHN EFISNLPNIK
    210
    NYITNRKESV Y
    Length:211
    Mass (Da):24,789
    Last modified:October 1, 2002 - v1
    Checksum:iEDC79583CFC9D751
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti1M → MKL in AAL25087 (PubMed:12387854).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY014840 mRNA. Translation: AAK00582.1.
    AF426836 mRNA. Translation: AAL25087.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY014840 mRNA. Translation: AAK00582.1.
    AF426836 mRNA. Translation: AAL25087.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1OKTX-ray1.90A/B1-211[»]
    1PA3X-ray2.70A/B1-211[»]
    1Q4JX-ray2.20A/B1-211[»]
    2AAWX-ray2.40A/C1-211[»]
    3FR3X-ray1.90A/B1-211[»]
    3FR6X-ray2.60A/B1-211[»]
    3FR9X-ray2.40A/B1-211[»]
    3FRCX-ray2.00A/B1-211[»]
    4ZXGX-ray1.70A/B3-207[»]
    ProteinModelPortaliQ8MU52.
    SMRiQ8MU52.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi5833.PF14_0187.

    Chemistry databases

    BindingDBiQ8MU52.
    ChEMBLiCHEMBL1697656.
    DrugBankiDB00608. Chloroquine.

    Proteomic databases

    PaxDbiQ8MU52.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG410IN5F. Eukaryota.
    ENOG41127WC. LUCA.

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 4889.
    SABIO-RKQ8MU52.

    Miscellaneous databases

    EvolutionaryTraceiQ8MU52.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF14497. GST_C_3. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGST_PLAFA
    AccessioniPrimary (citable) accession number: Q8MU52
    Secondary accession number(s): Q95V54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: October 1, 2002
    Last modified: November 2, 2016
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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.