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Protein

Glutathione S-transferase class-mu 26 kDa isozyme 1

Gene
N/A
Organism
Fasciola hepatica (Liver fluke)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei110SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 2230.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase class-mu 26 kDa isozyme 1 (EC:2.5.1.18)
Short name:
GST1
Alternative name(s):
Fh1
OrganismiFasciola hepatica (Liver fluke)
Taxonomic identifieri6192 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaPlagiorchiidaEchinostomataEchinostomatoideaFasciolidaeFasciola

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001858102 – 221Glutathione S-transferase class-mu 26 kDa isozyme 1Add BLAST220

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1221
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Turni12 – 14Combined sources3
Helixi15 – 23Combined sources9
Beta strandi27 – 32Combined sources6
Helixi37 – 43Combined sources7
Turni44 – 46Combined sources3
Beta strandi54 – 58Combined sources5
Beta strandi63 – 66Combined sources4
Helixi67 – 77Combined sources11
Helixi85 – 109Combined sources25
Helixi114 – 136Combined sources23
Beta strandi144 – 146Combined sources3
Helixi149 – 164Combined sources16
Turni166 – 171Combined sources6
Helixi173 – 183Combined sources11
Helixi186 – 192Combined sources7
Beta strandi194 – 196Combined sources3
Beta strandi208 – 210Combined sources3
Beta strandi212 – 214Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FHEX-ray2.30A/B2-216[»]
ProteinModelPortaliP56598.
SMRiP56598.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56598.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 82GST N-terminalAdd BLAST81
Domaini84 – 202GST C-terminalAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 8Glutathione bindingCombined sources1 Publication2
Regioni40 – 44Glutathione bindingCombined sources1 Publication5
Regioni53 – 54Glutathione bindingCombined sources1 Publication2
Regioni66 – 67Glutathione bindingCombined sources1 Publication2

Sequence similaritiesi

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

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.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P56598-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAKLGYWKI RGLQQPVRLL LEYGEKYEEQ IYERDDGEKW FSKKFELGLD
60 70 80 90 100
LPNLPYYIDD KCKLTQSLAI LRYIADKHGM IGSTPEERAR VSMIEGAAVD
110 120 130 140 150
LRQGLSRISY DPKFEQLKEG YLKDLPTTMK MWSDFLGKNP YLRGTSVSHV
160 170 180 190 200
DFMVYEALDA IRYLEPHCLD HFPNLQQFMS RIEALPSIKA YMESNRFIKW
210 220
PLNGWHAQFG GGDAPPSHEK K
Length:221
Mass (Da):25,730
Last modified:January 23, 2007 - v2
Checksum:i17EAF460F750895F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23Y → V in CAA00118 (Ref. 2) Curated1
Sequence conflicti111 – 112DP → VS in CAA00118 (Ref. 2) Curated2
Sequence conflicti190A → P in CAA00118 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
A00993 Unassigned RNA. Translation: CAA00118.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
A00993 Unassigned RNA. Translation: CAA00118.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FHEX-ray2.30A/B2-216[»]
ProteinModelPortaliP56598.
SMRiP56598.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.5.1.18. 2230.

Miscellaneous databases

EvolutionaryTraceiP56598.

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.
IPR003081. GST_mu.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01267. GSTRNSFRASEM.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGST29_FASHE
AccessioniPrimary (citable) accession number: P56598
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 81 of the entry and version 2 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.