Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101SubstrateBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

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 lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaEchinostomidaEchinostomataEchinostomatoideaFasciolidaeFasciola

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 221220Glutathione S-transferase class-mu 26 kDa isozyme 1PRO_0000185810Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
221
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Turni12 – 143Combined sources
Helixi15 – 239Combined sources
Beta strandi27 – 326Combined sources
Helixi37 – 437Combined sources
Turni44 – 463Combined sources
Beta strandi54 – 585Combined sources
Beta strandi63 – 664Combined sources
Helixi67 – 7711Combined sources
Helixi85 – 10925Combined sources
Helixi114 – 13623Combined sources
Beta strandi144 – 1463Combined sources
Helixi149 – 16416Combined sources
Turni166 – 1716Combined sources
Helixi173 – 18311Combined sources
Helixi186 – 1927Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi212 – 2143Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP56598.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8281GST N-terminalAdd
BLAST
Domaini84 – 202119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Glutathione binding
Regioni40 – 445Glutathione binding
Regioni53 – 542Glutathione binding
Regioni66 – 672Glutathione binding

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]
PfamiPF00043. GST_C. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231Y → V in CAA00118 (Ref. 2) Curated
Sequence conflicti111 – 1122DP → VS in CAA00118 (Ref. 2) Curated
Sequence conflicti190 – 1901A → P in CAA00118 (Ref. 2) Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2FHEX-ray2.30A/B2-216[»]
ProteinModelPortaliP56598.
SMRiP56598. Positions 2-216.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
PfamiPF00043. GST_C. 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...

Publicationsi

  1. "Molecular characterization of cDNA sequences encoding glutathione S-transferases of Fasciola hepatica."
    Panaccio M., Wilson L.R., Crameri S.L., Wijffels G.L., Spithill T.W.
    Exp. Parasitol. 74:232-237(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE OF 23-221.
  3. "Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase."
    Rossjohn J., Feil S.C., Wilce M.C.J., Sexton J.L., Spithill T.W., Parker M.W.
    J. Mol. Biol. 273:857-872(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

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: October 29, 2014
This is version 73 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

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.