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Protein

Glutathione S-transferase class-mu 26 kDa isozyme 47

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 sitei111 – 1111SubstrateBy 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 47 (EC:2.5.1.18)
Short name:
GST47
Alternative name(s):
Fh47
OrganismiFasciola hepatica (Liver fluke)
Taxonomic identifieri6192 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaEchinostomidaEchinostomataEchinostomatoideaFasciolidaeFasciola

Subcellular locationi

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
Chaini2 – 218217Glutathione S-transferase class-mu 26 kDa isozyme 47PRO_0000185808Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Turni12 – 143Combined sources
Helixi15 – 239Combined sources
Beta strandi29 – 335Combined sources
Helixi39 – 424Combined sources
Turni43 – 475Combined sources
Beta strandi55 – 595Combined sources
Beta strandi64 – 674Combined sources
Helixi70 – 778Combined sources
Turni78 – 803Combined sources
Helixi86 – 10722Combined sources
Beta strandi110 – 1123Combined sources
Helixi115 – 1228Combined sources
Turni123 – 1253Combined sources
Helixi126 – 13712Combined sources
Beta strandi145 – 1473Combined sources
Helixi150 – 16213Combined sources
Turni163 – 1653Combined sources
Helixi167 – 1704Combined sources
Helixi174 – 18512Combined sources
Helixi187 – 1926Combined sources
Beta strandi206 – 2116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHEX-ray3.00A2-218[»]
ProteinModelPortaliP31670.
SMRiP31670. Positions 2-215.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31670.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8382GST N-terminalAdd
BLAST
Domaini85 – 203119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 82Glutathione binding
Regioni41 – 455Glutathione binding
Regioni54 – 552Glutathione binding
Regioni67 – 682Glutathione 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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 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.

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

P31670-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAKLGYWKL RGLAQPVRLF LEYLGEEYEE HLYGRDDREK WMSEKFNMGL
60 70 80 90 100
DLPNLPYYID DKCKLTQSVA IMRYIADKHG MLGTTPEERA RISMIEGAAM
110 120 130 140 150
DLRIGFGRVC YNPKFEEVKE EYVKELPKTL KMWSDFLGDR HYLTGSSVSH
160 170 180 190 200
VDFMLYETLD SIRYLAPHCL DEFPKLKEFK SRIEALPKIK AYMESKRFIK
210
WPLNGWAASF GAGDAPPS
Length:218
Mass (Da):25,412
Last modified:January 23, 2007 - v3
Checksum:i3FF8B667232663B3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661T → I in CAA00121 (Ref. 2) Curated
Sequence conflicti103 – 1064RIGF → FEEL (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77681 mRNA. Translation: AAA29140.1.
A00996 Unassigned RNA. Translation: CAA00121.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77681 mRNA. Translation: AAA29140.1.
A00996 Unassigned RNA. Translation: CAA00121.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHEX-ray3.00A2-218[»]
ProteinModelPortaliP31670.
SMRiP31670. Positions 2-215.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP31670.

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]
PfamiPF00043. GST_C. 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...

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 8-106.
  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 (3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

Entry informationi

Entry nameiGST27_FASHE
AccessioniPrimary (citable) accession number: P31670
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 83 of the entry and version 3 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.