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P30112

- GST26_FASHE

UniProt

P30112 - GST26_FASHE

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Protein

Glutathione S-transferase class-mu 26 kDa isozyme 51

Gene
N/A
Organism
Fasciola hepatica (Liver fluke)
Status
Reviewed - 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 51 (EC:2.5.1.18)
Short name:
GST51
Alternative name(s):
Fh51
OrganismiFasciola hepatica (Liver fluke)
Taxonomic identifieri6192 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaEchinostomidaEchinostomataEchinostomatoideaFasciolidaeFasciola

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 218217Glutathione S-transferase class-mu 26 kDa isozyme 51PRO_0000185807Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Turni12 – 143Combined sources
Helixi15 – 2410Combined sources
Beta strandi29 – 335Combined sources
Helixi38 – 447Combined sources
Beta strandi55 – 606Combined sources
Beta strandi63 – 675Combined sources
Helixi68 – 7811Combined sources
Helixi86 – 11025Combined sources
Helixi115 – 13723Combined sources
Beta strandi145 – 1473Combined sources
Helixi150 – 16213Combined sources
Turni163 – 1653Combined sources
Turni167 – 1726Combined sources
Helixi174 – 18411Combined sources
Helixi187 – 1948Combined sources
Beta strandi208 – 2114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WRTX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L1-218[»]
ProteinModelPortaliP30112.
SMRiP30112. Positions 2-215.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30112.

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 bindingBy similarity
Regioni41 – 455Glutathione bindingBy similarity
Regioni54 – 552Glutathione bindingBy similarity
Regioni67 – 682Glutathione bindingBy similarity

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.

P30112-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPAKLGYWKI RGLQQPVRLL LEYLGEEYEE HLYGRDDREK WFGDKFNMGL
60 70 80 90 100
DLPNLPYYID DKCKLTQSVA IMRYIADKHG MLGTTPEERA RISMIEGAAM
110 120 130 140 150
DLRMGFVRVC YNPKFEEVKG DYLKELPTTL KMWSNFLGDR HYLTGSPVSH
160 170 180 190 200
VDFMVYEALD CIRYLAPQCL EDFPKLKEFK SRIEDLPKIK AYMESEKFIK
210
WPLNSWIASF GGGDAAPA
Length:218
Mass (Da):25,373
Last modified:January 23, 2007 - v3
Checksum:iDF8A826E056A2196
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841T → S(PubMed:7682383)Curated
Sequence conflicti135 – 1351N → D(PubMed:7682383)Curated
Sequence conflicti147 – 1471P → T(PubMed:7682383)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77682 mRNA. Translation: AAA29141.1.
PIRiA48388.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77682 mRNA. Translation: AAA29141.1 .
PIRi A48388.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WRT X-ray 2.40 A/B/C/D/E/F/G/H/I/J/K/L 1-218 [» ]
ProteinModelPortali P30112.
SMRi P30112. Positions 2-215.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P30112.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "Sequence analysis of a Fasciola hepatica glutathione S-transferase cDNA clone."
    Muro A., Rodriguez-Medina J.R., Hillyer G.V.
    Am. J. Trop. Med. Hyg. 48:457-463(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-218.

Entry informationi

Entry nameiGST26_FASHE
AccessioniPrimary (citable) accession number: P30112
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 75 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