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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: -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 sitei111SubstrateBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionTransferase

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 lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaPlagiorchiidaEchinostomataEchinostomatoideaFasciolidaeFasciola

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001858072 – 218Glutathione S-transferase class-mu 26 kDa isozyme 51Add BLAST217

Proteomic databases

PRIDEiP30112

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1218
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Turni12 – 14Combined sources3
Helixi15 – 24Combined sources10
Beta strandi29 – 33Combined sources5
Helixi38 – 44Combined sources7
Beta strandi55 – 60Combined sources6
Beta strandi63 – 67Combined sources5
Helixi68 – 78Combined sources11
Helixi86 – 110Combined sources25
Helixi115 – 137Combined sources23
Beta strandi145 – 147Combined sources3
Helixi150 – 162Combined sources13
Turni163 – 165Combined sources3
Turni167 – 172Combined sources6
Helixi174 – 184Combined sources11
Helixi187 – 194Combined sources8
Beta strandi208 – 211Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP30112

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 83GST N-terminalAdd BLAST82
Domaini85 – 203GST C-terminalAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 8Glutathione bindingBy similarity2
Regioni41 – 45Glutathione bindingBy similarity5
Regioni54 – 55Glutathione bindingBy similarity2
Regioni67 – 68Glutathione bindingBy similarity2

Sequence similaritiesi

Belongs to the GST superfamily. Mu family.Curated

Family and domain databases

InterProiView protein in InterPro
IPR010987 Glutathione-S-Trfase_C-like
IPR036282 Glutathione-S-Trfase_C_sf
IPR004045 Glutathione_S-Trfase_N
IPR004046 GST_C
IPR036249 Thioredoxin-like_sf
PfamiView protein in Pfam
PF14497 GST_C_3, 1 hit
PF02798 GST_N, 1 hit
SUPFAMiSSF47616 SSF47616, 1 hit
SSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS50405 GST_CTER, 1 hit
PS50404 GST_NTER, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti84T → S (PubMed:7682383).Curated1
Sequence conflicti135N → D (PubMed:7682383).Curated1
Sequence conflicti147P → T (PubMed:7682383).Curated1

Sequence databases

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

Similar proteinsi

Entry informationi

Entry nameiGST26_FASHE
AccessioniPrimary (citable) accession number: P30112
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 87 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

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