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Protein

Glutathione S-transferase class-mu 28 kDa isozyme

Gene
N/A
Organism
Schistosoma bovis (Blood 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei10Glutathione1 Publication1
Binding sitei16Glutathione1 Publication1
Binding sitei53Glutathione; via amide nitrogen and carbonyl oxygen1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase class-mu 28 kDa isozyme (EC:2.5.1.181 Publication)
Short name:
GST 28
Alternative name(s):
Sb28GST
OrganismiSchistosoma bovis (Blood fluke)
Taxonomic identifieri6184 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10Y → F: Loss of enzyme activity. 1 Publication1
Mutagenesisi21R → L: Reduces catalytic activity 12-fold. 1 Publication1
Mutagenesisi21R → Q: Reduces catalytic activity 120-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001858121 – 211Glutathione S-transferase class-mu 28 kDa isozymeAdd BLAST211

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1211
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Turni13 – 17Combined sources5
Helixi18 – 26Combined sources9
Beta strandi32 – 35Combined sources4
Turni38 – 40Combined sources3
Helixi41 – 44Combined sources4
Helixi45 – 47Combined sources3
Beta strandi53 – 59Combined sources7
Beta strandi65 – 70Combined sources6
Helixi71 – 81Combined sources11
Helixi89 – 110Combined sources22
Turni111 – 114Combined sources4
Helixi117 – 129Combined sources13
Helixi131 – 144Combined sources14
Beta strandi147 – 155Combined sources9
Helixi158 – 173Combined sources16
Turni175 – 180Combined sources6
Helixi183 – 195Combined sources13
Helixi197 – 202Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C80X-ray2.30A/B1-211[»]
2C8UX-ray2.00A/B1-211[»]
2CA8X-ray2.49A1-211[»]
2CAIX-ray2.26A/B1-211[»]
2CAQX-ray2.00A1-211[»]
2F8FX-ray2.10A/B1-211[»]
ProteinModelPortaliP30113.
SMRiP30113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30113.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 86GST N-terminalAdd BLAST83
Domaini88 – 211GST C-terminalAdd BLAST124

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 11Glutathione bindingBy similarity2
Regioni41 – 45Glutathione binding1 Publication5
Regioni55 – 56Glutathione bindingBy similarity2
Regioni70 – 71Glutathione binding1 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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 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.

P30113-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGDHIKVIY FNGRGRAESI RMTLVAAGVN YEDERISFQD WPKIKPTIPG
60 70 80 90 100
GRLPAVKITD NHGHVKWMVE SLAIARYMAK KHHMMGGTEE EYYNVEKLIG
110 120 130 140 150
QAEDLEHEYY KTLMKPEEEK QKIIKEILNG KVPVLLDIIC ESLKASTGKL
160 170 180 190 200
AVGDKVTLAD LVLIAVIDHV TDLDKEFLTG KYPEIHKHRE NLLASSPRLA
210
KYLSDRAATP F
Length:211
Mass (Da):23,898
Last modified:June 1, 1994 - v2
Checksum:i9B9F1358710D3C76
GO

Sequence cautioni

The sequence AAA29892 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87799 Genomic DNA. Translation: AAA29892.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87799 Genomic DNA. Translation: AAA29892.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C80X-ray2.30A/B1-211[»]
2C8UX-ray2.00A/B1-211[»]
2CA8X-ray2.49A1-211[»]
2CAIX-ray2.26A/B1-211[»]
2CAQX-ray2.00A1-211[»]
2F8FX-ray2.10A/B1-211[»]
ProteinModelPortaliP30113.
SMRiP30113.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP30113.

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]
PfamiPF14497. GST_C_3. 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...

Entry informationi

Entry nameiGST28_SCHBO
AccessioniPrimary (citable) accession number: P30113
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 89 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.