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 28 kDa isozyme

Gene

GST28

Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed-Annotation score: Annotation score: 5 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)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:2.5.1.18)
Short name:
GST 28
Alternative name(s):
GSH transferase S.m. 1-1
Protective 28 kDa antigen
Sm28 antigen
Sm28GST
Smp28
Gene namesi
Name:GST28
ORF Names:Smp_054160
OrganismiSchistosoma mansoni (Blood fluke)
Taxonomic identifieri6183 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma
Proteomesi
  • UP000008854 Componenti: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001858152 – 211Glutathione S-transferase class-mu 28 kDa isozymeAdd BLAST210

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

Expressioni

Tissue specificityi

In the adult, expressed in excretory epithelial cells but absent from the caecal epithelium and flame cells. Also expressed in the tegument and its extensions into the parenchyma. In the schistosomulum, expressed in the tegument and associated structures. Not expressed in digestive tract, reproductive organs or muscles (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi6183.Smp_054160__mRNA.

Structurei

Secondary structure

1211
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 14Combined sources10
Helixi15 – 17Combined sources3
Helixi18 – 27Combined sources10
Beta strandi32 – 36Combined sources5
Turni38 – 40Combined sources3
Helixi41 – 44Combined sources4
Helixi45 – 47Combined sources3
Beta strandi55 – 59Combined sources5
Beta strandi61 – 63Combined sources3
Beta strandi65 – 69Combined sources5
Helixi71 – 81Combined sources11
Helixi89 – 110Combined sources22
Turni111 – 114Combined sources4
Helixi119 – 129Combined sources11
Helixi131 – 144Combined sources14
Beta strandi147 – 152Combined sources6
Helixi158 – 173Combined sources16
Turni175 – 180Combined sources6
Helixi183 – 195Combined sources13
Helixi197 – 205Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U3IX-ray1.89A1-211[»]
ProteinModelPortaliP09792.
SMRiP09792.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09792.

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

Phylogenomic databases

eggNOGiENOG410IN5B. Eukaryota.
ENOG4112BRZ. LUCA.
HOGENOMiHOG000115733.
InParanoidiP09792.
OrthoDBiEOG091G0MBB.
PhylomeDBiP09792.

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.

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

P09792-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGEHIKVIY FDGRGRAESI RMTLVAAGVD YEDERISFQD WPKIKPTIPG
60 70 80 90 100
GRLPAVKVTD DHGHVKWMLE SLAIARYMAK KHHMMGETDE EYYSVEKLIG
110 120 130 140 150
QAEDVEHEYH KTLMKPQEEK EKITKEILNG KVPVLLNMIC ESLKGSTGKL
160 170 180 190 200
AVGDKVTLAD LVLIAVIDHV TDLDKGFLTG KYPEIHKHRE NLLASSPRLA
210
KYLSNRPATP F
Length:211
Mass (Da):23,820
Last modified:July 1, 1989 - v1
Checksum:iF988AAF041D767E3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti47T → I AA sequence (PubMed:3284744).Curated1
Sequence conflicti106E → D AA sequence (PubMed:3284744).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05148 mRNA. Translation: CAA28796.1.
M98271 Genomic DNA. Translation: AAA29891.1.
S71584 mRNA. Translation: AAC60508.1.
CABG01000068 Genomic DNA. Translation: CCD60449.1.
PIRiJU0137.
S02458.

Genome annotation databases

EnsemblMetazoaiSmp_054160.1; Smp_054160.1:pep; Smp_054160.
GeneDBiSmp_054160.1:pep.
Smp_059340.1:pep.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05148 mRNA. Translation: CAA28796.1.
M98271 Genomic DNA. Translation: AAA29891.1.
S71584 mRNA. Translation: AAC60508.1.
CABG01000068 Genomic DNA. Translation: CCD60449.1.
PIRiJU0137.
S02458.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U3IX-ray1.89A1-211[»]
ProteinModelPortaliP09792.
SMRiP09792.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6183.Smp_054160__mRNA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiSmp_054160.1; Smp_054160.1:pep; Smp_054160.
GeneDBiSmp_054160.1:pep.
Smp_059340.1:pep.

Phylogenomic databases

eggNOGiENOG410IN5B. Eukaryota.
ENOG4112BRZ. LUCA.
HOGENOMiHOG000115733.
InParanoidiP09792.
OrthoDBiEOG091G0MBB.
PhylomeDBiP09792.

Miscellaneous databases

EvolutionaryTraceiP09792.

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_SCHMA
AccessioniPrimary (citable) accession number: P09792
Secondary accession number(s): G4LZY1, Q7M446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

There are at least three isoenzymes of GST in S.mansoni.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.