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Protein

Glutathione S-transferase class-mu 28 kDa isozyme

Gene
N/A
Organism
Schistosoma haematobium (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.1 Publication
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.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Glutathione1 Publication
Binding sitei16 – 161Glutathione1 Publication
Binding sitei53 – 531Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 7965.

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):
Sh28GST
OrganismiSchistosoma haematobium (Blood fluke)
Taxonomic identifieri6185 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Glutathione S-transferase class-mu 28 kDa isozymePRO_0000185813Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Helixi18 – 269Combined sources
Beta strandi32 – 354Combined sources
Turni38 – 403Combined sources
Helixi41 – 444Combined sources
Helixi45 – 473Combined sources
Helixi49 – 513Combined sources
Beta strandi55 – 595Combined sources
Beta strandi65 – 706Combined sources
Helixi71 – 8111Combined sources
Helixi89 – 11022Combined sources
Turni111 – 1144Combined sources
Helixi117 – 12812Combined sources
Helixi131 – 14414Combined sources
Beta strandi147 – 1526Combined sources
Helixi158 – 17316Combined sources
Turni175 – 1806Combined sources
Helixi183 – 19513Combined sources
Helixi197 – 20610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OE7X-ray1.80A/B1-211[»]
1OE8X-ray1.65A/B1-211[»]
ProteinModelPortaliP30114.
SMRiP30114. Positions 4-211.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30114.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8683GST N-terminalAdd
BLAST
Domaini88 – 211124GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 455Glutathione binding
Regioni70 – 712Glutathione 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.

P30114-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGDHIKVIY FNGRGRAESI RMTLVAAGVN YEDERISFQD WPKIKPTIPG
60 70 80 90 100
GRLPAVKITD NHGHVKWMLE SLAIARYMAK KHHMMGETDE EYYNVEKLIG
110 120 130 140 150
QVEDLEHEYH KTLMKPEEEK QKITKEILNG KVPVLLDIIC ESLKASTGKL
160 170 180 190 200
AVGDKVTLAD LVLIAVIDHV TDLDKEFLTG KYPEIHKHRE NLLASSPRLA
210
KYLSDRAATP F
Length:211
Mass (Da):23,960
Last modified:March 31, 1993 - v1
Checksum:i954B2B60AA22E2C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87800 Genomic DNA. Translation: AAA29893.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87800 Genomic DNA. Translation: AAA29893.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OE7X-ray1.80A/B1-211[»]
1OE8X-ray1.65A/B1-211[»]
ProteinModelPortaliP30114.
SMRiP30114. Positions 4-211.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.5.1.18. 7965.

Miscellaneous databases

EvolutionaryTraceiP30114.

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. "Inter-species variation of schistosome 28-kDa glutathione S-transferases."
    Trottein F., Goding G., Sellin B., Gorillot I., Samaio M., Lecocq J.-P., Capron A.
    Mol. Biochem. Parasitol. 54:63-72(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma haematobium."
    Johnson K.A., Angelucci F., Bellelli A., Herve M., Fontaine J., Tsernoglou D., Capron A., Trottein F., Brunori M.
    Biochemistry 42:10084-10094(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiGST28_SCHHA
AccessioniPrimary (citable) accession number: P30114
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1993
Last sequence update: March 31, 1993
Last modified: March 31, 2015
This is version 79 of the entry and version 1 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.