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P30113

- GST28_SCHBO

UniProt

P30113 - GST28_SCHBO

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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: 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 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

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):
Sb28GST
OrganismiSchistosoma bovis (Blood fluke)
Taxonomic identifieri6184 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101Y → F: Loss of enzyme activity. 1 Publication
Mutagenesisi21 – 211R → L: Reduces catalytic activity 12-fold. 1 Publication
Mutagenesisi21 – 211R → Q: Reduces catalytic activity 120-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Glutathione S-transferase class-mu 28 kDa isozymePRO_0000185812Add
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 – 117
Turni13 – 175
Helixi18 – 2710
Beta strandi32 – 354
Turni38 – 403
Turni42 – 443
Helixi45 – 473
Beta strandi53 – 597
Beta strandi65 – 695
Helixi71 – 8111
Helixi89 – 11022
Helixi117 – 12913
Helixi131 – 14414
Beta strandi147 – 1526
Helixi158 – 17316
Helixi183 – 19513
Helixi197 – 2037

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 4-211.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30113.

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.

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 AAA29892.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87799 Genomic DNA. Translation: AAA29892.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87799 Genomic DNA. Translation: AAA29892.1 . Different initiation.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C80 X-ray 2.30 A/B 1-211 [» ]
2C8U X-ray 2.00 A/B 1-211 [» ]
2CA8 X-ray 2.49 A 1-211 [» ]
2CAI X-ray 2.26 A/B 1-211 [» ]
2CAQ X-ray 2.00 A 1-211 [» ]
2F8F X-ray 2.10 A/B 1-211 [» ]
ProteinModelPortali P30113.
SMRi P30113. Positions 4-211.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P30113.

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. "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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography."
    Baiocco P., Gourlay L.J., Angelucci F., Fontaine J., Herve M., Miele A.E., Trottein F., Brunori M., Bellelli A.
    J. Mol. Biol. 360:678-689(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT, MUTAGENESIS OF TYR-10 AND ARG-21.

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: October 29, 2014
This is version 82 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

External Data

Dasty 3