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P83246 (GST_ASADI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase

EC=2.5.1.18
Alternative name(s):
GST class-sigma
adGST
OrganismAsaphis dichotoma
Taxonomic identifier184428 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaHeteroconchiaVeneroidaTellinoideaPsammobiidaeAsaphis

Protein attributes

Sequence length15 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a strong specific activity toward 1-chloro-2,4-dinitrobenzene and ethacrynic acid. Ref.1

Catalytic activity

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

Subunit structure

Homodimer. Ref.1

Miscellaneous

In A.dichotoma there are at least two isozymes of glutathione S-transferase.

Sequence similarities

Belongs to the GST superfamily. Sigma family. UniProtKB P20137

Biophysicochemical properties

Kinetic parameters:

KM=0.68 mM for 1-chloro-2,4-dinitrobenzene

KM=0.106 mM for glutathione

Vmax=0.1446 mmol/min/mg enzyme toward CDNB

Vmax=0.033 mmol/min/mg enzyme toward GSH

pH dependence:

Optimum pH is 8.5 with 1-chloro-2,4-dinitrobenzene as substrate.

Mass spectrometry

Molecular mass is 23138 Da from positions 1 - ?. Determined by MALDI. Ref.1

Ontologies

Keywords
   Molecular functionTransferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionglutathione transferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›15›15Glutathione S-transferase
PRO_0000185923

Experimental info

Non-terminal residue151

Sequences

Sequence LengthMass (Da)Tools
P83246 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: CB3E4BF92D3CB0B9

FASTA151,767
        10 
PSYKLHYFDL RAAGE 

« Hide

References

[1]"Purification and characterization of a novel glutathione S-transferase from Asaphis dichotoma."
Yang H.-L., Nie L.-J., Zhu S.-G., Zhou X.-W.
Arch. Biochem. Biophys. 403:202-208(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY, CIRCULAR DICHROISM ANALYSIS.
Tissue: Gut and Liver.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameGST_ASADI
AccessionPrimary (citable) accession number: P83246
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2002
Last modified: April 3, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families