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Reviewed, UniProtKB/Swiss-Prot P46429 (GST2_MANSE)

Last modified January 19, 2010. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutathione S-transferase 2
    EC=2.5.1.18
Alternative name(s):
    GST class-sigma
Gene names
Name: GST2
OrganismManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifier7130 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

Protein attributes

Sequence length203 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Induction

By dietary chemicals.

Sequence similarities

Belongs to the GST superfamily. Sigma family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Molecular functionTransferase
Gene Ontology (GO)
   Molecular functionglutathione transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 203203Glutathione S-transferase 2
PRO_0000185918

Regions

Domain1 – 7878GST N-terminal
Domain80 – 203124GST C-terminal

Sequences

Sequence LengthMass (Da)Tools
P46429-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: D5EC67F119DE470D

FASTA20323,596
        10         20         30         40         50         60 
MPKVVFHYFG AKGWARPTML LAYGGQEFED HRVEYEQWPE FKPNTPFGQM PVLEIDGKKY 

        70         80         90        100        110        120 
AQSLAISRYL GRKYGLAGND IEEDFEIDQI VDFVNDIRAS AASVEYEQDA ANKEVKHEEN 

       130        140        150        160        170        180 
MKNKYPFQLN KLSEIITKNN GFLALGRLTW ADFVFVGMFD YLKKMLRMPD LEEQYPIFKK 

       190        200 
PIETVLSNPK LKAYLDSAPK KEF 

« Hide

References

[1]"Glutathione S-transferases from larval Manduca sexta midgut: sequence of two cDNAs and enzyme induction."
Snyder M.J., Walding J.K., Feyereisen R.
Insect Biochem. Mol. Biol. 25:455-465(1995) [PubMed: 7742833] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Midgut.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L32092 mRNA. Translation: AAA92881.1.

3D structure databases

SMRP46429. Positions 1-203.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.5.1.18. 15145.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGST2_MANSE
AccessionPrimary (citable) accession number: P46429
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 19, 2010
This is version 49 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents