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Protein

Glutathione S-transferase

Gene
N/A
Organism
Nototodarus sloanii (Wellington flying squid) (Ommastrephes sloanei)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

High activity toward 1-chloro-2,4-dinitrobenzene. Not very efficient at catalyzing the addition of GSH to enones and epoxides.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Glutathione
Binding sitei39 – 391Glutathione
Binding sitei43 – 431Glutathione

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 (EC:2.5.1.18)
Alternative name(s):
GST class-sigma
OrganismiNototodarus sloanii (Wellington flying squid) (Ommastrephes sloanei)
Taxonomic identifieri215440 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaCephalopodaColeoideaNeocoleoideaDecapodiformesTeuthidaOegopsinaOmmastrephidaeNototodarus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071F → Y: Improves action on epones and epoxides.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Glutathione S-transferasePRO_0000185920Add
BLAST

Expressioni

Tissue specificityi

More abundant in the digestive gland than in the testis, mantle, or lens.

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi10 – 123Combined sources
Helixi13 – 153Combined sources
Helixi16 – 249Combined sources
Beta strandi30 – 334Combined sources
Turni36 – 383Combined sources
Helixi39 – 424Combined sources
Helixi43 – 453Combined sources
Helixi47 – 493Combined sources
Beta strandi53 – 564Combined sources
Beta strandi59 – 613Combined sources
Helixi64 – 7411Combined sources
Helixi82 – 10625Combined sources
Helixi113 – 13624Combined sources
Turni137 – 1404Combined sources
Beta strandi141 – 1433Combined sources
Helixi152 – 16716Combined sources
Turni169 – 1746Combined sources
Helixi176 – 18611Combined sources
Helixi189 – 1979Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GSQX-ray2.40A2-203[»]
2GSQX-ray2.20A2-203[»]
ProteinModelPortaliP46088.
SMRiP46088. Positions 2-203.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46088.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7978GST N-terminalAdd
BLAST
Domaini81 – 203123GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 513Glutathione binding
Regioni63 – 642Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Sigma 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.
IPR003083. S-crystallin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01269. SCRYSTALLIN.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46088-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKYTLHYFP LMGRAELCRF VLAAHGEEFT DRVVEMADWP NLKATMYSNA
60 70 80 90 100
MPVLDIDGTK MSQSMCIARH LAREFGLDGK TSLEKYRVDE ITETLQDIFN
110 120 130 140 150
DVVKIKFAPE AAKEAVQQNY EKSCKRLAPF LEGLLVSNGG GDGFFVGNSM
160 170 180 190 200
TLADLHCYVA LEVPLKHTPE LLKDCPKIVA LRKRVAECPK IAAYLKKRPV

RDF
Length:203
Mass (Da):22,919
Last modified:November 1, 1995 - v1
Checksum:iF46F56682F1C9591
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti124 – 1241C → Y.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02054
, L02053, L02052, L02051, L02050 Genomic DNA. Translation: AAA92066.1.
PIRiA45463.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02054
, L02053, L02052, L02051, L02050 Genomic DNA. Translation: AAA92066.1.
PIRiA45463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GSQX-ray2.40A2-203[»]
2GSQX-ray2.20A2-203[»]
ProteinModelPortaliP46088.
SMRiP46088. Positions 2-203.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP46088.

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.
IPR003083. S-crystallin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01269. SCRYSTALLIN.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Squid glutathione S-transferase. Relationships with other glutathione S-transferases and S-crystallins of cephalopods."
    Tomarev S.I., Zinovieva R.D., Guo K., Piatigorsky J.
    J. Biol. Chem. 268:4534-4542(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-60 AND 86-104.
    Strain: Pacificus.
    Tissue: Digestive gland.
  2. "Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods."
    Ji X., von Rosenvinge E.C., Johnson W.W., Tomarev S.I., Piatigorsky J., Armstrong R.N., Gilliland G.L.
    Biochemistry 34:5317-5328(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
  3. "Location of a potential transport binding site in a sigma class glutathione transferase by X-ray crystallography."
    Ji X., von Rosenvinge E.C., Johnson W.W., Armstrong R.N., Gilliland G.L.
    Proc. Natl. Acad. Sci. U.S.A. 93:8208-8213(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.

Entry informationi

Entry nameiGST_NOTSL
AccessioniPrimary (citable) accession number: P46088
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.