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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)DescriptionActionsGraphical viewLength
Binding sitei8Glutathione1 Publication1
Binding sitei39Glutathione2 Publications1
Binding sitei43Glutathione2 Publications1

GO - Molecular functioni

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107F → Y: Improves action on epones and epoxides. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001859201 – 203Glutathione S-transferaseAdd BLAST203

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

1203
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi10 – 12Combined sources3
Helixi13 – 15Combined sources3
Helixi16 – 24Combined sources9
Beta strandi30 – 33Combined sources4
Turni36 – 38Combined sources3
Helixi39 – 42Combined sources4
Helixi43 – 45Combined sources3
Helixi47 – 49Combined sources3
Beta strandi53 – 56Combined sources4
Beta strandi59 – 61Combined sources3
Helixi64 – 74Combined sources11
Helixi82 – 106Combined sources25
Helixi113 – 136Combined sources24
Turni137 – 140Combined sources4
Beta strandi141 – 143Combined sources3
Helixi152 – 167Combined sources16
Turni169 – 174Combined sources6
Helixi176 – 186Combined sources11
Helixi189 – 197Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP46088.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 79GST N-terminalAdd BLAST78
Domaini81 – 203GST C-terminalAdd BLAST123

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 51Glutathione binding2 Publications3
Regioni63 – 64Glutathione binding2 Publications2

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]
PfamiPF14497. GST_C_3. 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)DescriptionActionsGraphical viewLength
Natural varianti124C → Y.1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GSQX-ray2.40A2-203[»]
2GSQX-ray2.20A2-203[»]
ProteinModelPortaliP46088.
SMRiP46088.
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]
PfamiPF14497. GST_C_3. 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...

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: November 2, 2016
This is version 91 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

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 one 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.