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P46088

- GST_NOTSL

UniProt

P46088 - GST_NOTSL

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Protein
Glutathione S-transferase
Gene
N/A
Organism
Nototodarus sloanii (Wellington flying squid) (Ommastrephes sloanei)
Status
Reviewed - 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-transferase
PRO_0000185920Add
BLAST

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GSQX-ray2.40A2-203[»]
2GSQX-ray2.20A2-203[»]
ProteinModelPortaliP46088.
SMRiP46088. Positions 2-203.

Miscellaneous databases

EvolutionaryTraceiP46088.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the GST superfamily. Sigma family.

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

MPKYTLHYFP LMGRAELCRF VLAAHGEEFT DRVVEMADWP NLKATMYSNA    50
MPVLDIDGTK MSQSMCIARH LAREFGLDGK TSLEKYRVDE ITETLQDIFN 100
DVVKIKFAPE AAKEAVQQNY EKSCKRLAPF LEGLLVSNGG GDGFFVGNSM 150
TLADLHCYVA LEVPLKHTPE LLKDCPKIVA LRKRVAECPK IAAYLKKRPV 200
RDF 203
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L02054
, L02053 , L02052 , L02051 , L02050 Genomic DNA. Translation: AAA92066.1 .
PIRi A45463.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GSQ X-ray 2.40 A 2-203 [» ]
2GSQ X-ray 2.20 A 2-203 [» ]
ProteinModelPortali P46088.
SMRi P46088. Positions 2-203.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P46088.

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.
IPR003083. S-crystallin.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01269. SCRYSTALLIN.
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. "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: April 16, 2014
This is version 82 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

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