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P46088

- GST_NOTSL

UniProt

P46088 - GST_NOTSL

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
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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

    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

    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 – 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.
    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

    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: October 1, 2014
    This is version 83 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