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Protein

Glutathione S-transferase 1

Gene

GST1

Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can also function as a GSH peroxidase.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei8GlutathioneBy similarity1
Binding sitei39GlutathioneBy similarity1
Binding sitei43GlutathioneBy similarity1

GO - Molecular functioni

  • glutathione peroxidase activity Source: WormBase
  • glutathione transferase activity Source: UniProtKB

GO - Biological processi

  • oxidation-reduction process Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 474.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 1 (EC:2.5.1.18)
Alternative name(s):
GST class-sigma
Gene namesi
Name:GST1
OrganismiAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifieri6253 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

Subcellular locationi

GO - Cellular componenti

  • brush border Source: WormBase
  • cytoplasm Source: WormBase
Complete GO annotation...

Pathology & Biotechi

Protein family/group databases

Allergomei10991. Asc l 13.
10992. Asc l 13.0101.
11669. Asc s 13.0101.
7680. Asc s 13.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001859222 – 206Glutathione S-transferase 1Add BLAST205

Structurei

Secondary structure

1206
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Turni13 – 15Combined sources3
Helixi16 – 24Combined sources9
Beta strandi30 – 34Combined sources5
Helixi36 – 38Combined sources3
Helixi39 – 42Combined sources4
Helixi43 – 45Combined sources3
Beta strandi46 – 49Combined sources4
Beta strandi53 – 56Combined sources4
Beta strandi59 – 62Combined sources4
Helixi64 – 74Combined sources11
Helixi82 – 102Combined sources21
Helixi103 – 105Combined sources3
Helixi106 – 110Combined sources5
Helixi117 – 123Combined sources7
Helixi125 – 143Combined sources19
Beta strandi145 – 152Combined sources8
Helixi155 – 170Combined sources16
Turni172 – 177Combined sources6
Helixi179 – 190Combined sources12
Helixi192 – 200Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Q5FX-ray2.45A/D1-206[»]
ProteinModelPortaliP46436.
SMRiP46436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 79GST N-terminalAdd BLAST78
Domaini81 – 206GST C-terminalAdd BLAST126

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 51Glutathione bindingBy similarity3
Regioni63 – 64Glutathione bindingBy similarity2

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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46436-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQYKLTYFD IRGLGEGARL IFHQAGVKFE DNRLKREDWP ALKPKTPFGQ
60 70 80 90 100
LPLLEVDGEV LAQSAAIYRY LGRQFGLAGK TPMEEAQVDS IFDQFKDFMA
110 120 130 140 150
ELRPCFRVLA GFEEGDKEKV LKEVAVPARD KHLPLLEKFL AKSGSEYMVG
160 170 180 190 200
KSVTWADLVI TDSLASWESL IPDFLSGHLQ LKKYIEHVRE LPNIKKWIAE

RPKTPY
Length:206
Mass (Da):23,585
Last modified:January 23, 2007 - v3
Checksum:iB8366238A63DF399
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75502 mRNA. Translation: CAA53218.1.
Y10613 Genomic DNA. Translation: CAA71620.1.
PIRiS38626.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75502 mRNA. Translation: CAA53218.1.
Y10613 Genomic DNA. Translation: CAA71620.1.
PIRiS38626.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Q5FX-ray2.45A/D1-206[»]
ProteinModelPortaliP46436.
SMRiP46436.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei10991. Asc l 13.
10992. Asc l 13.0101.
11669. Asc s 13.0101.
7680. Asc s 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.5.1.18. 474.

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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGST1_ASCSU
AccessioniPrimary (citable) accession number: P46436
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 68 of the entry and version 3 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.