P46436 (GST1_ASCSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 52.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glutathione S-transferase 1 EC=2.5.1.18 Alternative name(s): GST class-sigma | ||
| Gene names |
| ||
| Organism | Ascaris suum (Pig roundworm) (Ascaris lumbricoides) | ||
| Taxonomic identifier | 6253 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Ascaridida › Ascaridoidea › Ascarididae › Ascaris![]() |
Protein attributes
| Sequence length | 206 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can also function as a GSH peroxidase. |
| Catalytic activity | RX + glutathione = HX + R-S-glutathione. |
| Sequence similarities | Belongs to the GST superfamily. Sigma family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Transferase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular_function | glutathione transferase activity Non-traceable author statement Ref.1. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.1 | ||||||
| Chain | 2 – 206 | 205 | Glutathione S-transferase 1 | PRO_0000185922 | |||||
Regions | |||||||||
| Domain | 2 – 79 | 78 | GST N-terminal | ||||||
| Domain | 81 – 206 | 126 | GST C-terminal | ||||||
| Region | 50 – 51 | 2 | Glutathione binding By similarity | ||||||
| Region | 63 – 64 | 2 | Glutathione binding By similarity | ||||||
Sites | |||||||||
| Binding site | 8 | 1 | Glutathione By similarity | ||||||
| Binding site | 39 | 1 | Glutathione By similarity | ||||||
| Binding site | 43 | 1 | Glutathione By similarity | ||||||
Sequences
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References
| [1] | "Molecular cloning and expression of a cDNA encoding glutathione S-transferase from Ascaris suum." Liebau E., Schoenberger O.L., Walter R.D., Henkle-Duehrsen K.J. Mol. Biochem. Parasitol. 63:167-170(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 2-41. |
| [2] | "Structural and functional analysis of a glutathione S-transferase from Ascaris suum." Liebau E., Eckelt V.H., Wildenburg G., Teesdale-Spittle P., Brophy P.M., Walter R.D., Henkle-Duehrsen K. Biochem. J. 324:659-666(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X75502 mRNA. Translation: CAA53218.1. Y10613 Genomic DNA. Translation: CAA71620.1. |
| PIR | S38626. |
3D structure databases | |
| ProteinModelPortal | P46436. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 1.20.1050.10. 1 hit. 3.40.30.10. 1 hit. |
| InterPro | IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| Pfam | PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view] |
| SUPFAM | SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit. |
| PROSITE | PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GST1_ASCSU | ||||||||
| Accession | Primary (citable) accession number: P46436 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
