Reviewed,
UniProtKB/Swiss-Prot P46436 (GST1_ASCSU)
Last modified
January 19, 2010.
Version 40.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names 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 › 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 Ref.1 Non-traceable author statement. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
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: 8183318] [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: 9182731] [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 | |
| SMR | P46436. Positions 1-206. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.5.1.18. 649. |
Family and domain databases | |
| 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. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view] |
| 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) | ||||||||

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