O60993 (TRYS_CRIFA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 47.
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: Trypanothione synthetase EC=6.3.1.9 Alternative name(s): Cf-TS | ||
| Gene names |
| ||
| Organism | Crithidia fasciculata | ||
| Taxonomic identifier | 5656 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Crithidia![]() |
Protein attributes
| Sequence length | 652 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Conjugates glutathione (gamma-Glu-Cys-Gly) and glutathionylspermidine to form trypanothione (N1,N(8)-bis(glutathionyl)spermidine), which is involved in maintaining intracellular thiol redox and in defense against oxidants. |
| Catalytic activity | Glutathione + glutathionylspermidine + ATP = N1,N(8)-bis-(glutathionyl)spermidine + ADP + phosphate. |
| Cofactor | Magnesium. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Contains 1 peptidase C51 domain. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Magnesium Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW trypanothione synthase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and characterization of the two enzymes responsible for trypanothione biosynthesis in Crithidia fasciculata." Tetaud E., Manai F., Barrett M.P., Nadeau K., Walsh C.T., Fairlamb A.H. J. Biol. Chem. 273:19383-19390(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 168-191; 232-255; 437-450; 457-474; 592-610 AND 617-630. Strain: HS6. |
| [2] | "Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata." Smith K., Nadeau K., Bradley M., Walsh C., Fairlamb A.H. Protein Sci. 1:874-883(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 168-191; 232-255; 437-450; 457-474; 592-610 AND 617-630, CHARACTERIZATION. |
| [3] | "Convenient isolation and kinetic mechanism of glutathionylspermidine synthetase from Crithidia fasciculata." Koenig K., Menge U., Kiess M., Wray V., Flohe L. J. Biol. Chem. 272:11908-11915(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-36; 224-229; 235-242; 515-533; 550-561 AND 617-629, CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF006615 Genomic DNA. Translation: AAC39132.1. |
3D structure databases | |
| ProteinModelPortal | O60993. |
| SMR | O60993. Positions 1-632. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C51.A01. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| SABIO-RK | O60993. |
Family and domain databases | |
| InterPro | IPR007921. CHAP. IPR005494. GSPS_pre-ATP-grasp-like_dom. IPR016185. PreATP-grasp_dom. [Graphical view] |
| Pfam | PF05257. CHAP. 1 hit. PF03738. GSP_synth. 1 hit. [Graphical view] |
| SUPFAM | SSF52440. PreATP-grasp-like. 1 hit. |
| PROSITE | PS50911. CHAP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TRYS_CRIFA | ||||||||
| Accession | Primary (citable) accession number: O60993 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
