Reviewed,
UniProtKB/Swiss-Prot P39051 (TYTR_TRYBB)
Last modified
June 16, 2009.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Trypanothione reductase Short name=TR EC=1.8.1.12 Alternative name(s): N(1),N(8)-bis(glutathionyl)spermidine reductase | ||
| Gene names |
| ||
| Organism | Trypanosoma brucei brucei | ||
| Taxonomic identifier | 5702 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma |
Protein attributes
| Sequence length | 492 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase. |
| Catalytic activity | Trypanothione + NADP+ = trypanothione disulfide + NADPH. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Miscellaneous | The active site is a redox-active disulfide bond. |
| Sequence similarities | Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro disulfide oxidoreductase activityInferred from electronic annotation. Source: InterPro trypanothione-disulfide reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 492 | 492 | Trypanothione reductase | PRO_0000067990 | |||||||
Regions | |||||||||||
| Nucleotide binding | 35 – 52 | 18 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 461 | 1 | Proton acceptor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 52 ↔ 57 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Molecular characterization of the trypanothione reductase gene from Crithidia fasciculata and Trypanosoma brucei: comparison with other flavoprotein disulphide oxidoreductases with respect to substrate specificity and catalytic mechanism." Aboagye-Kwarteng T., Smith K., Fairlamb A.H. Mol. Microbiol. 6:3089-3099(1992) [PubMed: 1453951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ILTAT 1.1. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X63188 Genomic DNA. Translation: CAA44870.1. | |||||||||||||
| PIR | S28003. | ||||||||||||
3D structure databases | |||||||||||||
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| SMR | P39051. Positions 2-485. | ||||||||||||
| ModBase | Search... | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 1.8.1.12. 74165. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. IPR001864. Trypnth_redctse. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. | ||||||||||||
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00368. FADPNR. | ||||||||||||
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| TIGRFAMs | TIGR01423. trypano_reduc. 1 hit. | ||||||||||||
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | TYTR_TRYBB | ||||||||
| Accession | Primary (citable) accession number: P39051 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


