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Reviewed, UniProtKB/Swiss-Prot P39051 (TYTR_TRYBB)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Trypanothione reductase
      Short name=TR
    EC=1.8.1.12
Alternative name(s):
    N(1),N(8)-bis(glutathionyl)spermidine reductase
Gene names
Name: TPR
OrganismTrypanosoma brucei brucei
Taxonomic identifier5702 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Cytoplasm.

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 componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

trypanothione-disulfide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Trypanothione reductase
PRO_0000067990

Regions

Nucleotide binding35 – 5218FAD By similarity

Sites

Active site4611Proton acceptor By similarity

Amino acid modifications

Disulfide bond52 ↔ 57Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P39051-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: FFCA2F11B66F7FF4

FASTA49253,284
        10         20         30         40         50         60 
MSKIFDLVVI GAGSGGLEAG WNAATLYKKR VAVIDVQTHH GPPHYAALGG TCVNVGCVPK 

        70         80         90        100        110        120 
KLMVTGAQYM DHLRESAGFG WEFDGSSVKA NWKKLIAAKN EAVLDINKSY EGMFNDTEGL 

       130        140        150        160        170        180 
DFFLGWGSLE SKNVVVVRET ADPKSAVKER LQADHILLAT GSWPQMPAIP GVEHCISSNE 

       190        200        210        220        230        240 
AFYLPEPPRR VLTVGGGFIS VEFAGIFNAY KPPGGKVTLC YRNNLILRGF DETIREEVTK 

       250        260        270        280        290        300 
QLTANGIEIM TNENPAKVSL NTDGSKHVTF ESGKTLDVDV VMMAIGRIPR TNDLQLGNVG 

       310        320        330        340        350        360 
VKLTPKGGVQ VDEFSRTNVP NIYAIGDITD RLMLTPVAIN EGAALVDTVF GNKPRKTDHT 

       370        380        390        400        410        420 
RVASAVFSIP PIGTCGLIEE VAAKEFEKVA VYMSSFTPLM HNISGSKYKK FVAKIVTNHS 

       430        440        450        460        470        480 
DGTVLGVHLL GDGAPEIIQA VGVCLRLNAK ISDFYNTIGV HPTSAEELCS MRTPSYYYLK 

       490 
GEKMETLPES SL 

« Hide

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.
PIRS28003.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2VE2X-ray2.30A/B1-490[»]
SMRP39051. Positions 2-485.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.8.1.12. 74165.

Family and domain databases

InterProIPR013027. 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]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01423. trypano_reduc. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTYTR_TRYBB
AccessionPrimary (citable) accession number: P39051
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents