Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P28593 (TYTR_TRYCR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 cruzi
Taxonomic identifier5693 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
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.

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

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondisulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

trypanothione-disulfide reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Trypanothione reductase
PRO_0000067992

Regions

Nucleotide binding36 – 5217FAD

Sites

Active site4611Proton acceptor By similarity

Amino acid modifications

Disulfide bond53 ↔ 58Redox-active Ref.3

Natural variations

Natural variant951K → N in strain: Silvio.
Natural variant1401E → A in strain: Silvio.
Natural variant1561N → H in strain: Silvio.
Natural variant3531N → T in strain: Silvio.
Natural variant402 – 4032NI → KV in strain: Silvio.
Natural variant4411V → I in strain: Silvio.

Secondary structure

......................................................................................... 492
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28593 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 4AF179952A20750F

FASTA49253,868
        10         20         30         40         50         60 
MMSKIFDLVV IGAGSGGLEA AWNAATLYKK RVAVIDVQMV HGPPFFSALG GTCVNVGCVP 

        70         80         90        100        110        120 
KKLMVTGAQY MEHLRESAGF GWEFDRTTLR AEWKKLIAVK DEAVLNINKS YEEMFRDTEG 

       130        140        150        160        170        180 
LEFFLGWGSL ESKNVVNVRE SADPASAVKE RLETENILLA SGSWPHMPNI PGIEHCISSN 

       190        200        210        220        230        240 
EAFYLPEPPR RVLTVGGGFI SVEFAGIFNA YKPKDGQVTL CYRGEMILRG FDHTLREELT 

       250        260        270        280        290        300 
KQLTANGIQI LTKENPAKVE LNADGSKSVT FESGKKMDFD LVMMAIGRSP RTKDLQLQNA 

       310        320        330        340        350        360 
GVMIKNGGVQ VDEYSRTNVS NIYAIGDVTN RVMLTPVAIN EAAALVDTVF GTNPRKTDHT 

       370        380        390        400        410        420 
RVASAVFSIP PIGTCGLIEE VASKRYEVVA VYLSSFTPLM HNISGSKYKT FVAKIITNHS 

       430        440        450        460        470        480 
DGTVLGVHLL GDNAPEIIQG VGICLKLNAK ISDFYNTIGV HPTSAEELCS MRTPSYYYVK 

       490 
GEKMEKPSEA SL 

« Hide

References

[1]"Cloning, sequencing, overproduction and purification of trypanothione reductase from Trypanosoma cruzi."
Sullivan F.X., Walsh C.T.
Mol. Biochem. Parasitol. 44:145-148(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Site-directed mutagenesis of the redox-active cysteines of Trypanosoma cruzi trypanothione reductase."
Borges A., Cunningham M.L., Tover J., Fairlamb A.H.
Eur. J. Biochem. 228:745-752(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Silvio.
[3]"Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease."
Krauth-Siegel R.L., Sticherling C., Jost I., Walsh C.T., Pai E.F., Kabsch W., Lantwin C.B.
FEBS Lett. 317:105-108(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 2-492, DISULFIDE BOND.
[4]"The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state."
Lantwin C.B., Schlichting I., Kabsch W., Pai E.F., Krauth-Siegel R.L.
Proteins 18:161-173(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
[5]"The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3-A resolution."
Zhang Y., Bond C.S., Bailey S., Cunningham M.L., Fairlamb A.H., Hunter W.N.
Protein Sci. 5:52-61(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Strain: Silvio.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M38051 Genomic DNA. Translation: AAA63547.1.
Z13958 Genomic DNA. Translation: CAA78360.1.
PIRS68968.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOGX-ray2.30A/B3-487[»]
1BZLX-ray2.40A/B2-487[»]
1GXFX-ray2.70A/B1-492[»]
1NDAX-ray3.30A/B/C/D2-492[»]
ProteinModelPortalP28593.
SMRP28593. Positions 5-485.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP28593.
ChEMBLCHEMBL5131.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR001864. Trypnth_redctse.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00470. TRYPANRDTASE.
SUPFAMSSF55424. SSF55424. 1 hit.
TIGRFAMsTIGR01423. trypano_reduc. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP28593.

Entry information

Entry nameTYTR_TRYCR
AccessionPrimary (citable) accession number: P28593
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references