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Reviewed, UniProtKB/Swiss-Prot P28593 (TYTR_TRYCR)

Last modified June 16, 2009. Version 81. 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

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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 lineageEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Schizotrypanum

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Protein attributes

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

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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.

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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...

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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

1 ....................................................................................... 492
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P28593-1 [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

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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: 2011150] [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: 7737173] [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: 8428618] [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: 8159665] [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: 8771196] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Strain: Silvio.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M38051 Genomic DNA. Translation: AAA63547.1.
Z13958 Genomic DNA. Translation: CAA78360.1.
PIRS68968.

3D structure databases

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[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.8.1.12. 884.

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...

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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: June 16, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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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