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UniProtKB/Swiss-Prot entry P28593

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TYTR_TRYCR
Primary accession number P28593
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 75)
Name and origin of the protein
Protein name Trypanothione reductase
Synonyms TR
EC 1.8.1.12
N(1),N(8)-bis(glutathionyl)spermidine reductase
Gene name
Name: TPR
From
Trypanosoma cruzi [TaxID: 5693] 
Taxonomy Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0166-6851(91)90231-T; PubMed=2011150 [NCBI, ExPASy, EBI, Israel, Japan]
Sullivan F.X., Walsh C.T.;
"Cloning, sequencing, overproduction and purification of trypanothione reductase from Trypanosoma cruzi.";
Mol. Biochem. Parasitol. 44:145-148(1991).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Silvio;
PubMed=7737173 [NCBI, ExPASy, EBI, Israel, Japan]
Borges A., Cunningham M.L., Tover J., Fairlamb A.H.;
"Site-directed mutagenesis of the redox-active cysteines of Trypanosoma cruzi trypanothione reductase.";
Eur. J. Biochem. 228:745-752(1995).
[3]
 X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 2-492, AND DISULFIDE BOND.
DOI=10.1016/0014-5793(93)81501-P; PubMed=8428618 [NCBI, ExPASy, EBI, Israel, Japan]
Krauth-Siegel R.L., Sticherling C., Jost I., Walsh C.T., Pai E.F., Kabsch W., Lantwin C.B.;
"Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease.";
FEBS Lett. 317:105-108(1993).
[4]
 X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
DOI=10.1002/prot.340180208; PubMed=8159665 [NCBI, ExPASy, EBI, Israel, Japan]
Lantwin C.B., Schlichting I., Kabsch W., Pai E.F., Krauth-Siegel R.L.;
"The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state.";
Proteins 18:161-173(1994).
[5]
 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
STRAIN=Silvio;
PubMed=8771196 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Bond C.S., Bailey S., Cunningham M.L., Fairlamb A.H., Hunter W.N.;
"The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3-A resolution.";
Protein Sci. 5:52-61(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M38051; AAA63547.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z13958; CAA78360.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S68968; S68968.
3D structure databases
PDB
1AOG; X-ray; 2.30 A; A/B=3-487.[ExPASy / RCSB / EBI]
1BZL; X-ray; 2.40 A; A/B=2-487.[ExPASy / RCSB / EBI]
1GXF; X-ray; 2.70 A; A/B=1-492.[ExPASy / RCSB / EBI]
1NDA; X-ray; 3.30 A; A/B/C/D=2-492.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AOG; -.
1BZL; -.
1GXF; -.
1NDA; -.
ModBase P28593.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0015036; Molecular function: disulfide oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0015042; Molecular function: trypanothione-disulfide reductase activity (inferred from electronic annotation from EC).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR001864; Trypnth_redctse.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.
PR00470; TRYPANRDTASE.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01423; trypano_reduc; 1.
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
ProtoNet P28593.
Other
LinkHub P28593; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   492  492     Trypanothione reductase. PRO_0000067992
NP_BIND   36    52  17     FAD. 
ACT_SITE   461   461        Proton acceptor (By similarity). 
DISULFID   53    58        Redox-active. 
VARIANT   95    95  1     K -> N (in strain: Silvio). 
VARIANT   140   140  1     E -> A (in strain: Silvio). 
VARIANT   156   156  1     N -> H (in strain: Silvio). 
VARIANT   353   353  1     N -> T (in strain: Silvio). 
VARIANT   402   403  2     NI -> KV (in strain: Silvio). 
VARIANT   441   441  1     V -> I (in strain: Silvio). 
STRAND   5    11  7      
HELIX   15    26  12      
STRAND   32    37  6      
STRAND   39    42  4      
TURN   43    45  3      
HELIX   51    56  6      
HELIX   58    76  19      
HELIX   77    80  4      
HELIX   86    88  3      
HELIX   93   117  25      
STRAND   121   132  12      
STRAND   135   143  9      
STRAND   148   155  8      
STRAND   157   159  3      
STRAND   163   165  3      
HELIX   173   175  3      
HELIX   179   182  4      
STRAND   190   195  6      
HELIX   199   211  13      
STRAND   217   228  12      
HELIX   233   245  13      
STRAND   249   253  5      
STRAND   256   261  6      
STRAND   267   271  5      
STRAND   276   284  9      
STRAND   288   290  3      
HELIX   293   295  3      
HELIX   297   299  3      
STRAND   322   324  3      
HELIX   326   329  4      
HELIX   335   350  16      
STRAND   351   353  3      
STRAND   364   366  3      
STRAND   372   376  5      
HELIX   379   385  7      
STRAND   387   396  10      
HELIX   399   404  6      
STRAND   411   418  8      
TURN   419   421  3      
STRAND   423   431  9      
HELIX   434   446  13      
HELIX   451   455  5      
HELIX   465   469  5      
STRAND   475   479  5      
STRAND   482   484  3      
Sequence information
Length: 492 AA [This is the length of the unprocessed precursor] Molecular weight: 53868 Da [This is the MW of the unprocessed precursor] CRC64: 4AF179952A20750F [This is a checksum on the sequence] 
        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
P28593 in FASTA format

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