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P28593

- TYTR_TRYCR

UniProt

P28593 - TYTR_TRYCR

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Protein
Trypanothione reductase
Gene
TPR
Organism
Trypanosoma cruzi
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.

Catalytic activityi

Trypanothione + NADP+ = trypanothione disulfide + NADPH.

Cofactori

Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei461 – 4611Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 5217FAD
Add
BLAST

GO - Molecular functioni

  1. disulfide oxidoreductase activity Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro
  3. trypanothione-disulfide reductase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Trypanothione reductase (EC:1.8.1.12)
Short name:
TR
Alternative name(s):
N(1),N(8)-bis(glutathionyl)spermidine reductase
Gene namesi
Name:TPR
OrganismiTrypanosoma cruzi
Taxonomic identifieri5693 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Trypanothione reductase
PRO_0000067992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 58Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117
Helixi15 – 2612
Beta strandi32 – 376
Beta strandi39 – 424
Turni43 – 453
Helixi51 – 566
Helixi58 – 7619
Helixi77 – 804
Helixi86 – 883
Helixi93 – 11725
Beta strandi121 – 13212
Beta strandi135 – 1439
Beta strandi148 – 1558
Beta strandi157 – 1593
Beta strandi163 – 1653
Helixi173 – 1753
Helixi179 – 1824
Beta strandi190 – 1956
Helixi199 – 21113
Beta strandi217 – 22812
Helixi233 – 24513
Beta strandi249 – 2535
Beta strandi256 – 2616
Beta strandi267 – 2715
Beta strandi276 – 2849
Beta strandi288 – 2903
Helixi293 – 2953
Helixi297 – 2993
Beta strandi306 – 3094
Beta strandi322 – 3243
Helixi326 – 3294
Helixi335 – 35016
Beta strandi351 – 3533
Beta strandi364 – 3663
Beta strandi372 – 3765
Helixi379 – 3857
Beta strandi387 – 39610
Helixi399 – 4046
Beta strandi411 – 4188
Turni419 – 4213
Beta strandi423 – 4319
Helixi434 – 44613
Helixi451 – 4555
Helixi465 – 4695
Beta strandi475 – 4795
Beta strandi482 – 4843

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP28593.
SMRiP28593. Positions 5-485.

Miscellaneous databases

EvolutionaryTraceiP28593.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. 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]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
PR00470. TRYPANRDTASE.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01423. trypano_reduc. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28593-1 [UniParc]FASTAAdd to Basket

« Hide

MMSKIFDLVV IGAGSGGLEA AWNAATLYKK RVAVIDVQMV HGPPFFSALG    50
GTCVNVGCVP KKLMVTGAQY MEHLRESAGF GWEFDRTTLR AEWKKLIAVK 100
DEAVLNINKS YEEMFRDTEG LEFFLGWGSL ESKNVVNVRE SADPASAVKE 150
RLETENILLA SGSWPHMPNI PGIEHCISSN EAFYLPEPPR RVLTVGGGFI 200
SVEFAGIFNA YKPKDGQVTL CYRGEMILRG FDHTLREELT KQLTANGIQI 250
LTKENPAKVE LNADGSKSVT FESGKKMDFD LVMMAIGRSP RTKDLQLQNA 300
GVMIKNGGVQ VDEYSRTNVS NIYAIGDVTN RVMLTPVAIN EAAALVDTVF 350
GTNPRKTDHT RVASAVFSIP PIGTCGLIEE VASKRYEVVA VYLSSFTPLM 400
HNISGSKYKT FVAKIITNHS DGTVLGVHLL GDNAPEIIQG VGICLKLNAK 450
ISDFYNTIGV HPTSAEELCS MRTPSYYYVK GEKMEKPSEA SL 492
Length:492
Mass (Da):53,868
Last modified:December 1, 1992 - v1
Checksum:i4AF179952A20750F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951K → N in strain: Silvio.
Natural varianti140 – 1401E → A in strain: Silvio.
Natural varianti156 – 1561N → H in strain: Silvio.
Natural varianti353 – 3531N → T in strain: Silvio.
Natural varianti402 – 4032NI → KV in strain: Silvio.
Natural varianti441 – 4411V → I in strain: Silvio.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M38051 Genomic DNA. Translation: AAA63547.1.
Z13958 Genomic DNA. Translation: CAA78360.1.
PIRiS68968.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M38051 Genomic DNA. Translation: AAA63547.1 .
Z13958 Genomic DNA. Translation: CAA78360.1 .
PIRi S68968.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AOG X-ray 2.30 A/B 3-487 [» ]
1BZL X-ray 2.40 A/B 2-487 [» ]
1GXF X-ray 2.70 A/B 1-492 [» ]
1NDA X-ray 3.30 A/B/C/D 2-492 [» ]
ProteinModelPortali P28593.
SMRi P28593. Positions 5-485.
ModBasei Search...

Chemistry

BindingDBi P28593.
ChEMBLi CHEMBL5131.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P28593.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. 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 ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
PR00470. TRYPANRDTASE.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01423. trypano_reduc. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiTYTR_TRYCR
AccessioniPrimary (citable) accession number: P28593
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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