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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

FADNote: Binds 1 FAD per subunit.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 5217FADAdd
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

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-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Trypanothione reductasePRO_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

1
492
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Helixi15 – 2612Combined sources
Beta strandi32 – 376Combined sources
Beta strandi39 – 424Combined sources
Turni43 – 453Combined sources
Helixi51 – 566Combined sources
Helixi58 – 7619Combined sources
Helixi77 – 804Combined sources
Helixi86 – 883Combined sources
Helixi93 – 11725Combined sources
Beta strandi121 – 13212Combined sources
Beta strandi135 – 1439Combined sources
Beta strandi148 – 1558Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi163 – 1653Combined sources
Helixi173 – 1753Combined sources
Helixi179 – 1824Combined sources
Beta strandi190 – 1956Combined sources
Helixi199 – 21113Combined sources
Beta strandi217 – 22812Combined sources
Helixi233 – 24513Combined sources
Beta strandi249 – 2535Combined sources
Beta strandi256 – 2616Combined sources
Beta strandi267 – 2715Combined sources
Beta strandi276 – 2849Combined sources
Beta strandi288 – 2903Combined sources
Helixi293 – 2953Combined sources
Helixi297 – 2993Combined sources
Beta strandi306 – 3094Combined sources
Beta strandi322 – 3243Combined sources
Helixi326 – 3294Combined sources
Helixi335 – 35016Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi372 – 3765Combined sources
Helixi379 – 3857Combined sources
Beta strandi387 – 39610Combined sources
Helixi399 – 4046Combined sources
Beta strandi411 – 4188Combined sources
Turni419 – 4213Combined sources
Beta strandi423 – 4319Combined sources
Helixi434 – 44613Combined sources
Helixi451 – 4555Combined sources
Helixi465 – 4695Combined sources
Beta strandi475 – 4795Combined sources
Beta strandi482 – 4843Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MMSKIFDLVV IGAGSGGLEA AWNAATLYKK RVAVIDVQMV HGPPFFSALG
60 70 80 90 100
GTCVNVGCVP KKLMVTGAQY MEHLRESAGF GWEFDRTTLR AEWKKLIAVK
110 120 130 140 150
DEAVLNINKS YEEMFRDTEG LEFFLGWGSL ESKNVVNVRE SADPASAVKE
160 170 180 190 200
RLETENILLA SGSWPHMPNI PGIEHCISSN EAFYLPEPPR RVLTVGGGFI
210 220 230 240 250
SVEFAGIFNA YKPKDGQVTL CYRGEMILRG FDHTLREELT KQLTANGIQI
260 270 280 290 300
LTKENPAKVE LNADGSKSVT FESGKKMDFD LVMMAIGRSP RTKDLQLQNA
310 320 330 340 350
GVMIKNGGVQ VDEYSRTNVS NIYAIGDVTN RVMLTPVAIN EAAALVDTVF
360 370 380 390 400
GTNPRKTDHT RVASAVFSIP PIGTCGLIEE VASKRYEVVA VYLSSFTPLM
410 420 430 440 450
HNISGSKYKT FVAKIITNHS DGTVLGVHLL GDNAPEIIQG VGICLKLNAK
460 470 480 490
ISDFYNTIGV HPTSAEELCS MRTPSYYYVK GEKMEKPSEA SL
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:
EMBLi
GenBanki
DDBJi
Links Updated
M38051 Genomic DNA. Translation: AAA63547.1.
Z13958 Genomic DNA. Translation: CAA78360.1.
PIRiS68968.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38051 Genomic DNA. Translation: AAA63547.1 .
Z13958 Genomic DNA. Translation: CAA78360.1 .
PIRi S68968.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi Search...

Chemistry

BindingDBi P28593.
ChEMBLi CHEMBL5131.
DrugBanki DB03147. Flavin adenine dinucleotide.

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: November 26, 2014
This is version 104 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