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Protein

Trypanothione reductase

Gene

TPR

Organism
Trypanosoma cruzi
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei461Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 52FADAdd BLAST17

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.8.1.12. 6524.

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5131.
DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000679921 – 492Trypanothione reductaseAdd BLAST492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi53 ↔ 58Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP28593.
PRIDEiP28593.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi353153.XP_805296.1.

Chemistry databases

BindingDBiP28593.

Structurei

Secondary structure

1492
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Helixi15 – 26Combined sources12
Beta strandi32 – 37Combined sources6
Beta strandi39 – 42Combined sources4
Turni43 – 45Combined sources3
Helixi51 – 56Combined sources6
Helixi58 – 76Combined sources19
Helixi77 – 80Combined sources4
Helixi86 – 88Combined sources3
Helixi93 – 117Combined sources25
Beta strandi121 – 132Combined sources12
Beta strandi135 – 143Combined sources9
Beta strandi148 – 155Combined sources8
Beta strandi157 – 159Combined sources3
Beta strandi163 – 165Combined sources3
Helixi173 – 175Combined sources3
Helixi179 – 182Combined sources4
Beta strandi190 – 195Combined sources6
Helixi199 – 211Combined sources13
Beta strandi217 – 228Combined sources12
Helixi233 – 245Combined sources13
Beta strandi249 – 253Combined sources5
Beta strandi256 – 261Combined sources6
Beta strandi267 – 271Combined sources5
Beta strandi276 – 284Combined sources9
Beta strandi288 – 290Combined sources3
Helixi293 – 295Combined sources3
Helixi297 – 299Combined sources3
Beta strandi306 – 309Combined sources4
Beta strandi322 – 324Combined sources3
Helixi326 – 329Combined sources4
Helixi335 – 350Combined sources16
Beta strandi351 – 353Combined sources3
Beta strandi364 – 366Combined sources3
Beta strandi372 – 376Combined sources5
Helixi379 – 385Combined sources7
Beta strandi387 – 396Combined sources10
Helixi399 – 404Combined sources6
Beta strandi411 – 418Combined sources8
Turni419 – 421Combined sources3
Beta strandi423 – 431Combined sources9
Helixi434 – 446Combined sources13
Helixi451 – 455Combined sources5
Helixi465 – 469Combined sources5
Beta strandi475 – 479Combined sources5
Beta strandi482 – 484Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP28593.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001864. Trypnth_redctse.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00470. TRYPANRDTASE.
SUPFAMiSSF51905. SSF51905. 2 hits.
SSF55424. 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)DescriptionActionsGraphical viewLength
Natural varianti95K → N in strain: Silvio. 1
Natural varianti140E → A in strain: Silvio. 1
Natural varianti156N → H in strain: Silvio. 1
Natural varianti353N → T in strain: Silvio. 1
Natural varianti402 – 403NI → KV in strain: Silvio. 2
Natural varianti441V → I in strain: Silvio. 1

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.
PIRiS68968.

3D structure databases

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

Protein-protein interaction databases

STRINGi353153.XP_805296.1.

Chemistry databases

BindingDBiP28593.
ChEMBLiCHEMBL5131.
DrugBankiDB03147. Flavin adenine dinucleotide.

Proteomic databases

PaxDbiP28593.
PRIDEiP28593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.

Enzyme and pathway databases

BRENDAi1.8.1.12. 6524.

Miscellaneous databases

EvolutionaryTraceiP28593.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001864. Trypnth_redctse.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00470. TRYPANRDTASE.
SUPFAMiSSF51905. SSF51905. 2 hits.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01423. trypano_reduc. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 115 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.