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Protein

Trypanothione reductase

Gene

TPR

Organism
Trypanosoma brucei brucei
Status
Reviewed-Annotation score: Annotation score: 4 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

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi35 – 5218FADBy similarityAdd
BLAST

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. 6519.

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 brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1837.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Trypanothione reductasePRO_0000067990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 57Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Chemistry

BindingDBiP39051.

Structurei

Secondary structure

1
492
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi14 – 2714Combined sources
Beta strandi31 – 366Combined sources
Beta strandi38 – 414Combined sources
Turni42 – 443Combined sources
Helixi50 – 556Combined sources
Helixi57 – 7519Combined sources
Helixi76 – 794Combined sources
Helixi85 – 873Combined sources
Helixi92 – 11625Combined sources
Beta strandi120 – 13112Combined sources
Beta strandi134 – 1429Combined sources
Beta strandi147 – 15812Combined sources
Beta strandi162 – 1643Combined sources
Helixi172 – 1743Combined sources
Helixi178 – 1814Combined sources
Beta strandi189 – 1946Combined sources
Helixi198 – 21013Combined sources
Beta strandi216 – 22712Combined sources
Helixi232 – 24312Combined sources
Turni244 – 2463Combined sources
Beta strandi247 – 2526Combined sources
Beta strandi255 – 2606Combined sources
Beta strandi266 – 2705Combined sources
Beta strandi275 – 2839Combined sources
Beta strandi287 – 2893Combined sources
Helixi296 – 2983Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi322 – 3243Combined sources
Helixi326 – 3294Combined sources
Helixi335 – 34915Combined sources
Beta strandi363 – 3664Combined 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 – 4865Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WBAX-ray2.30A/B1-492[»]
ProteinModelPortaliP39051.
SMRiP39051. Positions 4-485.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39051.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

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.

P39051-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKIFDLVVI GAGSGGLEAG WNAATLYKKR VAVIDVQTHH GPPHYAALGG
60 70 80 90 100
TCVNVGCVPK KLMVTGAQYM DHLRESAGFG WEFDGSSVKA NWKKLIAAKN
110 120 130 140 150
EAVLDINKSY EGMFNDTEGL DFFLGWGSLE SKNVVVVRET ADPKSAVKER
160 170 180 190 200
LQADHILLAT GSWPQMPAIP GVEHCISSNE AFYLPEPPRR VLTVGGGFIS
210 220 230 240 250
VEFAGIFNAY KPPGGKVTLC YRNNLILRGF DETIREEVTK QLTANGIEIM
260 270 280 290 300
TNENPAKVSL NTDGSKHVTF ESGKTLDVDV VMMAIGRIPR TNDLQLGNVG
310 320 330 340 350
VKLTPKGGVQ VDEFSRTNVP NIYAIGDITD RLMLTPVAIN EGAALVDTVF
360 370 380 390 400
GNKPRKTDHT RVASAVFSIP PIGTCGLIEE VAAKEFEKVA VYMSSFTPLM
410 420 430 440 450
HNISGSKYKK FVAKIVTNHS DGTVLGVHLL GDGAPEIIQA VGVCLRLNAK
460 470 480 490
ISDFYNTIGV HPTSAEELCS MRTPSYYYLK GEKMETLPES SL
Length:492
Mass (Da):53,284
Last modified:February 1, 1995 - v1
Checksum:iFFCA2F11B66F7FF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63188 Genomic DNA. Translation: CAA44870.1.
PIRiS28003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63188 Genomic DNA. Translation: CAA44870.1.
PIRiS28003.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WBAX-ray2.30A/B1-492[»]
ProteinModelPortaliP39051.
SMRiP39051. Positions 4-485.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP39051.
ChEMBLiCHEMBL1837.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.8.1.12. 6519.

Miscellaneous databases

EvolutionaryTraceiP39051.

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_TRYBB
AccessioniPrimary (citable) accession number: P39051
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 11, 2015
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

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.