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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)DescriptionActionsGraphical viewLength
Active sitei461Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi35 – 52FADBy similarityAdd BLAST18

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 databases

ChEMBLiCHEMBL1837.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000679901 – 492Trypanothione reductaseAdd BLAST492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi52 ↔ 57Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Chemistry databases

BindingDBiP39051.

Structurei

Secondary structure

1492
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Helixi14 – 27Combined sources14
Beta strandi31 – 36Combined sources6
Beta strandi38 – 41Combined sources4
Turni42 – 44Combined sources3
Helixi50 – 55Combined sources6
Helixi57 – 75Combined sources19
Helixi76 – 79Combined sources4
Helixi85 – 87Combined sources3
Helixi92 – 116Combined sources25
Beta strandi120 – 131Combined sources12
Beta strandi134 – 142Combined sources9
Beta strandi147 – 158Combined sources12
Beta strandi162 – 164Combined sources3
Helixi172 – 174Combined sources3
Helixi178 – 181Combined sources4
Beta strandi189 – 194Combined sources6
Helixi198 – 210Combined sources13
Beta strandi216 – 227Combined sources12
Helixi232 – 243Combined sources12
Turni244 – 246Combined sources3
Beta strandi247 – 252Combined sources6
Beta strandi255 – 260Combined sources6
Beta strandi266 – 270Combined sources5
Beta strandi275 – 283Combined sources9
Beta strandi287 – 289Combined sources3
Helixi296 – 298Combined sources3
Beta strandi307 – 309Combined sources3
Beta strandi322 – 324Combined sources3
Helixi326 – 329Combined sources4
Helixi335 – 349Combined sources15
Beta strandi363 – 366Combined sources4
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 – 486Combined sources5

3D structure databases

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

Chemistry databases

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 2, 2016
This is version 103 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.