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Protein

Trypanothione reductase

Gene

TPR

Organism
Crithidia fasciculata
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.

pH dependencei

Optimum pH is 7.5-8.0.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi35 – 5117FADAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13293.

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
OrganismiCrithidia fasciculata
Taxonomic identifieri5656 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5394.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Trypanothione reductasePRO_0000067988Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 57Redox-active1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Chemistry

BindingDBiP39040.

Structurei

Secondary structure

1
491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi14 – 2714Combined sources
Beta strandi31 – 366Combined sources
Beta strandi38 – 414Combined sources
Turni42 – 443Combined sources
Helixi51 – 555Combined sources
Helixi57 – 7519Combined sources
Helixi76 – 794Combined sources
Helixi85 – 873Combined sources
Helixi92 – 11524Combined 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 – 24413Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi255 – 2606Combined sources
Beta strandi266 – 2705Combined sources
Beta strandi275 – 2839Combined sources
Beta strandi287 – 2904Combined sources
Helixi292 – 2943Combined sources
Helixi296 – 2994Combined sources
Beta strandi322 – 3243Combined sources
Helixi326 – 3294Combined sources
Helixi335 – 35016Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi368 – 3703Combined 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
1FEAX-ray2.20A/B/C/D2-491[»]
1FEBX-ray2.00A/B2-491[»]
1FECX-ray1.70A/B2-491[»]
1TYPX-ray2.80A/B1-487[»]
1TYTX-ray2.60A/B1-487[»]
2TPRX-ray2.40A/B2-491[»]
ProteinModelPortaliP39040.
SMRiP39040. Positions 1-487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39040.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

KOiK04283.

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.

P39040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRAYDLVVI GAGSGGLEAG WNAASLHKKR VAVIDLQKHH GPPHYAALGG
60 70 80 90 100
TCVNVGCVPK KLMVTGANYM DTIRESAGFG WELDRESVRP NWKALIAAKN
110 120 130 140 150
KAVSGINDSY EGMFADTEGL TFHQGFGALQ DNHTVLVRES ADPNSAVLET
160 170 180 190 200
LDTEYILLAT GSWPQHLGIE GDDLCITSNE AFYLDEAPKR ALCVGGGYIS
210 220 230 240 250
IEFAGIFNAY KARGGQVDLA YRGDMILRGF DSELRKQLTE QLRANGINVR
260 270 280 290 300
THENPAKVTK NADGTRHVVF ESGAEADYDV VMLAIGRVPR SQTLQLDKAG
310 320 330 340 350
VEVAKNGAIK VDAYSKTNVD NIYAIGDVTD RVMLTPVAIN EGAAFVDTVF
360 370 380 390 400
ANKPRATDHT KVACAVFSIP PMGVCGYVEE DAAKKYDQVA VYESSFTPLM
410 420 430 440 450
HNISGSTYKK FMVRIVTNHA DGEVLGVHML GDSSPEIIQS VAICLKMGAK
460 470 480 490
ISDFYNTIGV HPTSAEELCS MRTPAYFYQK GKRVEKIDSN L
Length:491
Mass (Da):53,229
Last modified:February 1, 1995 - v1
Checksum:iEF749215A16F9187
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161G → R in AAA30322 (PubMed:1542316).Curated
Sequence conflicti16 – 161G → R in AAA30323 (PubMed:1542316).Curated
Sequence conflicti62 – 621L → Y AA sequence (PubMed:3718941).Curated
Sequence conflicti297 – 2971D → E in AAA30321 (PubMed:1542316).Curated
Sequence conflicti297 – 2971D → E in AAA30322 (PubMed:1542316).Curated
Sequence conflicti297 – 2971D → E in AAA30323 (PubMed:1542316).Curated
Sequence conflicti454 – 4541F → V in AAA30322 (PubMed:1542316).Curated
Sequence conflicti454 – 4541F → V in AAA30323 (PubMed:1542316).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti479 – 4791Q → E.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12618 Genomic DNA. Translation: CAA78264.1.
M73323 mRNA. Translation: AAA30321.1.
M73324 Genomic DNA. Translation: AAA30322.1.
M73325 Genomic DNA. Translation: AAA30323.1.
PIRiS28002.

Genome annotation databases

KEGGiag:CAA78264.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12618 Genomic DNA. Translation: CAA78264.1.
M73323 mRNA. Translation: AAA30321.1.
M73324 Genomic DNA. Translation: AAA30322.1.
M73325 Genomic DNA. Translation: AAA30323.1.
PIRiS28002.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FEAX-ray2.20A/B/C/D2-491[»]
1FEBX-ray2.00A/B2-491[»]
1FECX-ray1.70A/B2-491[»]
1TYPX-ray2.80A/B1-487[»]
1TYTX-ray2.60A/B1-487[»]
2TPRX-ray2.40A/B2-491[»]
ProteinModelPortaliP39040.
SMRiP39040. Positions 1-487.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP39040.
ChEMBLiCHEMBL5394.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA78264.

Phylogenomic databases

KOiK04283.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13293.

Miscellaneous databases

EvolutionaryTraceiP39040.

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...

Publicationsi

  1. "Molecular characterization of the trypanothione reductase gene from Crithidia fasciculata and Trypanosoma brucei: comparison with other flavoprotein disulphide oxidoreductases with respect to substrate specificity and catalytic mechanism."
    Aboagye-Kwarteng T., Smith K., Fairlamb A.H.
    Mol. Microbiol. 6:3089-3099(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning, sequencing, and demonstration of polymorphism in trypanothione reductase from Crithidia fasciculata."
    Field H., Cerami A., Henderson G.B.
    Mol. Biochem. Parasitol. 50:47-56(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. "Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases."
    Shames S.L., Fairlamb A.H., Cerami A., Walsh C.T.
    Biochemistry 25:3519-3526(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 39-62, CHARACTERIZATION.
  4. "Substrate interactions between trypanothione reductase and N1-glutathionylspermidine disulphide at 0.28-nm resolution."
    Bailey S., Smith K., Fairlamb A.H., Hunter W.N.
    Eur. J. Biochem. 213:67-75(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BOND.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  6. "Structure of trypanothione reductase from Crithidia fasciculata at 2.6-A resolution; enzyme-NADP interactions at 2.8-A resolution."
    Bailey S., Fairlamb A.H., Hunter W.N.
    Acta Crystallogr. D 50:139-154(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  7. "Overexpression of Crithidia fasciculata trypanothione reductase and crystallization using a novel geometry."
    Strickland C.L., Puchalski R., Savvides S.N., Karplus P.A.
    Acta Crystallogr. D 51:337-341(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).

Entry informationi

Entry nameiTYTR_CRIFA
AccessioniPrimary (citable) accession number: P39040
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 111 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, Direct protein sequencing

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.