Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei461Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi35 – 51FADAdd BLAST17

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 databases

ChEMBLiCHEMBL5394.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000679881 – 491Trypanothione reductaseAdd BLAST491

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi52 ↔ 57Redox-active1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Chemistry databases

BindingDBiP39040.

Structurei

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi14 – 27Combined sources14
Beta strandi31 – 36Combined sources6
Beta strandi38 – 41Combined sources4
Turni42 – 44Combined sources3
Helixi51 – 55Combined sources5
Helixi57 – 75Combined sources19
Helixi76 – 79Combined sources4
Helixi85 – 87Combined sources3
Helixi92 – 115Combined sources24
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 – 244Combined sources13
Beta strandi247 – 251Combined sources5
Beta strandi255 – 260Combined sources6
Beta strandi266 – 270Combined sources5
Beta strandi275 – 283Combined sources9
Beta strandi287 – 290Combined sources4
Helixi292 – 294Combined sources3
Helixi296 – 299Combined sources4
Beta strandi322 – 324Combined sources3
Helixi326 – 329Combined sources4
Helixi335 – 350Combined sources16
Beta strandi364 – 366Combined sources3
Beta strandi368 – 370Combined 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
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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti16G → R in AAA30322 (PubMed:1542316).Curated1
Sequence conflicti16G → R in AAA30323 (PubMed:1542316).Curated1
Sequence conflicti62L → Y AA sequence (PubMed:3718941).Curated1
Sequence conflicti297D → E in AAA30321 (PubMed:1542316).Curated1
Sequence conflicti297D → E in AAA30322 (PubMed:1542316).Curated1
Sequence conflicti297D → E in AAA30323 (PubMed:1542316).Curated1
Sequence conflicti454F → V in AAA30322 (PubMed:1542316).Curated1
Sequence conflicti454F → V in AAA30323 (PubMed:1542316).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti479Q → E.1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

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...

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: November 2, 2016
This is version 113 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.