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UniProtKB - P39040 (TYTR_CRIFA)
Protein
Trypanothione reductase
Gene
TPR
Organism
Crithidia fasciculata
Status
Functioni
Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
Miscellaneous
The active site is a redox-active disulfide bond.
Catalytic activityi
- EC:1.8.1.12
Cofactori
FADNote: Binds 1 FAD per subunit.
pH dependencei
Optimum pH is 7.5-8.0.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 461 | Proton acceptor | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 35 – 51 | FADAdd BLAST | 17 |
GO - Molecular functioni
- flavin adenine dinucleotide binding Source: InterPro
- trypanothione-disulfide reductase activity Source: UniProtKB-EC
GO - Biological processi
- cell redox homeostasis Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Ligand | FAD, Flavoprotein, NADP |
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 |
Organismi | Crithidia fasciculata |
Taxonomic identifieri | 5656 [NCBI] |
Taxonomic lineagei | Eukaryota › Discoba › Euglenozoa › Kinetoplastea › Metakinetoplastina › Trypanosomatida › Trypanosomatidae › Leishmaniinae › Crithidia |
Organism-specific databases
VEuPathDBi | TriTrypDB:CFAC1_020010000 |
Subcellular locationi
Cytoplasm and Cytosol
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000067988 | 1 – 491 | Trypanothione reductaseAdd BLAST | 491 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 52 ↔ 57 | Redox-active1 Publication |
Post-translational modificationi
The N-terminus is blocked.
Keywords - PTMi
Disulfide bondStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P39040 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P39040 |
Family & Domainsi
Sequence similaritiesi
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.Curated
Keywords - Domaini
Redox-active centerFamily and domain databases
Gene3Di | 3.30.390.30, 1 hit 3.50.50.60, 2 hits |
InterProi | View protein in InterPro IPR036188, FAD/NAD-bd_sf IPR023753, FAD/NAD-binding_dom IPR016156, FAD/NAD-linked_Rdtase_dimer_sf IPR001100, Pyr_nuc-diS_OxRdtase IPR004099, Pyr_nucl-diS_OxRdtase_dimer IPR012999, Pyr_OxRdtase_I_AS IPR001864, Trypnth_redctse |
Pfami | View protein in Pfam PF07992, Pyr_redox_2, 1 hit PF02852, Pyr_redox_dim, 1 hit |
PIRSFi | PIRSF000350, Mercury_reductase_MerA, 1 hit |
PRINTSi | PR00470, TRYPANRDTASE |
SUPFAMi | SSF51905, SSF51905, 1 hit SSF55424, SSF55424, 1 hit |
TIGRFAMsi | TIGR01423, trypano_reduc, 1 hit |
PROSITEi | View protein in PROSITE PS00076, PYRIDINE_REDOX_1, 1 hit |
i Sequence
Sequence statusi: Complete.
P39040-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 16 | G → R in AAA30322 (PubMed:1542316).Curated | 1 | |
Sequence conflicti | 16 | G → R in AAA30323 (PubMed:1542316).Curated | 1 | |
Sequence conflicti | 62 | L → Y AA sequence (PubMed:3718941).Curated | 1 | |
Sequence conflicti | 297 | D → E in AAA30321 (PubMed:1542316).Curated | 1 | |
Sequence conflicti | 297 | D → E in AAA30322 (PubMed:1542316).Curated | 1 | |
Sequence conflicti | 297 | D → E in AAA30323 (PubMed:1542316).Curated | 1 | |
Sequence conflicti | 454 | F → V in AAA30322 (PubMed:1542316).Curated | 1 | |
Sequence conflicti | 454 | F → V in AAA30323 (PubMed:1542316).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 479 | Q → 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 |
PIRi | S28002 |
Genome annotation databases
KEGGi | ag:CAA78264 |
Similar proteinsi
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 |
PIRi | S28002 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1FEA | X-ray | 2.20 | A/B/C/D | 2-491 | [»] | |
1FEB | X-ray | 2.00 | A/B | 2-491 | [»] | |
1FEC | X-ray | 1.70 | A/B | 2-491 | [»] | |
1TYP | X-ray | 2.80 | A/B | 1-487 | [»] | |
1TYT | X-ray | 2.60 | A/B | 1-487 | [»] | |
2TPR | X-ray | 2.40 | A/B | 2-491 | [»] | |
SMRi | P39040 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
BindingDBi | P39040 |
ChEMBLi | CHEMBL5394 |
Genome annotation databases
KEGGi | ag:CAA78264 |
Organism-specific databases
VEuPathDBi | TriTrypDB:CFAC1_020010000 |
Miscellaneous databases
EvolutionaryTracei | P39040 |
Family and domain databases
Gene3Di | 3.30.390.30, 1 hit 3.50.50.60, 2 hits |
InterProi | View protein in InterPro IPR036188, FAD/NAD-bd_sf IPR023753, FAD/NAD-binding_dom IPR016156, FAD/NAD-linked_Rdtase_dimer_sf IPR001100, Pyr_nuc-diS_OxRdtase IPR004099, Pyr_nucl-diS_OxRdtase_dimer IPR012999, Pyr_OxRdtase_I_AS IPR001864, Trypnth_redctse |
Pfami | View protein in Pfam PF07992, Pyr_redox_2, 1 hit PF02852, Pyr_redox_dim, 1 hit |
PIRSFi | PIRSF000350, Mercury_reductase_MerA, 1 hit |
PRINTSi | PR00470, TRYPANRDTASE |
SUPFAMi | SSF51905, SSF51905, 1 hit SSF55424, SSF55424, 1 hit |
TIGRFAMsi | TIGR01423, trypano_reduc, 1 hit |
PROSITEi | View protein in PROSITE PS00076, PYRIDINE_REDOX_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TYTR_CRIFA | |
Accessioni | P39040Primary (citable) accession number: P39040 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1995 |
Last sequence update: | February 1, 1995 | |
Last modified: | February 23, 2022 | |
This is version 135 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families