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Protein

Trypanothione reductase

Gene

TPR

Organism
Leishmania donovani
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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

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
OrganismiLeishmania donovani
Taxonomic identifieri5661 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2176840.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Trypanothione reductasePRO_0000067989Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi5661.XP_003858222.1.

Structurei

3D structure databases

ProteinModelPortaliP39050.
SMRiP39050. Positions 2-486.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
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.

P39050-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRAYDLVVL GAGSGGLEAG WNAAVTHKKK VAVVDVQATH GPPALVALGG
60 70 80 90 100
TCVNVGCVPK KLMVTGAQYM DLIRESGGFG WEMDRESLCP NWKTLIAAKN
110 120 130 140 150
KVVNSINESY KSMFADTEGL SFHMGFGALQ DAHTVVVRKS EDPHSDVLET
160 170 180 190 200
LDTEYILIAT GSWPTRLGVP GDEFCITSNE AFYLEDAPKR MLCVGGGYIA
210 220 230 240 250
VEFAGIFNGY KPCGGYVDLC YRGDLILRGF DTEVRKSLTK QLGANGIRVR
260 270 280 290 300
TNLNPTKITK NEDGSNHVHF NDGTEEDYDQ VMLAIGVPRS QALQLDKAGV
310 320 330 340 350
RTGKNGAVQV DAYSKTSVDN IYAIGDVTNR VMLTPVAINE GACVLLETVF
360 370 380 390 400
GGKPRATDHT KVACAVFSIP PIGTCGMTEE EAAKNYETVA VYASSFTPLM
410 420 430 440 450
HNISGSKHKE FMIRIITNES NGEVLGVHML GDSAPEIIQS VGICMKMGAK
460 470 480 490
ISDFHSTIGV HPTSAEELCS MRTPAYFYES GKRVEKLSSN L
Length:491
Mass (Da):52,933
Last modified:February 1, 1995 - v1
Checksum:i5A777DA32E8E752A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23135 Genomic DNA. Translation: CAA80668.1.
PIRiS34376.

Genome annotation databases

KEGGiag:CAA80668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z23135 Genomic DNA. Translation: CAA80668.1.
PIRiS34376.

3D structure databases

ProteinModelPortaliP39050.
SMRiP39050. Positions 2-486.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5661.XP_003858222.1.

Chemistry

ChEMBLiCHEMBL2176840.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA80668.

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
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]
ProtoNetiSearch...

Publicationsi

  1. "The structure, organization, and expression of the Leishmania donovani gene encoding trypanothione reductase."
    Taylor M.C., Kelly J.M., Chapman C.J., Fairlamb A.H., Miles M.A.
    Mol. Biochem. Parasitol. 64:293-301(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MHOM/ET/67/HU3.

Entry informationi

Entry nameiTYTR_LEIDO
AccessioniPrimary (citable) accession number: P39050
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 98 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.

Documents

  1. 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.