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Protein

Trypanothione reductase

Gene

TPR

Organism
Trypanosoma congolense
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

Kineticsi

  1. KM=18 µM for trypanothione

    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

    Enzyme and pathway databases

    SABIO-RKP13110.

    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 congolense
    Taxonomic identifieri5692 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaNannomonas

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi18 – 181E → A: KM=266 uM for trypanothione.
    Mutagenesisi21 – 211W → R: KM=600 uM for trypanothione.
    Mutagenesisi343 – 3431A → R: KM=9 uM for trypanothione.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 492492Trypanothione reductasePRO_0000067991Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    3D structure databases

    ProteinModelPortaliP13110.
    SMRiP13110. Positions 5-485.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.50.50.60. 3 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.

    P13110-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKAFDLVII GAGSGGLEAG WNAATLYKKR VAVVDVQTVH GPPFFAALGG
    60 70 80 90 100
    TCVNVGCVPK KLMVTGAQYM DQLRESAGFG WEFDASTIKA NWKTLIAAKN
    110 120 130 140 150
    AAVLDINKSY EDMFKDTEGL EFFLGWGALE QKNVVTVREG ADPKSKVKER
    160 170 180 190 200
    LQAEHIIIAT GSWPQMLKIP GIEHCISSNE AFYLEEPPRR VLTVGGGFIS
    210 220 230 240 250
    VEFAGIFNAY KPVGGKVTLC YRNNPILRGF DYTLRQELTK QLVANGIDIM
    260 270 280 290 300
    TNENPSKIEL NPDGSKHVTF ESGKTLDVDV VMMAIGRLPR TGYLQLQTVG
    310 320 330 340 350
    VNLTDKGAIQ VDEFSRTNVP NIYAIGDVTG RIMLTPVAIN EGASVVDTIF
    360 370 380 390 400
    GSKPRKTDHT RVASAVFSIP PIGTCGLTEE EAAKSFEKVA VYLSCFTPLM
    410 420 430 440 450
    HNISGSKYKK FVAKIITDHG DGTVVGVHLL GDSSPEIIQA VGICMKLNAK
    460 470 480 490
    ISDFYNTIGV HPTSAEELCS MRTPSHYYIK GEKMETLPDS SL
    Length:492
    Mass (Da):53,443
    Last modified:January 1, 1990 - v1
    Checksum:i48F305A4C8C09685
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M21122 Genomic DNA. Translation: AAA30258.1.
    PIRiA27727.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M21122 Genomic DNA. Translation: AAA30258.1.
    PIRiA27727.

    3D structure databases

    ProteinModelPortaliP13110.
    SMRiP13110. Positions 5-485.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    SABIO-RKP13110.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.50.50.60. 3 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_TRYCO
    AccessioniPrimary (citable) accession number: P13110
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: September 7, 2016
    This is version 104 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.