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P28593

- TYTR_TRYCR

UniProt

P28593 - TYTR_TRYCR

Protein

Trypanothione reductase

Gene

TPR

Organism
Trypanosoma cruzi
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.

    Catalytic activityi

    Trypanothione + NADP+ = trypanothione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi36 – 5217FADAdd
    BLAST

    GO - Molecular functioni

    1. disulfide oxidoreductase activity Source: InterPro
    2. flavin adenine dinucleotide binding Source: InterPro
    3. trypanothione-disulfide reductase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro

    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
    OrganismiTrypanosoma cruzi
    Taxonomic identifieri5693 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 492492Trypanothione reductasePRO_0000067992Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi53 ↔ 58Redox-active1 Publication

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    492
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Helixi15 – 2612
    Beta strandi32 – 376
    Beta strandi39 – 424
    Turni43 – 453
    Helixi51 – 566
    Helixi58 – 7619
    Helixi77 – 804
    Helixi86 – 883
    Helixi93 – 11725
    Beta strandi121 – 13212
    Beta strandi135 – 1439
    Beta strandi148 – 1558
    Beta strandi157 – 1593
    Beta strandi163 – 1653
    Helixi173 – 1753
    Helixi179 – 1824
    Beta strandi190 – 1956
    Helixi199 – 21113
    Beta strandi217 – 22812
    Helixi233 – 24513
    Beta strandi249 – 2535
    Beta strandi256 – 2616
    Beta strandi267 – 2715
    Beta strandi276 – 2849
    Beta strandi288 – 2903
    Helixi293 – 2953
    Helixi297 – 2993
    Beta strandi306 – 3094
    Beta strandi322 – 3243
    Helixi326 – 3294
    Helixi335 – 35016
    Beta strandi351 – 3533
    Beta strandi364 – 3663
    Beta strandi372 – 3765
    Helixi379 – 3857
    Beta strandi387 – 39610
    Helixi399 – 4046
    Beta strandi411 – 4188
    Turni419 – 4213
    Beta strandi423 – 4319
    Helixi434 – 44613
    Helixi451 – 4555
    Helixi465 – 4695
    Beta strandi475 – 4795
    Beta strandi482 – 4843

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AOGX-ray2.30A/B3-487[»]
    1BZLX-ray2.40A/B2-487[»]
    1GXFX-ray2.70A/B1-492[»]
    1NDAX-ray3.30A/B/C/D2-492[»]
    ProteinModelPortaliP28593.
    SMRiP28593. Positions 5-485.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28593.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR001864. Trypnth_redctse.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    PR00470. TRYPANRDTASE.
    SUPFAMiSSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR01423. trypano_reduc. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P28593-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMSKIFDLVV IGAGSGGLEA AWNAATLYKK RVAVIDVQMV HGPPFFSALG    50
    GTCVNVGCVP KKLMVTGAQY MEHLRESAGF GWEFDRTTLR AEWKKLIAVK 100
    DEAVLNINKS YEEMFRDTEG LEFFLGWGSL ESKNVVNVRE SADPASAVKE 150
    RLETENILLA SGSWPHMPNI PGIEHCISSN EAFYLPEPPR RVLTVGGGFI 200
    SVEFAGIFNA YKPKDGQVTL CYRGEMILRG FDHTLREELT KQLTANGIQI 250
    LTKENPAKVE LNADGSKSVT FESGKKMDFD LVMMAIGRSP RTKDLQLQNA 300
    GVMIKNGGVQ VDEYSRTNVS NIYAIGDVTN RVMLTPVAIN EAAALVDTVF 350
    GTNPRKTDHT RVASAVFSIP PIGTCGLIEE VASKRYEVVA VYLSSFTPLM 400
    HNISGSKYKT FVAKIITNHS DGTVLGVHLL GDNAPEIIQG VGICLKLNAK 450
    ISDFYNTIGV HPTSAEELCS MRTPSYYYVK GEKMEKPSEA SL 492
    Length:492
    Mass (Da):53,868
    Last modified:December 1, 1992 - v1
    Checksum:i4AF179952A20750F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti95 – 951K → N in strain: Silvio.
    Natural varianti140 – 1401E → A in strain: Silvio.
    Natural varianti156 – 1561N → H in strain: Silvio.
    Natural varianti353 – 3531N → T in strain: Silvio.
    Natural varianti402 – 4032NI → KV in strain: Silvio.
    Natural varianti441 – 4411V → I in strain: Silvio.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M38051 Genomic DNA. Translation: AAA63547.1.
    Z13958 Genomic DNA. Translation: CAA78360.1.
    PIRiS68968.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M38051 Genomic DNA. Translation: AAA63547.1 .
    Z13958 Genomic DNA. Translation: CAA78360.1 .
    PIRi S68968.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AOG X-ray 2.30 A/B 3-487 [» ]
    1BZL X-ray 2.40 A/B 2-487 [» ]
    1GXF X-ray 2.70 A/B 1-492 [» ]
    1NDA X-ray 3.30 A/B/C/D 2-492 [» ]
    ProteinModelPortali P28593.
    SMRi P28593. Positions 5-485.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P28593.
    ChEMBLi CHEMBL5131.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P28593.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR001864. Trypnth_redctse.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    PR00470. TRYPANRDTASE.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    TIGRFAMsi TIGR01423. trypano_reduc. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing, overproduction and purification of trypanothione reductase from Trypanosoma cruzi."
      Sullivan F.X., Walsh C.T.
      Mol. Biochem. Parasitol. 44:145-148(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Site-directed mutagenesis of the redox-active cysteines of Trypanosoma cruzi trypanothione reductase."
      Borges A., Cunningham M.L., Tover J., Fairlamb A.H.
      Eur. J. Biochem. 228:745-752(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Silvio.
    3. "Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease."
      Krauth-Siegel R.L., Sticherling C., Jost I., Walsh C.T., Pai E.F., Kabsch W., Lantwin C.B.
      FEBS Lett. 317:105-108(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 2-492, DISULFIDE BOND.
    4. "The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state."
      Lantwin C.B., Schlichting I., Kabsch W., Pai E.F., Krauth-Siegel R.L.
      Proteins 18:161-173(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
    5. "The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3-A resolution."
      Zhang Y., Bond C.S., Bailey S., Cunningham M.L., Fairlamb A.H., Hunter W.N.
      Protein Sci. 5:52-61(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
      Strain: Silvio.

    Entry informationi

    Entry nameiTYTR_TRYCR
    AccessioniPrimary (citable) accession number: P28593
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 102 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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3