Trypanothione reductase

Name	Trypanothione reductase
Synonyms	1.8.1.12 N(1),N(8)-bis(glutathionyl)spermidine reductase TR
Gene Name	TPR
Organism	Trypanosoma cruzi
Amino acid sequence	>lcl\|BSEQ0011099\|Trypanothione reductase MMSKIFDLVVIGAGSGGLEAAWNAATLYKKRVAVIDVQMVHGPPFFSALGGTCVNVGCVP KKLMVTGAQYMEHLRESAGFGWEFDRTTLRAEWKKLIAVKDEAVLNINKSYEEMFRDTEG LEFFLGWGSLESKNVVNVRESADPASAVKERLETENILLASGSWPHMPNIPGIEHCISSN EAFYLPEPPRRVLTVGGGFISVEFAGIFNAYKPKDGQVTLCYRGEMILRGFDHTLREELT KQLTANGIQILTKENPAKVELNADGSKSVTFESGKKMDFDLVMMAIGRSPRTKDLQLQNA GVMIKNGGVQVDEYSRTNVSNIYAIGDVTNRVMLTPVAINEAAALVDTVFGTNPRKTDHT RVASAVFSIPPIGTCGLIEEVASKRYEVVAVYLSSFTPLMHNISGSKYKTFVAKIITNHS DGTVLGVHLLGDNAPEIIQGVGICLKLNAKISDFYNTIGVHPTSAEELCSMRTPSYYYVK GEKMEKPSEASL
Number of residues	None
Molecular Weight	53867.475
Theoretical pI	6.68
GO Classification	Functions disulfide oxidoreductase activity flavin adenine dinucleotide binding trypanothione-disulfide reductase activity Processes cell redox homeostasis Components cytoplasm
General Function	Trypanothione-disulfide reductase activity
Specific Function	Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P28593
UniProtKB Entry Name
Cellular Location	Cytoplasm
Gene sequence	>lcl\|BSEQ0003079\|1479 bp ATGATGTCAAAAATTTTTGATTTGGTTGTCATTGGCGCCGGCTCGGGCGGACTGGAGGCT GCTTGGAACGCGGCGACACTCTACAAGAAGCGGGTTGCGGTGATTGATGTTCAGATGGTT CACGGGCCCCCGTTTTTTTCTGCTCTAGGCGGCACGTGTGTCAATGTTGGCTGCGTTCCG AAGAAATTGATGGTTACAGGGGCCCAATACATGGAACACCTGCGCGAGTCCGCTGGGTTC GGGTGGGAGTTTGATCGCACCACTCTCAGGGCGGAATGGAAGAAACTTATTGCTGTCAAG GACGAGGCGGTGCTGAATATCAACAAGAGTTATGAGGAGATGTTTCGGGACACGGAGGGT CTGGAGTTTTTTCTGGGCTGGGGATCACTGGAGTCAAAGAATGTCGTCAATGTTCGCGAG AGTGCCGACCCGGCCAGCGCAGTGAAGGAGCGCCTGGAGACGGAGAACATTCTACTTGCC AGTGGTTCGTGGCCGCACATGCCAAACATCCCTGGTATTGAGCATTGCATCAGCAGCAAT GAGGCATTTTACCTGCCGGAGCCACCGCGTCGTGTCCTCACTGTCGGCGGAGGTTTCATT TCCGTGGAGTTCGCCGGCATTTTTAACGCCTACAAGCCGAAAGACGGACAAGTGACGTTG TGCTACCGCGGTGAAATGATCCTTCGTGGCTTTGACCACACTCTCCGTGAGGAACTCACA AAGCAGCTCACCGCCAACGGCATTCAAATCCTTACAAAGGAAAATCCGGCCAAGGTGGAG TTGAACGCGGATGGCAGCAAAAGTGTTACTTTCGAGAGCGGCAAAAAGATGGACTTTGAT CTTGTCATGATGGCGATTGGCCGTTCTCCCCGAACAAAGGATTTACAGCTGCAAAACGCC GGCGTCATGATCAAGAACGGTGGTGTGCAGGTGGACGAGTACTCGCGCACGAATGTTTCC AACATTTACGCCATCGGTGACGTCACAAATCGTGTCATGTTGACACCCGTTGCCATAAAT GAAGCCGCTGCCCTTGTGGATACCGTCTTTGGTACCAATCCGCGAAAGACGGACCACACC CGTGTGGCGAGTGCCGTCTTCTCTATTCCTCCAATTGGTACCTGCGGTCTCATTGAAGAG GTTGCATCCAAGCGCTACGAGGTGGTGGCGGTATACCTTTCCAGCTTTACCCCGCTCATG CACAACATCAGCGGATCAAAGTATAAGACTTTTGTTGCAAAGATAATTACCAACCACTCC GATGGCACTGTGCTTGGTGTACATCTTCTTGGGGACAATGCCCCAGAAATCATCCAAGGT GTTGGTATCTGTCTCAAGTTAAATGCCAAAATATCCGACTTCTACAACACTATTGGTGTG CATCCCACAAGTGCGGAGGAGCTGTGCTCCATGCGCACTCCTTCTTACTACTATGTTAAA GGTGAGAAGATGGAAAAGCCTTCAGAGGCATCTCTGTAA
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	Sullivan FX, Walsh CT: Cloning, sequencing, overproduction and purification of trypanothione reductase from Trypanosoma cruzi. Mol Biochem Parasitol. 1991 Jan;44(1):145-7. [2011150 ] Borges A, Cunningham ML, Tovar J, Fairlamb AH: Site-directed mutagenesis of the redox-active cysteines of Trypanosoma cruzi trypanothione reductase. Eur J Biochem. 1995 Mar 15;228(3):745-52. [7737173 ] Krauth-Siegel RL, Sticherling C, Jost I, Walsh CT, Pai EF, Kabsch W, Lantwin CB: Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease. FEBS Lett. 1993 Feb 8;317(1-2):105-8. [8428618 ] Lantwin CB, Schlichting I, Kabsch W, Pai EF, Krauth-Siegel RL: The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state. Proteins. 1994 Feb;18(2):161-73. [8159665 ] Zhang Y, Bond CS, Bailey S, Cunningham ML, Fairlamb AH, Hunter WN: The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution. Protein Sci. 1996 Jan;5(1):52-61. [8771196 ]

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