Reviewed, UniProtKB/Swiss-Prot P13110 (TYTR_TRYCO)

Names and origin

Protein names

Recommended name:
    Trypanothione reductase
      Short name=TR
    EC=1.8.1.12
Alternative name(s):
    N(1),N(8)-bis(glutathionyl)spermidine reductase

Gene names

Name:

TPR

Organism

Trypanosoma congolense

Taxonomic identifier

5692 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Nannomonas

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
Catalytic activity	Trypanothione + NADP+ = trypanothione disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
biophysicochemical properties	Kinetic parameters: KM=18 µM for trypanothione

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro trypanothione-disulfide reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	Trypanothione reductase		PRO_0000067991
Regions
	Nucleotide binding	35 – 52	18	FAD By similarity
Sites
	Active site	461	1	Proton acceptor By similarity
Amino acid modifications
	Disulfide bond	52 ↔ 57		Redox-active By similarity
Experimental info
	Mutagenesis	18	1	E → A: KM=266 uM for trypanothione.
	Mutagenesis	21	1	W → R: KM=600 uM for trypanothione.
	Mutagenesis	343	1	A → R: KM=9 uM for trypanothione.

Sequences

	Sequence		Length	Mass (Da)
	P13110-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 48F305A4C8C09685	FASTA	492	53,443
	10 20 30 40 50 60 MSKAFDLVII GAGSGGLEAG WNAATLYKKR VAVVDVQTVH GPPFFAALGG TCVNVGCVPK 70 80 90 100 110 120 KLMVTGAQYM DQLRESAGFG WEFDASTIKA NWKTLIAAKN AAVLDINKSY EDMFKDTEGL 130 140 150 160 170 180 EFFLGWGALE QKNVVTVREG ADPKSKVKER LQAEHIIIAT GSWPQMLKIP GIEHCISSNE 190 200 210 220 230 240 AFYLEEPPRR VLTVGGGFIS VEFAGIFNAY KPVGGKVTLC YRNNPILRGF DYTLRQELTK 250 260 270 280 290 300 QLVANGIDIM TNENPSKIEL NPDGSKHVTF ESGKTLDVDV VMMAIGRLPR TGYLQLQTVG 310 320 330 340 350 360 VNLTDKGAIQ VDEFSRTNVP NIYAIGDVTG RIMLTPVAIN EGASVVDTIF GSKPRKTDHT 370 380 390 400 410 420 RVASAVFSIP PIGTCGLTEE EAAKSFEKVA VYLSCFTPLM HNISGSKYKK FVAKIITDHG 430 440 450 460 470 480 DGTVVGVHLL GDSSPEIIQA VGICMKLNAK ISDFYNTIGV HPTSAEELCS MRTPSHYYIK 490 GEKMETLPDS SL

References

[1]	"Trypanothione reductase of Trypanosoma congolense: gene isolation, primary sequence determination, and comparison to glutathione reductase." Shames S.L., Kimmel B.E., Peoples O.P., Agabian N., Walsh C.T. Biochemistry 27:5014-5019(1988) [PubMed: 3167026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular studies on trypanothione reductase, a target for antiparasitic drugs." Walsh C.T., Bradley M., Nadeau K. Trends Biochem. Sci. 16:305-309(1991) [PubMed: 1957352] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M21122 Genomic DNA. Translation: AAA30258.1.
PIR	A27727.
3D structure databases
HSSP	HSSP built from PDB template 1NDA based on UniProtKB P28593.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.12. 95989.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. IPR001864. Trypnth_redctse. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01423. trypano_reduc. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TYTR_TRYCO

Accession

Primary (citable) accession number: P13110

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)