Reviewed, UniProtKB/Swiss-Prot P39051 (TYTR_TRYBB)

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 brucei brucei

Taxonomic identifier

5702 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma

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.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure
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 electron carrier 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_0000067990

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

Secondary structure

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492

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Helix

22 – 27

6

Beta strand

31 – 34

4

Turn

52 – 54

3

Helix

58 – 64

7

Helix

69 – 75

7

Helix

92 – 110

19

Turn

114 – 116

3

Beta strand

121 – 123

3

Beta strand

129 – 131

3

Beta strand

134 – 142

9

Beta strand

147 – 158

12

Helix

178 – 181

4

Beta strand

189 – 194

6

Helix

199 – 203

5

Helix

207 – 210

4

Beta strand

217 – 226

10

Helix

232 – 244

13

Beta strand

248 – 252

5

Beta strand

255 – 260

6

Beta strand

266 – 270

5

Beta strand

275 – 283

9

Beta strand

322 – 324

3

Helix

335 – 340

6

Helix

344 – 350

7

Helix

379 – 385

7

Beta strand

387 – 396

10

Helix

399 – 403

5

Beta strand

411 – 418

8

Beta strand

428 – 430

3

Helix

435 – 438

4

Turn

444 – 448

5

Helix

451 – 455

5

Helix

465 – 469

5

Beta strand

475 – 479

5

Beta strand

483 – 486

4

Sequences

	Sequence		Length	Mass (Da)
	P39051-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: FFCA2F11B66F7FF4	FASTA	492	53,284
	10 20 30 40 50 60 MSKIFDLVVI GAGSGGLEAG WNAATLYKKR VAVIDVQTHH GPPHYAALGG TCVNVGCVPK 70 80 90 100 110 120 KLMVTGAQYM DHLRESAGFG WEFDGSSVKA NWKKLIAAKN EAVLDINKSY EGMFNDTEGL 130 140 150 160 170 180 DFFLGWGSLE SKNVVVVRET ADPKSAVKER LQADHILLAT GSWPQMPAIP GVEHCISSNE 190 200 210 220 230 240 AFYLPEPPRR VLTVGGGFIS VEFAGIFNAY KPPGGKVTLC YRNNLILRGF DETIREEVTK 250 260 270 280 290 300 QLTANGIEIM TNENPAKVSL NTDGSKHVTF ESGKTLDVDV VMMAIGRIPR TNDLQLGNVG 310 320 330 340 350 360 VKLTPKGGVQ VDEFSRTNVP NIYAIGDITD RLMLTPVAIN EGAALVDTVF GNKPRKTDHT 370 380 390 400 410 420 RVASAVFSIP PIGTCGLIEE VAAKEFEKVA VYMSSFTPLM HNISGSKYKK FVAKIVTNHS 430 440 450 460 470 480 DGTVLGVHLL GDGAPEIIQA VGVCLRLNAK ISDFYNTIGV HPTSAEELCS MRTPSYYYLK 490 GEKMETLPES SL

References

[1]

"Molecular characterization of the trypanothione reductase gene from Crithidia fasciculata and Trypanosoma brucei: comparison with other flavoprotein disulphide oxidoreductases with respect to substrate specificity and catalytic mechanism." Aboagye-Kwarteng T., Smith K., Fairlamb A.H. Mol. Microbiol. 6:3089-3099(1992) [PubMed: 1453951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ILTAT 1.1.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X63188 Genomic DNA. Translation: CAA44870.1.

PIR

S28003.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VE2	X-ray	2.30	A/B	1-490	[»]

SMR

P39051. Positions 2-485.

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.8.1.12. 74165.

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_TRYBB

Accession

Primary (citable) accession number: P39051

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	September 22, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)