[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1453951 [NCBI, ExPASy, EBI, Israel, Japan] Aboagye-Kwarteng T., Smith K., Fairlamb A.H.; "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."; Mol. Microbiol. 6:3089-3099(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. DOI=10.1016/0166-6851(92)90243-D; PubMed=1542316 [NCBI, ExPASy, EBI, Israel, Japan] Field H., Cerami A., Henderson G.B.; "Cloning, sequencing, and demonstration of polymorphism in trypanothione reductase from Crithidia fasciculata."; Mol. Biochem. Parasitol. 50:47-56(1992).
[3]	PROTEIN SEQUENCE OF 39-62, AND CHARACTERIZATION. DOI=10.1021/bi00360a007; PubMed=3718941 [NCBI, ExPASy, EBI, Israel, Japan] Shames S.L., Fairlamb A.H., Cerami A., Walsh C.T.; "Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases."; Biochemistry 25:3519-3526(1986).
[4]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND DISULFIDE BOND. PubMed=8477734 [NCBI, ExPASy, EBI, Israel, Japan] Bailey S., Smith K., Fairlamb A.H., Hunter W.N.; "Substrate interactions between trypanothione reductase and N1-glutathionylspermidine disulphide at 0.28-nm resolution."; Eur. J. Biochem. 213:67-75(1993).
[5]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). DOI=10.1016/0022-2836(92)90701-K; PubMed=1522596 [NCBI, ExPASy, EBI, Israel, Japan] Hunter W.N., Bailey S., Habash J., Harrop S.J., Helliwell J.R., Aboagye-Kwarteng T., Smith K., Fairlamb A.H.; "Active site of trypanothione reductase. A target for rational drug design."; J. Mol. Biol. 227:322-333(1992).
[6]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). DOI=10.1107/S0907444993011898; PubMed=15299452 [NCBI, ExPASy, EBI, Israel, Japan] Bailey S., Fairlamb A.H., Hunter W.N.; "Structure of trypanothione reductase from Crithidia fasciculata at 2.6-A resolution; enzyme-NADP interactions at 2.8-A resolution."; Acta Crystallogr. D 50:139-154(1994).
[7]	X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). DOI=10.1107/S0907444994010772; PubMed=15299300 [NCBI, ExPASy, EBI, Israel, Japan] Strickland C.L., Puchalski R., Savvides S.N., Karplus P.A.; "Overexpression of Crithidia fasciculata trypanothione reductase and crystallization using a novel geometry."; Acta Crystallogr. D 51:337-341(1995).

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.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 7.5-8.0;
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
PTM: The N-terminus is blocked.
MISCELLANEOUS: The active site is a redox-active disulfide bond.
SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z12618; CAA78264.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M73323; AAA30321.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M73324; AAA30322.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M73325; AAA30323.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S28002; S28002.

3D structure databases

PDB

1FEA; X-ray; 2.20 A; A/B/C/D=2-491.	[ExPASy / RCSB / EBI]
1FEB; X-ray; 2.00 A; A/B=2-491.	[ExPASy / RCSB / EBI]
1FEC; X-ray; 1.70 A; A/B=2-491.	[ExPASy / RCSB / EBI]
1TYP; X-ray; 2.80 A; A/B=1-487.	[ExPASy / RCSB / EBI]
1TYT; X-ray; 2.60 A; A=1-487, B=2-487.	[ExPASy / RCSB / EBI]
2TPR; X-ray; 2.40 A; A/B=2-491.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1FEA; -.
1FEB; -.
1FEC; -.
1TYP; -.
1TYT; -.
2TPR; -.

ModBase

P39040.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13293; -.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR001864; Trypnth_redctse.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.
PR00470; TRYPANRDTASE.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01423; trypano_reduc; 1.

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

Other

P39040; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 491`	`491`	`Trypanothione reductase.`	`PRO_0000067988`
`NP_BIND`	`35 51`	`17`	`FAD.`
`ACT_SITE`	`461 461`		`Proton acceptor.`
`DISULFID`	`52 57`		`Redox-active.`
`VARIANT`	`479 479`	`1`	`Q -> E.`
`CONFLICT`	`16 16`		`G -> R (in Ref. 2; AAA30322/AAA30323).`
`CONFLICT`	`62 62`		`L -> Y (in Ref. 3; AA sequence).`
`CONFLICT`	`297 297`		`D -> E (in Ref. 2; AAA30321/AAA30322/AAA30323).`
`CONFLICT`	`454 454`		`F -> V (in Ref. 2; AAA30322/AAA30323).`
`STRAND`	`4 10`	`7`
`HELIX`	`14 27`	`14`
`STRAND`	`31 36`	`6`
`STRAND`	`38 41`	`4`
`TURN`	`42 44`	`3`
`HELIX`	`51 55`	`5`
`HELIX`	`57 75`	`19`
`TURN`	`76 80`	`5`
`STRAND`	`81 90`	`10`
`HELIX`	`92 115`	`24`
`STRAND`	`120 131`	`12`
`STRAND`	`134 142`	`9`
`STRAND`	`147 158`	`12`
`STRAND`	`162 164`	`3`
`HELIX`	`172 174`	`3`
`HELIX`	`178 181`	`4`
`STRAND`	`189 194`	`6`
`HELIX`	`198 210`	`13`
`STRAND`	`216 227`	`12`
`HELIX`	`232 243`	`12`
`TURN`	`244 246`	`3`
`STRAND`	`248 251`	`4`
`STRAND`	`255 260`	`6`
`STRAND`	`266 270`	`5`
`STRAND`	`275 283`	`9`
`STRAND`	`287 289`	`3`
`HELIX`	`292 294`	`3`
`TURN`	`296 300`	`5`
`STRAND`	`322 324`	`3`
`HELIX`	`326 329`	`4`
`HELIX`	`335 350`	`16`
`STRAND`	`364 366`	`3`
`STRAND`	`372 376`	`5`
`HELIX`	`379 383`	`5`
`STRAND`	`387 396`	`10`
`HELIX`	`400 404`	`5`
`STRAND`	`411 418`	`8`
`TURN`	`419 422`	`4`
`STRAND`	`423 431`	`9`
`HELIX`	`434 446`	`13`
`HELIX`	`451 455`	`5`
`HELIX`	`465 470`	`6`
`STRAND`	`475 479`	`5`
`STRAND`	`482 486`	`5`

Sequence information

Length: 491 AA [This is the length of the unprocessed precursor]

Molecular weight: 53229 Da [This is the MW of the unprocessed precursor]

CRC64: EF749215A16F9187 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRAYDLVVI GAGSGGLEAG WNAASLHKKR VAVIDLQKHH GPPHYAALGG TCVNVGCVPK 

        70         80         90        100        110        120 
KLMVTGANYM DTIRESAGFG WELDRESVRP NWKALIAAKN KAVSGINDSY EGMFADTEGL 

       130        140        150        160        170        180 
TFHQGFGALQ DNHTVLVRES ADPNSAVLET LDTEYILLAT GSWPQHLGIE GDDLCITSNE 

       190        200        210        220        230        240 
AFYLDEAPKR ALCVGGGYIS IEFAGIFNAY KARGGQVDLA YRGDMILRGF DSELRKQLTE 

       250        260        270        280        290        300 
QLRANGINVR THENPAKVTK NADGTRHVVF ESGAEADYDV VMLAIGRVPR SQTLQLDKAG 

       310        320        330        340        350        360 
VEVAKNGAIK VDAYSKTNVD NIYAIGDVTD RVMLTPVAIN EGAAFVDTVF ANKPRATDHT 

       370        380        390        400        410        420 
KVACAVFSIP PMGVCGYVEE DAAKKYDQVA VYESSFTPLM HNISGSTYKK FMVRIVTNHA 

       430        440        450        460        470        480 
DGEVLGVHML GDSSPEIIQS VAICLKMGAK ISDFYNTIGV HPTSAEELCS MRTPAYFYQK 

       490 
GKRVEKIDSN L

P39040 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools