[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1021/bi00414a010; PubMed=3167026 [NCBI, ExPASy, EBI, Israel, Japan] Shames S.L., Kimmel B.E., Peoples O.P., Agabian N., Walsh C.T.; "Trypanothione reductase of Trypanosoma congolense: gene isolation, primary sequence determination, and comparison to glutathione reductase."; Biochemistry 27:5014-5019(1988).
[2]	REVIEW. DOI=10.1016/0968-0004(91)90124-E; PubMed=1957352 [NCBI, ExPASy, EBI, Israel, Japan] Walsh C.T., Bradley M., Nadeau K.; "Molecular studies on trypanothione reductase, a target for antiparasitic drugs."; Trends Biochem. Sci. 16:305-309(1991).

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).
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=18 µM for trypanothione;
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
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

M21122; AAA30258.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A27727; A27727.

3D structure databases

HSSP

P28593; 1NDA. [HSSP ENTRY / PDB]

ModBase

P13110.

Ontologies

GO:0015042;	Molecular function: trypanothione-disulfide reductase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
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.
PR00945; HGRDTASE.
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

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

Keywords

Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 492`	`492`	`Trypanothione reductase.`	`PRO_0000067991`
`NP_BIND`	`35 52`	`18`	`FAD (By similarity).`
`ACT_SITE`	`461 461`		`Proton acceptor (By similarity).`
`DISULFID`	`52 57`		`Redox-active (By similarity).`
`MUTAGEN`	`18 18`		`E->A: KM=266 uM for trypanothione.`
`MUTAGEN`	`21 21`		`W->R: KM=600 uM for trypanothione.`
`MUTAGEN`	`343 343`		`A->R: KM=9 uM for trypanothione.`

Sequence information

Length: 492 AA [This is the length of the unprocessed precursor]

Molecular weight: 53443 Da [This is the MW of the unprocessed precursor]

CRC64: 48F305A4C8C09685 [This is a checksum on the sequence]

        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

P13110 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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