NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MHOM/ET/67/HU3;
DOI=10.1016/0166-6851(94)00034-4; PubMed=7935607 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor M.C., Kelly J.M., Chapman C.J., Fairlamb A.H., Miles M.A.;
"The structure, organization, and expression of the Leishmania donovani gene encoding trypanothione reductase.";
Mol. Biochem. Parasitol. 64:293-301(1994).

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: 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

Z23135; CAA80668.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S34376; S34376.

3D structure databases

HSSP

P39040; 1TYT. [HSSP ENTRY / PDB]

ModBase

P39050.

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.
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

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`	`1 491`	`491`	`Trypanothione reductase.`	`PRO_0000067989`
`NP_BIND`	`35 52`	`18`	`FAD (By similarity).`
`ACT_SITE`	`461 461`		`Proton acceptor (By similarity).`
`DISULFID`	`52 57`		`Redox-active (By similarity).`

Sequence information

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

Molecular weight: 52933 Da [This is the MW of the unprocessed precursor]

CRC64: 5A777DA32E8E752A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRAYDLVVL GAGSGGLEAG WNAAVTHKKK VAVVDVQATH GPPALVALGG TCVNVGCVPK 

        70         80         90        100        110        120 
KLMVTGAQYM DLIRESGGFG WEMDRESLCP NWKTLIAAKN KVVNSINESY KSMFADTEGL 

       130        140        150        160        170        180 
SFHMGFGALQ DAHTVVVRKS EDPHSDVLET LDTEYILIAT GSWPTRLGVP GDEFCITSNE 

       190        200        210        220        230        240 
AFYLEDAPKR MLCVGGGYIA VEFAGIFNGY KPCGGYVDLC YRGDLILRGF DTEVRKSLTK 

       250        260        270        280        290        300 
QLGANGIRVR TNLNPTKITK NEDGSNHVHF NDGTEEDYDQ VMLAIGVPRS QALQLDKAGV 

       310        320        330        340        350        360 
RTGKNGAVQV DAYSKTSVDN IYAIGDVTNR VMLTPVAINE GACVLLETVF GGKPRATDHT 

       370        380        390        400        410        420 
KVACAVFSIP PIGTCGMTEE EAAKNYETVA VYASSFTPLM HNISGSKHKE FMIRIITNES 

       430        440        450        460        470        480 
NGEVLGVHML GDSAPEIIQS VGICMKMGAK ISDFHSTIGV HPTSAEELCS MRTPAYFYES 

       490 
GKRVEKLSSN L

P39050 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