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Reviewed, UniProtKB/Swiss-Prot P39040 (TYTR_CRIFA)

Last modified November 25, 2008. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
OrganismCrithidia fasciculata
Taxonomic identifier5656 [NCBI]
Taxonomic lineageEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Crithidia

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Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Post-translational modification

The N-terminus is blocked.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5-8.0.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Trypanothione reductase
PRO_0000067988

Regions

Nucleotide binding35 – 5117FAD

Sites

Active site4611Proton acceptor

Amino acid modifications

Disulfide bond52 ↔ 57Redox-active

Natural variations

Natural variant4791Q → E

Experimental info

Sequence conflict161G → R in AAA30322 and AAA30323. Ref.2
Sequence conflict621L → Y AA sequence Ref.3
Sequence conflict2971D → E in AAA30321, AAA30322 and AAA30323. Ref.2
Sequence conflict4541F → V in AAA30322 and AAA30323. Ref.2

Secondary structure

1 ................................................................................... 491
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P39040-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: EF749215A16F9187

FASTA49153,229
        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

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

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Cross-references

Sequence databases

Z12618 Genomic DNA. Translation: CAA78264.1.
M73323 mRNA. Translation: AAA30321.1.
M73324 Genomic DNA. Translation: AAA30322.1.
M73325 Genomic DNA. Translation: AAA30323.1.
PIRS28002.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FEAX-ray2.20A/B/C/D2-491[»]
1FEBX-ray2.00A/B2-491[»]
1FECX-ray1.70A/B2-491[»]
1TYPX-ray2.80A/B1-487[»]
1TYTX-ray2.60A1-487[»]
B2-487[»]
2TPRX-ray2.40A/B2-491[»]
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MON-13293.

Family and domain databases

InterProIPR013027. 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]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00411. PNDRDTASEI.
PR00470. TRYPANRDTASE.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01423. trypano_reduc. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP39040.

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Entry information

Entry nameTYTR_CRIFA
AccessionPrimary (citable) accession number: P39040
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 25, 2008
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents