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O60993 (TRYS_CRIFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trypanothione synthetase

EC=6.3.1.9
Alternative name(s):
Cf-TS
Gene names
Name:TRS
OrganismCrithidia fasciculata
Taxonomic identifier5656 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugates glutathione (gamma-Glu-Cys-Gly) and glutathionylspermidine to form trypanothione (N1,N(8)-bis(glutathionyl)spermidine), which is involved in maintaining intracellular thiol redox and in defense against oxidants.

Catalytic activity

Glutathione + glutathionylspermidine + ATP = N1,N(8)-bis-(glutathionyl)spermidine + ADP + phosphate.

Cofactor

Magnesium.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Contains 1 peptidase C51 domain.

Ontologies

Keywords
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionLigase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

trypanothione synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 652652Trypanothione synthetase
PRO_0000070445

Regions

Domain34 – 174141Peptidase C51

Sequences

Sequence LengthMass (Da)Tools
O60993 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 321BE90D39EEEA80

FASTA65274,517
        10         20         30         40         50         60 
MASAERVPVS FNKPGRVPFG EVQGYAPGHI PAYSNKHDHF FSGERSIDDN VFCGFKYQCV 

        70         80         90        100        110        120 
EFARRWLLER KGLVLPDVNW ACHIFKLKNV KDAATAEEVP VIAVRNGTEA KPEPDTLIIY 

       130        140        150        160        170        180 
PSSDVNTVGH VGAITEVGDD YVCIADQNYR FHKWEASYSY KLKLQHKDGV WTIIDDIDPN 

       190        200        210        220        230        240 
DVEIPLGWVT FPGYENRPEG AAPPALHPSL HFQPPEEPYL VRKTYEPTET KANWLDLNDP 

       250        260        270        280        290        300 
AEKLFVEEFG MDVSRSRLEE TTVNYYECDH EFHLRCIAYG TQLHDYFMEA TAQVINDDER 

       310        320        330        340        350        360 
LRIFKIPEEL WPRMRHSWKY QQTYISGRFD FAYNNETHQM KCFEYNADSA STLLECGRIQ 

       370        380        390        400        410        420 
QKWAESVGLD KEGTRGSGWA VERNLRTAWA TCGATGRVHF LVDDEKEEQY TALYCLQAAE 

       430        440        450        460        470        480 
AVGLEGKLCV MYDEFRFNEE GYVVDSDGVR VRNIWKTWMW ESAISDYFAA QAERGADWKA 

       490        500        510        520        530        540 
TPADKVRLCD LMLGKDWDIL YFEPMWKLIP SNKAILPIIY HNHPDHPAIL RAEYELTDEL 

       550        560        570        580        590        600 
RAVGYARKPI VGRVGRNVTI TDGTGEVHAE SGGNFGERDM IYQELFSLTK QDGYYAIIGG 

       610        620        630        640        650 
WMLGDAFSGT GIREDKSIIT GLDSPFAAIR IKINAIPRPL THKDLDKLAE DE 

« Hide

References

[1]"Cloning and characterization of the two enzymes responsible for trypanothione biosynthesis in Crithidia fasciculata."
Tetaud E., Manai F., Barrett M.P., Nadeau K., Walsh C.T., Fairlamb A.H.
J. Biol. Chem. 273:19383-19390(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 168-191; 232-255; 437-450; 457-474; 592-610 AND 617-630.
Strain: HS6.
[2]"Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata."
Smith K., Nadeau K., Bradley M., Walsh C., Fairlamb A.H.
Protein Sci. 1:874-883(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 168-191; 232-255; 437-450; 457-474; 592-610 AND 617-630, CHARACTERIZATION.
[3]"Convenient isolation and kinetic mechanism of glutathionylspermidine synthetase from Crithidia fasciculata."
Koenig K., Menge U., Kiess M., Wray V., Flohe L.
J. Biol. Chem. 272:11908-11915(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-36; 224-229; 235-242; 515-533; 550-561 AND 617-629, CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF006615 Genomic DNA. Translation: AAC39132.1.

3D structure databases

ProteinModelPortalO60993.
SMRO60993. Positions 1-632.
ModBaseSearch...

Protein family/group databases

MEROPSC51.A01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKO60993.

Family and domain databases

InterProIPR007921. CHAP.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view]
SUPFAMSSF52440. PreATP-grasp-like. 1 hit.
PROSITEPS50911. CHAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRYS_CRIFA
AccessionPrimary (citable) accession number: O60993
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: August 1, 1998
Last modified: April 3, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families