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Q9GT49 (TRYS_TRYCC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 50. 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=6.3.1.8
EC=6.3.1.9
Gene names
Name:TRS
Synonyms:TryS
ORF Names:Tc00.1047053509099.50, Tc00.1047053509319.90
OrganismTrypanosoma cruzi (strain CL Brener) [Complete proteome]
Taxonomic identifier353153 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Protein attributes

Sequence length647 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme which catalyzes the formation of trypanothione (N1,N(8)-bis(glutathionyl)spermidine) from glutathione and spermidine. Converts spermidine or glutathionylspermidine into trypanothione. Can also convert aminopropylcadaverine into glutothionylaminopropylcadaverine and homotrypanothione. Also has low amidase activity, hydrolyzing trypanothione, homotrypanothione or glutathionylspermidine to form glutathione and the corresponding polyamine. Ref.1

Catalytic activity

Glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate. Ref.1

Glutathione + glutathionylspermidine + ATP = N1,N(8)-bis-(glutathionyl)spermidine + ADP + phosphate. Ref.1

Enzyme regulation

Subject to high-substrate inhibition by glutathione. Ref.1

Subunit structure

Monomer. Ref.1

Sequence similarities

In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.

Contains 1 peptidase C51 domain.

Biophysicochemical properties

Kinetic parameters:

KM=570 µM for glutathione with spermidine as cosubstrate Ref.1

KM=190 µM for glutathione with glutathionylspermidine as cosubstrate Ref.1

KM=53 µM for MgATP Ref.1

KM=625 µM for spermidine Ref.1

KM=662 µM for aminopropylcadaverine Ref.1

KM=66 µM for glutathionylspermidine Ref.1

pH dependence:

Optimum pH is 8.1 with spermidine as substrate. Optimum pH is 8.5 with glutathionylspermidine as substrate. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 647647Trypanothione synthetase
PRO_0000403111

Regions

Domain26 – 166141Peptidase C51
Nucleotide binding316 – 3183ATP By similarity
Nucleotide binding606 – 6083ATP By similarity

Sites

Metal binding3181Magnesium 1 By similarity
Metal binding3321Magnesium 1 By similarity
Metal binding3321Magnesium 2 By similarity
Metal binding3341Magnesium 2 By similarity
Binding site5011ATP By similarity
Binding site5361ATP By similarity
Binding site5431ATP; via amide nitrogen By similarity
Binding site5711ATP By similarity
Site3161Transition state stabilizer By similarity

Natural variations

Natural variant21P → T in strain Silvio X10/7. Ref.1
Natural variant51Q → K in strain Silvio X10/7. Ref.1
Natural variant711D → E in allele TRS-2. Ref.2 PubMed 16020724
Natural variant891K → Q in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant901P → N in allele TRS-2. Ref.2 PubMed 16020724
Natural variant1061V → A in allele TRS-2. Ref.2 PubMed 16020724
Natural variant1321K → N in allele TRS-2. Ref.2 PubMed 16020724
Natural variant1751K → R in allele TRS-2. Ref.2 PubMed 16020724
Natural variant1841D → E in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant2071L → V in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant2181T → N in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant2371D → G in strain Silvio X10/7. Ref.1
Natural variant2371D → S in allele TRS-2. Ref.2 PubMed 16020724
Natural variant2481L → V in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant2651A → T in allele TRS-2. Ref.2 PubMed 16020724
Natural variant2651A → V in strain Silvio X10/7. Ref.1
Natural variant2831L → I in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant2881L → Q in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant2911L → V in allele TRS-2. Ref.2 PubMed 16020724
Natural variant2931C → H in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant304 – 3052HS → YL in strain Silvio X10/7. Ref.1
Natural variant3651S → C in allele TRS-2. Ref.2 PubMed 16020724
Natural variant3691V → I in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant3811E → G in strain Silvio X10/7. Ref.1
Natural variant3921N → K in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant3971H → Y in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant4871L → M in strain Silvio X10/7. Ref.1
Natural variant4981P → S in strain Silvio X10/7. Ref.1
Natural variant5261V → I in strain Silvio X10/7. Ref.1
Natural variant5351R → K in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant5621D → N in allele TRS-2 and strain Silvio X10/7. Ref.1 Ref.2 PubMed 16020724
Natural variant5641S → L in strain Silvio X10/7. Ref.1
Natural variant6041K → T in strain Silvio X10/7. Ref.1
Natural variant6151S → I in allele TRS-2. Ref.2 PubMed 16020724
Natural variant6151S → R in strain Silvio X10/7. Ref.1
Natural variant6241Q → P in allele TRS-2. Ref.2 PubMed 16020724
Natural variant6351K → N in strain Silvio X10/7. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9GT49 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: CA8C76ACD0D90F24

FASTA64773,458
        10         20         30         40         50         60 
MPTLQSLAVP FGCVQGYAPG GIPAYSNKHE SYFSGERSID GNLFCGFKYQ CVEFARRWLF 

        70         80         90        100        110        120 
ERKSLVLPDV DWAVHIFNLK EVSDARTGKP VRCVAIRNGT AAKPVVDSLL IYPSDDYSPV 

       130        140        150        160        170        180 
GHVAAITEVG DKWVRIADQN HRFHKWDANY AAELPLIHEK GVWTILDPLE DEVLKPLGWV 

       190        200        210        220        230        240 
TFPDTPDRNP NEPLVLHESL HFKRGELPTL RRLTFTPTSR EKDWLDLTNE AEAYFADVCG 

       250        260        270        280        290        300 
IDVKNPKLEK ASYYQMNREL YLDCAKYGNQ LHQMFLEATK FVLGSDELLR LFCIPEEYWP 

       310        320        330        340        350        360 
RLRHSWETQP HAITGRFDFA FDEDTQQFKC FEYNADSAST LLECGVIQQK WARSVGLDDG 

       370        380        390        400        410        420 
TTYSSGSLVS SRLQLAWEMA EVTGRVHFLI DNDDEEHYTA LYVMQHASAA GLETKLCVLF 

       430        440        450        460        470        480 
DEFHFDENGV VVDSDGVAVT TVWKTWMWET AIADHQKARV QRGNDWRPTP KDEVRLCDIL 

       490        500        510        520        530        540 
LGPNWDLRVF EPMWKIIPSN KAILPIIYNK HPDHPALLRA SYELTVELQR TGYVRKPIVG 

       550        560        570        580        590        600 
RVGRNVTVTE ASGDIAAKSD GDFSDRDMVY QELFRLPERD GYYAILGGWV IGDVYCGTGV 

       610        620        630        640 
REDKTIITGL ESPFSALRVY QGAQRRPLTH EDLDKAEAAA VGGGLKT 

« Hide

References

« Hide 'large scale' references
[1]"A single enzyme catalyses formation of Trypanothione from glutathione and spermidine in Trypanosoma cruzi."
Oza S.L., Tetaud E., Ariyanayagam M.R., Warnon S.S., Fairlamb A.H.
J. Biol. Chem. 277:35853-35861(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
Strain: Silvio X10/7.
[2]"Trypanothione synthetase locus in Trypanosoma cruzi CL Brener strain shows an extensive allelic divergence."
Tran A.N., Andersson B., Pettersson U., Aslund L.
Acta Trop. 87:269-278(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES TRS-1 AND TRS-2), POLYMORPHISM.
Strain: CL Brener.
[3]"Trypanosoma cruzi (Tulahuen 0): expression, purification and functional characterization of an enzyme catalyzing trypanothione synthesis."
Comini M.A., Salame M., Menge U., Martinez R., Miglieta H., Claus J.D., Guerrero S.A., Flohe L.
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE TRS-1).
Strain: Tulahuen 0.
[4]"The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease."
El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., Anupama A., Arner E., Aslund L. expand/collapse author list , Attipoe P., Bontempi E., Bringaud F., Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H., da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G., Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y., Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J., Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y., Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L., Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J., Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C., Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D., Andersson B.
Science 309:409-415(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES TRS-1 AND TRS-2).
Strain: CL Brener.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF311782 Genomic DNA. Translation: AAL26803.1.
AF283000 Genomic DNA. Translation: AAG15408.1.
AF283001 Genomic DNA. Translation: AAG15409.1.
AY155571 Genomic DNA. Translation: AAO00722.1.
AAHK01000291 Genomic DNA. Translation: EAN94225.1.
AAHK01000838 Genomic DNA. Translation: EAN88749.1.
RefSeqXP_810600.1. XM_805507.1.
XP_816076.1. XM_810983.1.

3D structure databases

ProteinModelPortalQ9GT49.
SMRQ9GT49. Positions 8-620.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC51.A01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3541408.
3547898.
KEGGtcr:509099.50.
tcr:509319.90.

Phylogenomic databases

KOK01833.
ProtClustDBCLSZ2440485.

Family and domain databases

InterProIPR007921. CHAP_dom.
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. SSF52440. 1 hit.
PROSITEPS50911. CHAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRYS_TRYCC
AccessionPrimary (citable) accession number: Q9GT49
Secondary accession number(s): Q95WL5, Q9GT48
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: March 1, 2001
Last modified: October 16, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries