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Q9GT49

- TRYS_TRYCC

UniProt

Q9GT49 - TRYS_TRYCC

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Protein
Trypanothione synthetase
Gene
TRS, TryS, Tc00.1047053509099.50, Tc00.1047053509319.90
Organism
Trypanosoma cruzi (strain CL Brener)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Enzyme regulationi

Subject to high-substrate inhibition by glutathione.1 Publication

Kineticsi

  1. KM=570 µM for glutathione with spermidine as cosubstrate1 Publication
  2. KM=190 µM for glutathione with glutathionylspermidine as cosubstrate1 Publication
  3. KM=53 µM for MgATP1 Publication
  4. KM=625 µM for spermidine1 Publication
  5. KM=662 µM for aminopropylcadaverine1 Publication
  6. KM=66 µM for glutathionylspermidine1 Publication

pH dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei316 – 3161Transition state stabilizer By similarity
Metal bindingi318 – 3181Magnesium 1 By similarity
Metal bindingi332 – 3321Magnesium 1 By similarity
Metal bindingi332 – 3321Magnesium 2 By similarity
Metal bindingi334 – 3341Magnesium 2 By similarity
Binding sitei501 – 5011ATP By similarity
Binding sitei536 – 5361ATP By similarity
Binding sitei543 – 5431ATP; via amide nitrogen By similarity
Binding sitei571 – 5711ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi316 – 3183ATP By similarity
Nucleotide bindingi606 – 6083ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutathionylspermidine synthase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. trypanothione synthase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. trypanothione biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Protein family/group databases

MEROPSiC51.A01.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypanothione synthetase (EC:6.3.1.9)
Gene namesi
Name:TRS
Synonyms:TryS
ORF Names:Tc00.1047053509099.50, Tc00.1047053509319.90
OrganismiTrypanosoma cruzi (strain CL Brener)
Taxonomic identifieri353153 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum
ProteomesiUP000002296: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 647647Trypanothione synthetase
PRO_0000403111Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9GT49.
SMRiQ9GT49. Positions 8-620.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 166141Peptidase C51
Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

KOiK01833.

Family and domain databases

InterProiIPR007921. CHAP_dom.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS50911. CHAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9GT49-1 [UniParc]FASTAAdd to Basket

« Hide

MPTLQSLAVP FGCVQGYAPG GIPAYSNKHE SYFSGERSID GNLFCGFKYQ    50
CVEFARRWLF ERKSLVLPDV DWAVHIFNLK EVSDARTGKP VRCVAIRNGT 100
AAKPVVDSLL IYPSDDYSPV GHVAAITEVG DKWVRIADQN HRFHKWDANY 150
AAELPLIHEK GVWTILDPLE DEVLKPLGWV TFPDTPDRNP NEPLVLHESL 200
HFKRGELPTL RRLTFTPTSR EKDWLDLTNE AEAYFADVCG IDVKNPKLEK 250
ASYYQMNREL YLDCAKYGNQ LHQMFLEATK FVLGSDELLR LFCIPEEYWP 300
RLRHSWETQP HAITGRFDFA FDEDTQQFKC FEYNADSAST LLECGVIQQK 350
WARSVGLDDG TTYSSGSLVS SRLQLAWEMA EVTGRVHFLI DNDDEEHYTA 400
LYVMQHASAA GLETKLCVLF DEFHFDENGV VVDSDGVAVT TVWKTWMWET 450
AIADHQKARV QRGNDWRPTP KDEVRLCDIL LGPNWDLRVF EPMWKIIPSN 500
KAILPIIYNK HPDHPALLRA SYELTVELQR TGYVRKPIVG RVGRNVTVTE 550
ASGDIAAKSD GDFSDRDMVY QELFRLPERD GYYAILGGWV IGDVYCGTGV 600
REDKTIITGL ESPFSALRVY QGAQRRPLTH EDLDKAEAAA VGGGLKT 647
Length:647
Mass (Da):73,458
Last modified:March 1, 2001 - v1
Checksum:iCA8C76ACD0D90F24
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21P → T in strain: Silvio X10/7. 1 Publication
Natural varianti5 – 51Q → K in strain: Silvio X10/7. 1 Publication
Natural varianti71 – 711D → E in allele TRS-2. 2 Publications
Natural varianti89 – 891K → Q in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti90 – 901P → N in allele TRS-2. 2 Publications
Natural varianti106 – 1061V → A in allele TRS-2. 2 Publications
Natural varianti132 – 1321K → N in allele TRS-2. 2 Publications
Natural varianti175 – 1751K → R in allele TRS-2. 2 Publications
Natural varianti184 – 1841D → E in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti207 – 2071L → V in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti218 – 2181T → N in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti237 – 2371D → G in strain: Silvio X10/7. 1 Publication
Natural varianti237 – 2371D → S in allele TRS-2. 2 Publications
Natural varianti248 – 2481L → V in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti265 – 2651A → T in allele TRS-2. 2 Publications
Natural varianti265 – 2651A → V in strain: Silvio X10/7. 1 Publication
Natural varianti283 – 2831L → I in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti288 – 2881L → Q in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti291 – 2911L → V in allele TRS-2. 2 Publications
Natural varianti293 – 2931C → H in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti304 – 3052HS → YL in strain: Silvio X10/7. 1 Publication
Natural varianti365 – 3651S → C in allele TRS-2. 2 Publications
Natural varianti369 – 3691V → I in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti381 – 3811E → G in strain: Silvio X10/7. 1 Publication
Natural varianti392 – 3921N → K in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti397 – 3971H → Y in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti487 – 4871L → M in strain: Silvio X10/7. 1 Publication
Natural varianti498 – 4981P → S in strain: Silvio X10/7. 1 Publication
Natural varianti526 – 5261V → I in strain: Silvio X10/7. 1 Publication
Natural varianti535 – 5351R → K in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti562 – 5621D → N in allele TRS-2 and strain Silvio X10/7. 3 Publications
Natural varianti564 – 5641S → L in strain: Silvio X10/7. 1 Publication
Natural varianti604 – 6041K → T in strain: Silvio X10/7. 1 Publication
Natural varianti615 – 6151S → I in allele TRS-2. 2 Publications
Natural varianti615 – 6151S → R in strain: Silvio X10/7. 1 Publication
Natural varianti624 – 6241Q → P in allele TRS-2. 2 Publications
Natural varianti635 – 6351K → N in strain: Silvio X10/7. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiXP_810600.1. XM_805507.1.
XP_816076.1. XM_810983.1.

Genome annotation databases

GeneIDi3541408.
3547898.
KEGGitcr:509099.50.
tcr:509319.90.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi XP_810600.1. XM_805507.1.
XP_816076.1. XM_810983.1.

3D structure databases

ProteinModelPortali Q9GT49.
SMRi Q9GT49. Positions 8-620.
ModBasei Search...

Protein family/group databases

MEROPSi C51.A01.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3541408.
3547898.
KEGGi tcr:509099.50.
tcr:509319.90.

Phylogenomic databases

KOi K01833.

Family and domain databases

InterProi IPR007921. CHAP_dom.
IPR005494. GSPS_pre-ATP-grasp-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view ]
Pfami PF05257. CHAP. 1 hit.
PF03738. GSP_synth. 1 hit.
[Graphical view ]
SUPFAMi SSF52440. SSF52440. 1 hit.
PROSITEi PS50911. CHAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTRYS_TRYCC
AccessioniPrimary (citable) accession number: Q9GT49
Secondary accession number(s): Q95WL5, Q9GT48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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