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Protein

Trypanothione synthetase

Gene

TRS

Organism
Trypanosoma cruzi (strain CL Brener)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
    Sitei316Transition state stabilizerBy similarity1
    Metal bindingi318Magnesium 1By similarity1
    Metal bindingi332Magnesium 1By similarity1
    Metal bindingi332Magnesium 2By similarity1
    Metal bindingi334Magnesium 2By similarity1
    Binding sitei501ATPBy similarity1
    Binding sitei536ATPBy similarity1
    Binding sitei543ATP; via amide nitrogenBy similarity1
    Binding sitei571ATPBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi316 – 318ATPBy similarity3
    Nucleotide bindingi606 – 608ATPBy similarity3

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • glutathionylspermidine synthase activity Source: UniProtKB
    • metal ion binding Source: UniProtKB-KW
    • trypanothione synthase activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi6.3.1.9. 6524.

    Protein family/group databases

    MEROPSiC51.A01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trypanothione synthetaseImported (EC:6.3.1.9)
    Gene namesi
    Name:TRSImported
    Synonyms:TrySImported
    ORF Names:Tc00.1047053509099.50, Tc00.1047053509319.90
    OrganismiTrypanosoma cruzi (strain CL Brener)
    Taxonomic identifieri353153 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum
    Proteomesi
    • UP000002296 Componenti: Unassembled WGS sequence

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004031111 – 647Trypanothione synthetaseAdd BLAST647

    Proteomic databases

    PaxDbiQ9GT49.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi353153.XP_810600.1.

    Chemistry databases

    BindingDBiQ9GT49.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9GT49.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini26 – 166Peptidase C51PROSITE-ProRule annotationAdd BLAST141

    Sequence similaritiesi

    In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.Curated
    Contains 1 peptidase C51 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG410J4YY. Eukaryota.
    COG0754. LUCA.
    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

            10         20         30         40         50
    MPTLQSLAVP FGCVQGYAPG GIPAYSNKHE SYFSGERSID GNLFCGFKYQ
    60 70 80 90 100
    CVEFARRWLF ERKSLVLPDV DWAVHIFNLK EVSDARTGKP VRCVAIRNGT
    110 120 130 140 150
    AAKPVVDSLL IYPSDDYSPV GHVAAITEVG DKWVRIADQN HRFHKWDANY
    160 170 180 190 200
    AAELPLIHEK GVWTILDPLE DEVLKPLGWV TFPDTPDRNP NEPLVLHESL
    210 220 230 240 250
    HFKRGELPTL RRLTFTPTSR EKDWLDLTNE AEAYFADVCG IDVKNPKLEK
    260 270 280 290 300
    ASYYQMNREL YLDCAKYGNQ LHQMFLEATK FVLGSDELLR LFCIPEEYWP
    310 320 330 340 350
    RLRHSWETQP HAITGRFDFA FDEDTQQFKC FEYNADSAST LLECGVIQQK
    360 370 380 390 400
    WARSVGLDDG TTYSSGSLVS SRLQLAWEMA EVTGRVHFLI DNDDEEHYTA
    410 420 430 440 450
    LYVMQHASAA GLETKLCVLF DEFHFDENGV VVDSDGVAVT TVWKTWMWET
    460 470 480 490 500
    AIADHQKARV QRGNDWRPTP KDEVRLCDIL LGPNWDLRVF EPMWKIIPSN
    510 520 530 540 550
    KAILPIIYNK HPDHPALLRA SYELTVELQR TGYVRKPIVG RVGRNVTVTE
    560 570 580 590 600
    ASGDIAAKSD GDFSDRDMVY QELFRLPERD GYYAILGGWV IGDVYCGTGV
    610 620 630 640
    REDKTIITGL ESPFSALRVY QGAQRRPLTH EDLDKAEAAA VGGGLKT
    Length:647
    Mass (Da):73,458
    Last modified:March 1, 2001 - v1
    Checksum:iCA8C76ACD0D90F24
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural varianti2P → T in strain: Silvio X10/7. 1 Publication1
    Natural varianti5Q → K in strain: Silvio X10/7. 1 Publication1
    Natural varianti71D → E in allele TRS-2. 1 Publication1
    Natural varianti89K → Q in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti90P → N in allele TRS-2. 1 Publication1
    Natural varianti106V → A in allele TRS-2. 1 Publication1
    Natural varianti132K → N in allele TRS-2. 1 Publication1
    Natural varianti175K → R in allele TRS-2. 1 Publication1
    Natural varianti184D → E in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti207L → V in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti218T → N in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti237D → G in strain: Silvio X10/7. 1 Publication1
    Natural varianti237D → S in allele TRS-2. 1 Publication1
    Natural varianti248L → V in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti265A → T in allele TRS-2. 1 Publication1
    Natural varianti265A → V in strain: Silvio X10/7. 1 Publication1
    Natural varianti283L → I in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti288L → Q in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti291L → V in allele TRS-2. 1 Publication1
    Natural varianti293C → H in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti304 – 305HS → YL in strain: Silvio X10/7. 1 Publication2
    Natural varianti365S → C in allele TRS-2. 1 Publication1
    Natural varianti369V → I in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti381E → G in strain: Silvio X10/7. 1 Publication1
    Natural varianti392N → K in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti397H → Y in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti487L → M in strain: Silvio X10/7. 1 Publication1
    Natural varianti498P → S in strain: Silvio X10/7. 1 Publication1
    Natural varianti526V → I in strain: Silvio X10/7. 1 Publication1
    Natural varianti535R → K in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti562D → N in allele TRS-2 and strain Silvio X10/7. 2 Publications1
    Natural varianti564S → L in strain: Silvio X10/7. 1 Publication1
    Natural varianti604K → T in strain: Silvio X10/7. 1 Publication1
    Natural varianti615S → I in allele TRS-2. 1 Publication1
    Natural varianti615S → R in strain: Silvio X10/7. 1 Publication1
    Natural varianti624Q → P in allele TRS-2. 1 Publication1
    Natural varianti635K → N in strain: Silvio X10/7. 1 Publication1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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

    EnsemblProtistsiEAN88749; EAN88749; Tc00.1047053509319.90.
    EAN94225; EAN94225; Tc00.1047053509099.50.
    GeneIDi3541408.
    3547898.
    KEGGitcr:509099.50.
    tcr:509319.90.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    ProteinModelPortaliQ9GT49.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi353153.XP_810600.1.

    Chemistry databases

    BindingDBiQ9GT49.

    Protein family/group databases

    MEROPSiC51.A01.

    Proteomic databases

    PaxDbiQ9GT49.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblProtistsiEAN88749; EAN88749; Tc00.1047053509319.90.
    EAN94225; EAN94225; Tc00.1047053509099.50.
    GeneIDi3541408.
    3547898.
    KEGGitcr:509099.50.
    tcr:509319.90.

    Phylogenomic databases

    eggNOGiENOG410J4YY. Eukaryota.
    COG0754. LUCA.
    KOiK01833.

    Enzyme and pathway databases

    BRENDAi6.3.1.9. 6524.

    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]
    ProtoNetiSearch...

    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: October 5, 2016
    This is version 62 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.