TRYS_CRIFA
ID TRYS_CRIFA Reviewed; 652 AA.
AC O60993;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Trypanothione synthetase;
DE EC=6.3.1.9;
DE AltName: Full=Cf-TS;
GN Name=TRS;
OS Crithidia fasciculata.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX NCBI_TaxID=5656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 168-191;
RP 232-255; 437-450; 457-474; 592-610 AND 617-630.
RC STRAIN=HS6;
RX PubMed=9677355; DOI=10.1074/jbc.273.31.19383;
RA Tetaud E., Manai F., Barrett M.P., Nadeau K., Walsh C.T., Fairlamb A.H.;
RT "Cloning and characterization of the two enzymes responsible for
RT trypanothione biosynthesis in Crithidia fasciculata.";
RL J. Biol. Chem. 273:19383-19390(1998).
RN [2]
RP PROTEIN SEQUENCE OF 168-191; 232-255; 437-450; 457-474; 592-610 AND
RP 617-630, AND CHARACTERIZATION.
RX PubMed=1304372; DOI=10.1002/pro.5560010705;
RA Smith K., Nadeau K., Bradley M., Walsh C., Fairlamb A.H.;
RT "Purification of glutathionylspermidine and trypanothione synthetases from
RT Crithidia fasciculata.";
RL Protein Sci. 1:874-883(1992).
RN [3]
RP PROTEIN SEQUENCE OF 17-36; 224-229; 235-242; 515-533; 550-561 AND 617-629,
RP AND CHARACTERIZATION.
RX PubMed=9115252; DOI=10.1074/jbc.272.18.11908;
RA Koenig K., Menge U., Kiess M., Wray V., Flohe L.;
RT "Convenient isolation and kinetic mechanism of glutathionylspermidine
RT synthetase from Crithidia fasciculata.";
RL J. Biol. Chem. 272:11908-11915(1997).
CC -!- FUNCTION: Conjugates glutathione (gamma-Glu-Cys-Gly) and
CC glutathionylspermidine to form trypanothione (N(1),N(8)-
CC bis(glutathionyl)spermidine), which is involved in maintaining
CC intracellular thiol redox and in defense against oxidants.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione + spermidine = ADP + glutathionylspermidine
CC + H(+) + phosphate; Xref=Rhea:RHEA:21272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57834,
CC ChEBI:CHEBI:57835, ChEBI:CHEBI:57925, ChEBI:CHEBI:456216; EC=6.3.1.9;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione + glutathionylspermidine = ADP + H(+) +
CC phosphate + trypanothione; Xref=Rhea:RHEA:21532, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57835,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58290, ChEBI:CHEBI:456216; EC=6.3.1.9;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC glutathionylspermidine synthase preATP-grasp family. {ECO:0000305}.
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DR EMBL; AF006615; AAC39132.1; -; Genomic_DNA.
DR AlphaFoldDB; O60993; -.
DR SMR; O60993; -.
DR KEGG; ag:AAC39132; -.
DR VEuPathDB; TriTrypDB:CFAC1_210035400; -.
DR BRENDA; 6.3.1.9; 1365.
DR SABIO-RK; O60993; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008885; F:glutathionylspermidine synthase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047479; F:trypanothione synthase activity; IEA:UniProtKB-EC.
DR InterPro; IPR007921; CHAP_dom.
DR InterPro; IPR005494; GSPS_pre-ATP-grasp-like_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF05257; CHAP; 1.
DR Pfam; PF03738; GSP_synth; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50911; CHAP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..652
FT /note="Trypanothione synthetase"
FT /id="PRO_0000070445"
FT DOMAIN 34..174
FT /note="Peptidase C51"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
FT BINDING 328..330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 618..620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 328
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 652 AA; 74517 MW; 321BE90D39EEEA80 CRC64;
MASAERVPVS FNKPGRVPFG EVQGYAPGHI PAYSNKHDHF FSGERSIDDN VFCGFKYQCV
EFARRWLLER KGLVLPDVNW ACHIFKLKNV KDAATAEEVP VIAVRNGTEA KPEPDTLIIY
PSSDVNTVGH VGAITEVGDD YVCIADQNYR FHKWEASYSY KLKLQHKDGV WTIIDDIDPN
DVEIPLGWVT FPGYENRPEG AAPPALHPSL HFQPPEEPYL VRKTYEPTET KANWLDLNDP
AEKLFVEEFG MDVSRSRLEE TTVNYYECDH EFHLRCIAYG TQLHDYFMEA TAQVINDDER
LRIFKIPEEL WPRMRHSWKY QQTYISGRFD FAYNNETHQM KCFEYNADSA STLLECGRIQ
QKWAESVGLD KEGTRGSGWA VERNLRTAWA TCGATGRVHF LVDDEKEEQY TALYCLQAAE
AVGLEGKLCV MYDEFRFNEE GYVVDSDGVR VRNIWKTWMW ESAISDYFAA QAERGADWKA
TPADKVRLCD LMLGKDWDIL YFEPMWKLIP SNKAILPIIY HNHPDHPAIL RAEYELTDEL
RAVGYARKPI VGRVGRNVTI TDGTGEVHAE SGGNFGERDM IYQELFSLTK QDGYYAIIGG
WMLGDAFSGT GIREDKSIIT GLDSPFAAIR IKINAIPRPL THKDLDKLAE DE
