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Trypanothione synthetase (EC 6.3.1.9)

 TRYS_TRYCC              Reviewed;         647 AA.
Q9GT49; Q95WL5; Q9GT48;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
18-JUL-2018, entry version 69.
RecName: Full=Trypanothione synthetase {ECO:0000312|EMBL:AAL26803.1};
EC=6.3.1.9;
Name=TRS {ECO:0000312|EMBL:AAG15409.1};
Synonyms=TryS {ECO:0000312|EMBL:AAL26803.1};
ORFNames=Tc00.1047053509099.50, Tc00.1047053509319.90;
Trypanosoma cruzi (strain CL Brener).
Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma;
Schizotrypanum.
NCBI_TaxID=353153;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL26803.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND SUBUNIT.
STRAIN=Silvio X10/7 {ECO:0000269|PubMed:12121990};
PubMed=12121990; DOI=10.1074/jbc.M204403200;
Oza S.L., Tetaud E., Ariyanayagam M.R., Warnon S.S., Fairlamb A.H.;
"A single enzyme catalyses formation of Trypanothione from glutathione
and spermidine in Trypanosoma cruzi.";
J. Biol. Chem. 277:35853-35861(2002).
[2] {ECO:0000305, ECO:0000312|EMBL:AAG15409.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES TRS-1 AND TRS-2), AND
POLYMORPHISM.
STRAIN=CL Brener {ECO:0000312|EMBL:AAG15409.1};
PubMed=12826302; DOI=10.1016/S0001-706X(03)00067-6;
Tran A.N., Andersson B., Pettersson U., Aslund L.;
"Trypanothione synthetase locus in Trypanosoma cruzi CL Brener strain
shows an extensive allelic divergence.";
Acta Trop. 87:269-278(2003).
[3] {ECO:0000305, ECO:0000312|EMBL:AAO00722.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE TRS-1).
STRAIN=Tulahuen 0;
Comini M.A., Salame M., Menge U., Martinez R., Miglieta H.,
Claus J.D., Guerrero S.A., Flohe L.;
"Trypanosoma cruzi (Tulahuen 0): expression, purification and
functional characterization of an enzyme catalyzing trypanothione
synthesis.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES TRS-1 AND
TRS-2).
STRAIN=CL Brener;
PubMed=16020725; DOI=10.1126/science.1112631;
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.;
"The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
disease.";
Science 309:409-415(2005).
-!- FUNCTION: Bifunctional enzyme which catalyzes the formation of
trypanothione (N(1),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.
{ECO:0000269|PubMed:12121990}.
-!- CATALYTIC ACTIVITY: Glutathione + spermidine + ATP =
glutathionylspermidine + ADP + phosphate.
{ECO:0000269|PubMed:12121990}.
-!- CATALYTIC ACTIVITY: Glutathione + glutathionylspermidine + ATP =
N(1),N(8)-bis(glutathionyl)spermidine + ADP + phosphate.
{ECO:0000269|PubMed:12121990}.
-!- ENZYME REGULATION: Subject to high-substrate inhibition by
glutathione. {ECO:0000269|PubMed:12121990}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=570 uM for glutathione with spermidine as cosubstrate
{ECO:0000269|PubMed:12121990};
KM=190 uM for glutathione with glutathionylspermidine as
cosubstrate {ECO:0000269|PubMed:12121990};
KM=53 uM for MgATP {ECO:0000269|PubMed:12121990};
KM=625 uM for spermidine {ECO:0000269|PubMed:12121990};
KM=662 uM for aminopropylcadaverine
{ECO:0000269|PubMed:12121990};
KM=66 uM for glutathionylspermidine
{ECO:0000269|PubMed:12121990};
pH dependence:
Optimum pH is 8.1 with spermidine as substrate. Optimum pH is
8.5 with glutathionylspermidine as substrate.
{ECO:0000269|PubMed:12121990};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12121990}.
-!- SIMILARITY: In the C-terminal section; belongs to the
glutathionylspermidine synthase preATP-grasp family.
{ECO:0000305}.
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EMBL; AF311782; AAL26803.1; -; Genomic_DNA.
EMBL; AF283000; AAG15408.1; -; Genomic_DNA.
EMBL; AF283001; AAG15409.1; -; Genomic_DNA.
EMBL; AY155571; AAO00722.1; -; Genomic_DNA.
EMBL; AAHK01000291; EAN94225.1; -; Genomic_DNA.
EMBL; AAHK01000838; EAN88749.1; -; Genomic_DNA.
RefSeq; XP_810600.1; XM_805507.1.
RefSeq; XP_816076.1; XM_810983.1.
ProteinModelPortal; Q9GT49; -.
SMR; Q9GT49; -.
STRING; 353153.XP_810600.1; -.
BindingDB; Q9GT49; -.
MEROPS; C51.A01; -.
PaxDb; Q9GT49; -.
PRIDE; Q9GT49; -.
EnsemblProtists; EAN88749; EAN88749; Tc00.1047053509319.90.
EnsemblProtists; EAN94225; EAN94225; Tc00.1047053509099.50.
GeneDB; TcCLB.509099.50:pep; -.
GeneDB; TcCLB.509319.90:pep; -.
GeneID; 3541408; -.
GeneID; 3547898; -.
KEGG; tcr:509099.50; -.
KEGG; tcr:509319.90; -.
eggNOG; ENOG410J4YY; Eukaryota.
eggNOG; COG0754; LUCA.
KO; K01833; -.
BRENDA; 6.3.1.9; 6524.
Proteomes; UP000002296; Unassembled WGS sequence.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008885; F:glutathionylspermidine synthase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0047479; F:trypanothione synthase activity; IDA:UniProtKB.
GO; GO:0019342; P:trypanothione biosynthetic process; IDA:UniProtKB.
InterPro; IPR007921; CHAP_dom.
InterPro; IPR005494; GSPS_pre-ATP-grasp-like_dom.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR016185; PreATP-grasp_dom_sf.
Pfam; PF05257; CHAP; 1.
Pfam; PF03738; GSP_synth; 1.
SUPFAM; SSF52440; SSF52440; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS50911; CHAP; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Ligase; Magnesium; Metal-binding;
Multifunctional enzyme; Nucleotide-binding; Polymorphism;
Reference proteome.
CHAIN 1 647 Trypanothione synthetase.
/FTId=PRO_0000403111.
DOMAIN 26 166 Peptidase C51. {ECO:0000255|PROSITE-
ProRule:PRU00048}.
NP_BIND 316 318 ATP. {ECO:0000250}.
NP_BIND 606 608 ATP. {ECO:0000250}.
METAL 318 318 Magnesium 1. {ECO:0000250}.
METAL 332 332 Magnesium 1. {ECO:0000250}.
METAL 332 332 Magnesium 2. {ECO:0000250}.
METAL 334 334 Magnesium 2. {ECO:0000250}.
BINDING 501 501 ATP. {ECO:0000250}.
BINDING 536 536 ATP. {ECO:0000250}.
BINDING 543 543 ATP; via amide nitrogen. {ECO:0000250}.
BINDING 571 571 ATP. {ECO:0000250}.
SITE 316 316 Transition state stabilizer.
{ECO:0000250}.
VARIANT 2 2 P -> T (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 5 5 Q -> K (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 71 71 D -> E (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 89 89 K -> Q (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 90 90 P -> N (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 106 106 V -> A (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 132 132 K -> N (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 175 175 K -> R (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 184 184 D -> E (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 207 207 L -> V (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 218 218 T -> N (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 237 237 D -> G (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 237 237 D -> S (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 248 248 L -> V (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 265 265 A -> T (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 265 265 A -> V (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 283 283 L -> I (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 288 288 L -> Q (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 291 291 L -> V (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 293 293 C -> H (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 304 305 HS -> YL (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 365 365 S -> C (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 369 369 V -> I (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 381 381 E -> G (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 392 392 N -> K (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 397 397 H -> Y (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 487 487 L -> M (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 498 498 P -> S (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 526 526 V -> I (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 535 535 R -> K (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 562 562 D -> N (in allele TRS-2 and strain Silvio
X10/7). {ECO:0000269|PubMed:12121990,
ECO:0000269|PubMed:12826302}.
VARIANT 564 564 S -> L (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 604 604 K -> T (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 615 615 S -> I (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 615 615 S -> R (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
VARIANT 624 624 Q -> P (in allele TRS-2).
{ECO:0000269|PubMed:12826302}.
VARIANT 635 635 K -> N (in strain: Silvio X10/7).
{ECO:0000269|PubMed:12121990}.
SEQUENCE 647 AA; 73458 MW; CA8C76ACD0D90F24 CRC64;
MPTLQSLAVP FGCVQGYAPG GIPAYSNKHE SYFSGERSID GNLFCGFKYQ CVEFARRWLF
ERKSLVLPDV DWAVHIFNLK EVSDARTGKP VRCVAIRNGT AAKPVVDSLL IYPSDDYSPV
GHVAAITEVG DKWVRIADQN HRFHKWDANY AAELPLIHEK GVWTILDPLE DEVLKPLGWV
TFPDTPDRNP NEPLVLHESL HFKRGELPTL RRLTFTPTSR EKDWLDLTNE AEAYFADVCG
IDVKNPKLEK ASYYQMNREL YLDCAKYGNQ LHQMFLEATK FVLGSDELLR LFCIPEEYWP
RLRHSWETQP HAITGRFDFA FDEDTQQFKC FEYNADSAST LLECGVIQQK WARSVGLDDG
TTYSSGSLVS SRLQLAWEMA EVTGRVHFLI DNDDEEHYTA LYVMQHASAA GLETKLCVLF
DEFHFDENGV VVDSDGVAVT TVWKTWMWET AIADHQKARV QRGNDWRPTP KDEVRLCDIL
LGPNWDLRVF EPMWKIIPSN KAILPIIYNK HPDHPALLRA SYELTVELQR TGYVRKPIVG
RVGRNVTVTE ASGDIAAKSD GDFSDRDMVY QELFRLPERD GYYAILGGWV IGDVYCGTGV
REDKTIITGL ESPFSALRVY QGAQRRPLTH EDLDKAEAAA VGGGLKT


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