ID GSP_CRIFA Reviewed; 719 AA. AC P90518; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 2. DT 27-MAR-2024, entry version 80. DE RecName: Full=Glutathionylspermidine synthase; DE EC=6.3.1.8; GN Name=GSP; 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 PARTIAL PROTEIN SEQUENCE. 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 191-209; 351-358; 512-530; 532-538 AND 695-710, AND RP 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). CC -!- FUNCTION: Conjugates glutathione (gamma-Glu-Cys-Gly) and spermidine to CC form glutathionylspermidine in the biosynthesis trypanothione CC (N(1),N(8)-bis(glutathionyl)spermidine), which is involved in CC maintaining 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=6.3.1.8; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U66520; AAC48361.2; -; Genomic_DNA. DR AlphaFoldDB; P90518; -. DR SMR; P90518; -. DR BindingDB; P90518; -. DR ChEMBL; CHEMBL3354; -. DR KEGG; ag:AAC48361; -. DR VEuPathDB; TriTrypDB:CFAC1_230008300; -. DR OrthoDB; 117498at2759; -. DR BRENDA; 6.3.1.8; 1365. DR SABIO-RK; P90518; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008885; F:glutathionylspermidine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.1490.330; -; 1. DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1. 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 PANTHER; PTHR30094; BIFUNCTIONAL GLUTATHIONYLSPERMIDINE SYNTHETASE/AMIDASE-RELATED; 1. DR PANTHER; PTHR30094:SF0; BIFUNCTIONAL GLUTATHIONYLSPERMIDINE SYNTHETASE_AMIDASE-RELATED; 1. DR Pfam; PF05257; CHAP; 1. DR Pfam; PF03738; GSP_synth; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 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..719 FT /note="Glutathionylspermidine synthase" FT /id="PRO_0000070442" FT DOMAIN 54..200 FT /note="Peptidase C51" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00048" FT BINDING 350..352 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 350 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 352 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 364 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 364 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 366 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 369 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 432 FT /ligand="spermidine" FT /ligand_id="ChEBI:CHEBI:57834" FT /evidence="ECO:0000250" FT BINDING 433 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 501 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 544 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 579 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 586 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 653 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 689..691 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT SITE 350 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 719 AA; 80322 MW; 46069BE9C40EEEFC CRC64; MSSLPHNHHY ETHHRGTAEV PFDELIGVTP DGVPVISNGN EAHFSNLESI TAACLPLSSF ERKAPCKQPY RKMGVKWQCV EFVRRYLASR KAVWMTSLCT AEEVWREENL FVDVRDGRPV EVVRTPNKST GPAPAVADIV VWGEGPETPF GHVAIVTEVC ASCVRVAEQN QGFEKWPEDV PFSREIAMRT TESGEVELLD EDPLLGWVTV QAPFYNFDDG DLADSFRLVV GQGQILRQPF PKHVDVPWLN TGEECDTILK HSLVVDGNMG EGAHAEEGDV PGAFYFLDYD MFCRLGRAAS SLHRIAMAAT AKVLEDPEST HLLEHYFGVP PEIQPLLRRS WEMTPPMGGR FDFGYDGKNV VMLEYNCDSS GALLECCNTQ EKMARFYGVS QGTSTGSFLG AKCVTYFQRL LTNEKVCPQH RLIHFMIDED DEERYTARCM MGFAEQAGFR TKLCVKLVNF RYRDGPPSNA APLATPCDHP TIVDGEDEEV LMVWKTWSWD TVLHQYHSQR SSSDAVNTPT LSDILLNNNI RVLEPLWKAV TGSKAILPFM HALAPDHEHM LAASFLPTRE IISRHYISKP VNGRAGQNIM MYDPVTSPTE LEGAPQQDIC EALSQNASAR SLLNGSPLPL SQSVDQTNEC SPGKFFDSVL VYQQRLFLKK FDGKYFPIFC GWMVGDEFGG VVVREDTSKI TKLSSMVVPA RVVRDNVPLG VSYSDEGET //