ID A0A0V0UME8_9BILA Unreviewed; 894 AA.
AC A0A0V0UME8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glutathione synthetase {ECO:0000256|ARBA:ARBA00020821};
DE EC=6.3.2.3 {ECO:0000256|ARBA:ARBA00012214};
DE AltName: Full=Glutathione synthase {ECO:0000256|ARBA:ARBA00030403};
GN ORFNames=T09_2725 {ECO:0000313|EMBL:KRX52464.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX52464.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX52464.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX52464.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP +
CC glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
CC ChEBI:CHEBI:456216; EC=6.3.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00029288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13558;
CC Evidence={ECO:0000256|ARBA:ARBA00029288};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 2/2. {ECO:0000256|ARBA:ARBA00004965}.
CC -!- SIMILARITY: Belongs to the eukaryotic GSH synthase family.
CC {ECO:0000256|ARBA:ARBA00010385}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX52464.1}.
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DR EMBL; JYDN01000245; KRX52464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UME8; -.
DR STRING; 181606.A0A0V0UME8; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd01671; CARD; 1.
DR CDD; cd00032; CASc; 1.
DR Gene3D; 3.30.1490.50; -; 1.
DR Gene3D; 3.30.1490.80; -; 1.
DR Gene3D; 3.40.50.1460; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 3.40.50.1760; Glutathione synthase, substrate-binding domain superfamily, eukaryotic; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR005615; Glutathione_synthase.
DR InterPro; IPR014042; Glutathione_synthase_a-hlx.
DR InterPro; IPR014709; Glutathione_synthase_C_euk.
DR InterPro; IPR014049; Glutathione_synthase_N_euk.
DR InterPro; IPR037013; GSH-S_sub-bd_sf.
DR InterPro; IPR004887; GSH_synth_subst-bd.
DR InterPro; IPR011600; Pept_C14_caspase.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01986; glut_syn_euk; 1.
DR PANTHER; PTHR11130; GLUTATHIONE SYNTHETASE; 1.
DR PANTHER; PTHR11130:SF0; GLUTATHIONE SYNTHETASE; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF03917; GSH_synth_ATP; 1.
DR Pfam; PF03199; GSH_synthase; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 1..89
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT DOMAIN 179..303
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 337..398
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
SQ SEQUENCE 894 AA; 100507 MW; 30FBBB189EABA3E2 CRC64;
MDDWQRQALD SNLIALADSL DLIELLPFLQ QKGILREYHV DAIRKKTPYE ARLEFVSIIK
RRGPNAFEAL CEGLARSGQT HLEQALRSCK SPNQPVEINN GSGGGGQLME CPEELNSNPQ
ETKLQLVKTS AEQYYFAESI LFSDVPMTDG LLSWLKVKNE GTIPADYNTV DCYKHSSKPK
GLALIINNCA FTCDLPNRLG SDIDCKNIYR LLTDLGYDVI KKHNLTAKGI VETMVKFSLN
KEHERCDSAV VVILTHGLEG EIYGSDGGLV SVQKMIQLLD AVNCPALKNK PKLFFLQACR
GQRYDSGHDV IDSGDAIGSA NARCKLNSLD ENDAAALRRK VPTQADILIA YSTTPGFVSW
RNSLRGTWFI QAVCEVFSEY AWKEEVLHLF TRMSTVFSKI KLPPGITFDE LIDSAKDWAQ
IHGLCIRLPG KYENSDEVQL APFTLLPSPF SKSCFDTAVN LHQAMMAVYH QIAFDYDFME
DALSPVMLSD VFVSKLFGIY RAVMKHGNMM SRLVLNIQRC DYMMQEEPNS SYSLKQVEVN
HVAASFAGLG VQCRQWHRLM LSQMVENAKL DLLPENHALE TVALGLLSAW RAYGHSEAII
LIMVEDELRN FADQRLVEYK IQSLAEFQHV PMRRFRLTHC PGNVAVDRRG RLMLNGVEVA
VVYYRTGYLP KHFPNEDVWS AFLQIELSEA IKCPWIGFHL AGMKRMQLLL SNSDTLRSVI
DKTKLLVWPV NMKRKILDDD DDEMYRQMKS VTVPMHDLDP SKAGADELMK HVDANADNFV
LKPHLEGGGN NFYGQNLIKQ LNQLCSNERS AYVLMERIRP PTFDNWIIRA NIPAQQTSVV
SELGTFGYSL ATGQQIISCS RDGGFLLRTK PSKEDEGGVM VGAAALDTPH LLLP
//
