GSHB_XENLA
ID GSHB_XENLA Reviewed; 474 AA.
AC P35668;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Glutathione synthetase {ECO:0000250|UniProtKB:P48637};
DE Short=GSH synthetase;
DE Short=GSH-S;
DE EC=6.3.2.3 {ECO:0000250|UniProtKB:P48637};
DE AltName: Full=Glutathione synthase;
GN Name=gss;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7916638; DOI=10.1016/0167-4781(93)90202-o;
RA Habenicht A., Hille S., Knoechel W.;
RT "Molecular cloning of the large subunit of glutathione synthetase from
RT Xenopus laevis embryos.";
RL Biochim. Biophys. Acta 1174:295-298(1993).
CC -!- FUNCTION: Catalyzes the production of glutathione from gamma-
CC glutamylcysteine and glycine in an ATP-dependent manner. Glutathione
CC (gamma-glutamylcysteinylglycine, GSH) is the most abundant
CC intracellular thiol in living aerobic cells and is required for
CC numerous processes including the protection of cells against oxidative
CC damage, amino acid transport, the detoxification of foreign compounds,
CC the maintenance of protein sulfhydryl groups in a reduced state and
CC acts as a cofactor for a number of enzymes.
CC {ECO:0000250|UniProtKB:P48637}.
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:0000250|UniProtKB:P48637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13558;
CC Evidence={ECO:0000250|UniProtKB:P48637};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P48637};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P48637};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 2/2. {ECO:0000250|UniProtKB:P48637}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P48637}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- SIMILARITY: Belongs to the eukaryotic GSH synthase family.
CC {ECO:0000305}.
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DR EMBL; X69662; CAA49351.1; -; mRNA.
DR PIR; S38333; S38333.
DR RefSeq; NP_001081013.1; NM_001087544.1.
DR AlphaFoldDB; P35668; -.
DR SMR; P35668; -.
DR DNASU; 394329; -.
DR GeneID; 394329; -.
DR KEGG; xla:394329; -.
DR CTD; 394329; -.
DR Xenbase; XB-GENE-6254454; gss.L.
DR OrthoDB; 1189955at2759; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 394329; Expressed in muscle tissue and 19 other tissues.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR CDD; cd00228; eu-GS; 1.
DR Gene3D; 1.10.1080.10; -; 1.
DR Gene3D; 3.30.1490.50; -; 1.
DR Gene3D; 3.30.1490.80; -; 1.
DR Gene3D; 3.40.50.1760; -; 1.
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; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11130; PTHR11130; 1.
DR Pfam; PF03917; GSH_synth_ATP; 1.
DR Pfam; PF03199; GSH_synthase; 1.
DR PIRSF; PIRSF001558; GSHase; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01986; glut_syn_euk; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glutathione biosynthesis; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..474
FT /note="Glutathione synthetase"
FT /id="PRO_0000211264"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 148..151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267..270
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 364..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 398..401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 461..462
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 474 AA; 53584 MW; 52CAA42C44079702 CRC64;
MADLWDDIYN DTKLLEELAP IAIDAALLQG VLMRTKESPN SSDVVSFAPF ALLPSPVPKA
LFEQAKCVQE DFNTLVDRIS QDTSFLEQVL SSTIKVDDFI RRLFAIHKQV QQEDCTQEVF
LGINRSDYMF DCRDDGTPAL KQIEINTIAA SFGGLASRTP AVHQHVLKFL RKSEESSSIL
TNDAVEGIGW GIAHAWALYG SVDATVMFLV ENEQRNILDQ RFIEAELCKR NVRVIRRRLA
DVFERGTLDE ERHLFIDGYE VAVAYFRTGY VPQDYTEQDW EARLMLERSR AVKCPDVPTQ
LVGTKKVQQE LSRPQILEKF LPDKPEAVAR IRETFTGLYS LDIGEEGDEA VRVALANPDQ
FVLKPQREGG GNNLYGEELK EKLQECKDSE ERTSYILMDK INPKPLKNCL LRAGGRVQIS
ECISELGMFG VYVRHRDQMI YYDQVGHLLR TKAIEHSDGG VAAGVAVLDN PYLV
