GSHB_MACFA
ID GSHB_MACFA Reviewed; 474 AA.
AC Q8HXX5;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
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; ORFNames=QccE-14611;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RA Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the eukaryotic GSH synthase family.
CC {ECO:0000305}.
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DR EMBL; AB083314; BAC20593.1; -; mRNA.
DR RefSeq; NP_001270338.1; NM_001283409.1.
DR AlphaFoldDB; Q8HXX5; -.
DR SMR; Q8HXX5; -.
DR STRING; 9541.XP_005568857.1; -.
DR PRIDE; Q8HXX5; -.
DR GeneID; 101866287; -.
DR CTD; 2937; -.
DR eggNOG; KOG0021; Eukaryota.
DR OrthoDB; 1189955at2759; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000233100; Unplaced.
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 Acetylation; ATP-binding; Glutathione biosynthesis; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P48637"
FT CHAIN 2..474
FT /note="Glutathione synthetase"
FT /id="PRO_0000211261"
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"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P48637"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48637"
SQ SEQUENCE 474 AA; 52413 MW; ECFB2A446B007C4D CRC64;
MATNWGSLLQ NEQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF TLFPSLVPSA
LLEQAYAVQM DFNLLVDAVN QNAAFLEQTL SSTIEQDDFT ARLFDIHKQV LKEGIAQTVF
LGLNRSDYMF QRSTDGSPAL KQIEINTISA SFGGLASRTP AVHRHVLSVL SKTKEAGKIL
SNNPSKGLAL GIAKAWELYG STNALVLLIA QEKERNIFDQ RAIENELLAR NIHVIRRTFE
DISEKGSLDQ DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSC AAKCPDIATQ
LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDMGEEGDQA IAKALAAPSR
FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK TEPEPFENCL LRPGSPAQVV
QCISELGIFG VYVRHEKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV
