GSHB_BOVIN
ID GSHB_BOVIN Reviewed; 474 AA.
AC Q5EAC2; Q2TBS8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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}.
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; BT020647; AAX08664.1; -; mRNA.
DR EMBL; BC109713; AAI09714.1; -; mRNA.
DR RefSeq; NP_001015630.1; NM_001015630.1.
DR RefSeq; XP_005214785.1; XM_005214728.3.
DR AlphaFoldDB; Q5EAC2; -.
DR SMR; Q5EAC2; -.
DR STRING; 9913.ENSBTAP00000004559; -.
DR PaxDb; Q5EAC2; -.
DR PeptideAtlas; Q5EAC2; -.
DR PRIDE; Q5EAC2; -.
DR GeneID; 525059; -.
DR KEGG; bta:525059; -.
DR CTD; 2937; -.
DR eggNOG; KOG0021; Eukaryota.
DR HOGENOM; CLU_025152_2_1_1; -.
DR InParanoid; Q5EAC2; -.
DR OrthoDB; 1189955at2759; -.
DR TreeFam; TF105187; -.
DR UniPathway; UPA00142; UER00210.
DR Proteomes; UP000009136; 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_0000247549"
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"
FT CONFLICT 238
FT /note="K -> R (in Ref. 2; AAI09714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 52066 MW; 964C08AF6A93FFF8 CRC64;
MATGWGSLLQ DEQQLEELAR QAVDRALAEG VLLRTSQAPS SSHVVSYAPF TLFPSPVPSA
LLEQAYAVQA DFNLLVDAVS QNAVFLEQTL SSTIKRDSFT ARLFDIHKQV LKEGIAQTVF
LGLNRSDYMF QCNPDGSAAL KQIEINTVSA SFGGLASRTP AVHRHVLSVL GKTKEAAKIL
SNNPSKGLAM GIAKAWELYG SANAQVLLIA QEKERNIFDQ RAIENELLAR NIHVIRRKFE
DVSEKGSLDQ DRRLFMDGQE IAVVYFRDGY MPGHYSLQNW EARLLLERSC AVKCPDIATQ
LAGTKKVQQE LSRVGVLESF LPGQPEAVAR LRATFAGLYS LDLGEEGDQA ITKAIAAPSC
FVLKPQREGG GNNLYGEEMV QALERLKDSE ERASYILMEK IEPEPFRNCL LRPGSPARVI
QCISELGIFG VYVREGKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV
