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Glutathione synthetase (GSH synthetase) (GSH-S) (EC 6.3.2.3) (Glutathione synthase)

 GSHB_HUMAN              Reviewed;         474 AA.
P48637; B2R697; B6F210; E1P5P9; Q4TTD9;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
26-FEB-2020, entry version 199.
RecName: Full=Glutathione synthetase;
Short=GSH synthetase;
Short=GSH-S;
EC=6.3.2.3;
AltName: Full=Glutathione synthase;
Name=GSS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=7646467; DOI=10.1042/bj3100353;
Gali R.R., Board P.G.;
"Sequencing and expression of a cDNA for human glutathione synthetase.";
Biochem. J. 310:353-358(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=19672693; DOI=10.1007/s11033-009-9675-3;
Uchida M., Sugaya M., Kanamaru T., Hisatomi H.;
"Alternative RNA splicing in expression of the glutathione synthetase gene
in human cells.";
Mol. Biol. Rep. 37:2105-2109(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
Shi Z.-Z., Galang R.L., Habib G.M., Lebovitz R.M., Lieberman M.W.;
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-437.
TISSUE=Substantia nigra;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-236 AND GLU-437.
NIEHS SNPs program;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 26-34; 113-125; 142-158; 222-230; 254-267; 274-283;
294-305; 419-434 AND 453-474, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-474 IN COMPLEX WITH ADP AND
GLUTATHIONE, COFACTOR, AND SUBUNIT.
PubMed=10369661; DOI=10.1093/emboj/18.12.3204;
Polekhina G., Board P.G., Gali R.R., Rossjohn J., Parker M.W.;
"Molecular basis of glutathione synthetase deficiency and a rare gene
permutation event.";
EMBO J. 18:3204-3213(1999).
[16]
VARIANTS GSS DEFICIENCY GLY-219; TRP-267 AND CYS-283.
PubMed=8896573; DOI=10.1038/ng1196-361;
Shi Z.-Z., Habib G.M., Rhead W.J., Gahl W.A., He X., Sazer S.,
Lieberman M.W.;
"Mutations in the glutathione synthetase gene cause 5-oxoprolinuria.";
Nat. Genet. 14:361-365(1996).
[17]
VARIANTS GSS DEFICIENCY.
PubMed=9215686; DOI=10.1093/hmg/6.7.1147;
Dahl N., Pigg M., Ristoff E., Gali R., Carlsson B., Mannervik B.,
Larsson A., Board P.;
"Missense mutations in the human glutathione synthetase gene result in
severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and
neurological dysfunction.";
Hum. Mol. Genet. 6:1147-1152(1997).
[18]
VARIANTS GSS DEFICIENCY GLY-219 AND PRO-301.
PubMed=27581854; DOI=10.1542/peds.2015-4324;
Signolet I., Chenouard R., Oca F., Barth M., Reynier P., Denis M.C.,
Simard G.;
"Recurrent isolated neonatal hemolytic anemia: think about glutathione
synthetase deficiency.";
Pediatrics 138:0-0(2016).
-!- CATALYTIC ACTIVITY:
Reaction=ATP + glycine + L-gamma-glutamyl-L-cysteine = ADP +
glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
ChEBI:CHEBI:456216; EC=6.3.2.3;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10369661};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:10369661};
-!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
L-cysteine and L-glutamate: step 2/2.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10369661}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-2969145, EBI-2969145;
P54274:TERF1; NbExp=2; IntAct=EBI-2969145, EBI-710997;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P48637-1; Sequence=Displayed;
Name=2;
IsoId=P48637-2; Sequence=VSP_047617;
-!- DISEASE: Glutathione synthetase deficiency (GSS deficiency)
[MIM:266130]: Severe form characterized by an increased rate of
hemolysis and defective function of the central nervous system.
{ECO:0000269|PubMed:27581854, ECO:0000269|PubMed:8896573,
ECO:0000269|PubMed:9215686}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Glutathione synthetase deficiency of erythrocytes (GLUSYNDE)
[MIM:231900]: Mild form causing hemolytic anemia. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: [Isoform 2]: Detected in colon, kidney, lung, liver,
placenta, peripheral blood and uterus, but not in heart, skeletal
muscle and spleen. {ECO:0000305}.
-!- SIMILARITY: Belongs to the eukaryotic GSH synthase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/gss/";
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EMBL; L42531; AAA69492.1; -; mRNA.
EMBL; AB459500; BAG75452.1; -; mRNA.
EMBL; U34683; AAB62390.1; -; mRNA.
EMBL; AK312492; BAG35394.1; -; mRNA.
EMBL; DQ074975; AAY57328.1; -; Genomic_DNA.
EMBL; AL133324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW76239.1; -; Genomic_DNA.
EMBL; CH471077; EAW76240.1; -; Genomic_DNA.
EMBL; BC007927; AAH07927.1; -; mRNA.
CCDS; CCDS13245.1; -. [P48637-1]
PIR; S56748; S56748.
RefSeq; NP_000169.1; NM_000178.3. [P48637-1]
RefSeq; NP_001309423.1; NM_001322494.1. [P48637-1]
RefSeq; NP_001309424.1; NM_001322495.1. [P48637-1]
PDB; 2HGS; X-ray; 2.10 A; A=1-474.
PDBsum; 2HGS; -.
SMR; P48637; -.
BioGrid; 109192; 27.
IntAct; P48637; 4.
MINT; P48637; -.
STRING; 9606.ENSP00000216951; -.
DrugBank; DB06151; Acetylcysteine.
DrugBank; DB09130; Copper.
DrugBank; DB03408; gamma-Glutamylcysteine.
DrugBank; DB00143; Glutathione.
DrugBank; DB00145; Glycine.
DrugBank; DB00151; L-Cysteine.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
iPTMnet; P48637; -.
PhosphoSitePlus; P48637; -.
BioMuta; GSS; -.
DMDM; 1346191; -.
OGP; P48637; -.
REPRODUCTION-2DPAGE; IPI00010706; -.
CPTAC; CPTAC-210; -.
CPTAC; CPTAC-211; -.
EPD; P48637; -.
jPOST; P48637; -.
MassIVE; P48637; -.
PaxDb; P48637; -.
PeptideAtlas; P48637; -.
PRIDE; P48637; -.
ProteomicsDB; 55917; -. [P48637-1]
ProteomicsDB; 6247; -.
DNASU; 2937; -.
Ensembl; ENST00000451957; ENSP00000407517; ENSG00000100983. [P48637-2]
Ensembl; ENST00000643188; ENSP00000493903; ENSG00000100983. [P48637-1]
Ensembl; ENST00000644793; ENSP00000495750; ENSG00000100983. [P48637-1]
Ensembl; ENST00000646735; ENSP00000493763; ENSG00000100983. [P48637-2]
Ensembl; ENST00000651619; ENSP00000498303; ENSG00000100983. [P48637-1]
GeneID; 2937; -.
KEGG; hsa:2937; -.
UCSC; uc010zuo.3; human. [P48637-1]
CTD; 2937; -.
DisGeNET; 2937; -.
GeneCards; GSS; -.
HGNC; HGNC:4624; GSS.
HPA; HPA054508; -.
HPA; HPA059315; -.
MalaCards; GSS; -.
MIM; 231900; phenotype.
MIM; 266130; phenotype.
MIM; 601002; gene.
neXtProt; NX_P48637; -.
OpenTargets; ENSG00000100983; -.
Orphanet; 289846; Glutathione synthetase deficiency with 5-oxoprolinuria.
Orphanet; 289849; Glutathione synthetase deficiency without 5-oxoprolinuria.
PharmGKB; PA29015; -.
eggNOG; KOG0021; Eukaryota.
eggNOG; ENOG410XPHH; LUCA.
GeneTree; ENSGT00390000013764; -.
HOGENOM; CLU_025152_2_1_1; -.
InParanoid; P48637; -.
KO; K21456; -.
OMA; ICELGIY; -.
OrthoDB; 1189955at2759; -.
PhylomeDB; P48637; -.
TreeFam; TF105187; -.
BioCyc; MetaCyc:HS02174-MONOMER; -.
BRENDA; 6.3.2.3; 2681.
Reactome; R-HSA-174403; Glutathione synthesis and recycling.
Reactome; R-HSA-5579006; Defective GSS causes Glutathione synthetase deficiency (GSS deficiency).
SABIO-RK; P48637; -.
UniPathway; UPA00142; UER00210.
ChiTaRS; GSS; human.
EvolutionaryTrace; P48637; -.
GenomeRNAi; 2937; -.
Pharos; P48637; Tbio.
PRO; PR:P48637; -.
Proteomes; UP000005640; Chromosome 20.
RNAct; P48637; protein.
Bgee; ENSG00000100983; Expressed in cerebral cortex and 233 other tissues.
ExpressionAtlas; P48637; baseline and differential.
Genevisible; P48637; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0043295; F:glutathione binding; IDA:UniProtKB.
GO; GO:0004363; F:glutathione synthase activity; IBA:GO_Central.
GO; GO:0016594; F:glycine binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
GO; GO:0006750; P:glutathione biosynthetic process; TAS:Reactome.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
CDD; cd00228; eu-GS; 1.
Gene3D; 1.10.1080.10; -; 1.
Gene3D; 3.30.1490.50; -; 1.
Gene3D; 3.30.1490.80; -; 1.
Gene3D; 3.40.50.1760; -; 1.
InterPro; IPR005615; Glutathione_synthase.
InterPro; IPR014042; Glutathione_synthase_a-hlx.
InterPro; IPR014709; Glutathione_synthase_C_euk.
InterPro; IPR014049; Glutathione_synthase_N_euk.
InterPro; IPR037013; GSH-S_sub-bd_sf.
InterPro; IPR004887; GSH_synth_subst-bd.
InterPro; IPR016185; PreATP-grasp_dom_sf.
PANTHER; PTHR11130; PTHR11130; 1.
Pfam; PF03917; GSH_synth_ATP; 1.
Pfam; PF03199; GSH_synthase; 1.
PIRSF; PIRSF001558; GSHase; 1.
SUPFAM; SSF52440; SSF52440; 1.
TIGRFAMs; TIGR01986; glut_syn_euk; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Direct protein sequencing; Disease mutation; Glutathione biosynthesis;
Hereditary hemolytic anemia; Ligase; Magnesium; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895"
CHAIN 2..474
/note="Glutathione synthetase"
/id="PRO_0000211260"
NP_BIND 364..373
/note="ATP"
NP_BIND 398..401
/note="ATP"
REGION 148..151
/note="Substrate binding"
REGION 214..216
/note="Substrate binding"
REGION 267..270
/note="Substrate binding"
REGION 461..462
/note="Substrate binding"
METAL 144
/note="Magnesium"
METAL 146
/note="Magnesium"
METAL 368
/note="Magnesium"
BINDING 125
/note="Substrate"
BINDING 144
/note="ATP"
BINDING 220
/note="Substrate"
BINDING 305
/note="ATP"
BINDING 375
/note="ATP"
BINDING 425
/note="ATP"
BINDING 450
/note="Substrate"
BINDING 452
/note="ATP"
BINDING 458
/note="ATP; via carbonyl oxygen"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895"
MOD_RES 415
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
VAR_SEQ 93..203
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:19672693"
/id="VSP_047617"
VARIANT 26
/note="A -> D (in GSS deficiency; dbSNP:rs759253242)"
/id="VAR_003602"
VARIANT 188
/note="L -> P (in GSS deficiency; 100-fold reduction of
activity)"
/id="VAR_003603"
VARIANT 219
/note="D -> A (in GSS deficiency; dbSNP:rs28938472)"
/id="VAR_003604"
VARIANT 219
/note="D -> G (in GSS deficiency; dbSNP:rs28938472)"
/evidence="ECO:0000269|PubMed:27581854,
ECO:0000269|PubMed:8896573"
/id="VAR_003605"
VARIANT 236
/note="R -> Q (in dbSNP:rs34239729)"
/evidence="ECO:0000269|Ref.5"
/id="VAR_025047"
VARIANT 254
/note="L -> R (in GSS deficiency)"
/id="VAR_003606"
VARIANT 267
/note="R -> W (in GSS deficiency; dbSNP:rs121909308)"
/evidence="ECO:0000269|PubMed:8896573"
/id="VAR_003607"
VARIANT 270
/note="Y -> C (in GSS deficiency; 100-fold reduction of
activity; dbSNP:rs1325986563)"
/id="VAR_003608"
VARIANT 270
/note="Y -> H (in GSS deficiency; 100-fold reduction of
activity)"
/id="VAR_003609"
VARIANT 283
/note="R -> C (in GSS deficiency; 10-fold reduction of
activity; dbSNP:rs121909309)"
/evidence="ECO:0000269|PubMed:8896573"
/id="VAR_003610"
VARIANT 286
/note="L -> Q (in GSS deficiency; dbSNP:rs1296000099)"
/id="VAR_003611"
VARIANT 301
/note="L -> P (in GSS deficiency)"
/evidence="ECO:0000269|PubMed:27581854"
/id="VAR_078567"
VARIANT 330
/note="R -> C (in GSS deficiency; dbSNP:rs148640446)"
/id="VAR_003612"
VARIANT 437
/note="K -> E (in dbSNP:rs34852238)"
/evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
/id="VAR_025048"
VARIANT 464
/note="G -> V (in GSS deficiency)"
/id="VAR_003613"
VARIANT 469
/note="D -> E (in GSS deficiency; dbSNP:rs1419704426)"
/id="VAR_003614"
HELIX 6..9
/evidence="ECO:0000244|PDB:2HGS"
HELIX 12..28
/evidence="ECO:0000244|PDB:2HGS"
STRAND 32..34
/evidence="ECO:0000244|PDB:2HGS"
STRAND 43..47
/evidence="ECO:0000244|PDB:2HGS"
STRAND 50..53
/evidence="ECO:0000244|PDB:2HGS"
STRAND 56..58
/evidence="ECO:0000244|PDB:2HGS"
HELIX 59..67
/evidence="ECO:0000244|PDB:2HGS"
HELIX 69..81
/evidence="ECO:0000244|PDB:2HGS"
HELIX 83..91
/evidence="ECO:0000244|PDB:2HGS"
HELIX 93..96
/evidence="ECO:0000244|PDB:2HGS"
HELIX 98..113
/evidence="ECO:0000244|PDB:2HGS"
STRAND 119..132
/evidence="ECO:0000244|PDB:2HGS"
STRAND 134..136
/evidence="ECO:0000244|PDB:2HGS"
STRAND 138..146
/evidence="ECO:0000244|PDB:2HGS"
HELIX 153..158
/evidence="ECO:0000244|PDB:2HGS"
HELIX 160..169
/evidence="ECO:0000244|PDB:2HGS"
HELIX 173..176
/evidence="ECO:0000244|PDB:2HGS"
HELIX 184..199
/evidence="ECO:0000244|PDB:2HGS"
STRAND 205..209
/evidence="ECO:0000244|PDB:2HGS"
HELIX 217..228
/evidence="ECO:0000244|PDB:2HGS"
TURN 229..231
/evidence="ECO:0000244|PDB:2HGS"
STRAND 234..237
/evidence="ECO:0000244|PDB:2HGS"
HELIX 239..245
/evidence="ECO:0000244|PDB:2HGS"
STRAND 246..248
/evidence="ECO:0000244|PDB:2HGS"
STRAND 254..256
/evidence="ECO:0000244|PDB:2HGS"
STRAND 259..268
/evidence="ECO:0000244|PDB:2HGS"
HELIX 272..274
/evidence="ECO:0000244|PDB:2HGS"
HELIX 277..288
/evidence="ECO:0000244|PDB:2HGS"
STRAND 289..295
/evidence="ECO:0000244|PDB:2HGS"
HELIX 297..301
/evidence="ECO:0000244|PDB:2HGS"
HELIX 305..310
/evidence="ECO:0000244|PDB:2HGS"
HELIX 316..320
/evidence="ECO:0000244|PDB:2HGS"
HELIX 325..333
/evidence="ECO:0000244|PDB:2HGS"
STRAND 338..340
/evidence="ECO:0000244|PDB:2HGS"
STRAND 342..344
/evidence="ECO:0000244|PDB:2HGS"
HELIX 345..356
/evidence="ECO:0000244|PDB:2HGS"
HELIX 358..360
/evidence="ECO:0000244|PDB:2HGS"
STRAND 361..366
/evidence="ECO:0000244|PDB:2HGS"
STRAND 369..371
/evidence="ECO:0000244|PDB:2HGS"
HELIX 376..386
/evidence="ECO:0000244|PDB:2HGS"
HELIX 390..394
/evidence="ECO:0000244|PDB:2HGS"
STRAND 395..399
/evidence="ECO:0000244|PDB:2HGS"
STRAND 406..411
/evidence="ECO:0000244|PDB:2HGS"
STRAND 418..435
/evidence="ECO:0000244|PDB:2HGS"
STRAND 438..453
/evidence="ECO:0000244|PDB:2HGS"
TURN 461..464
/evidence="ECO:0000244|PDB:2HGS"
STRAND 467..469
/evidence="ECO:0000244|PDB:2HGS"
STRAND 472..474
/evidence="ECO:0000244|PDB:2HGS"
SEQUENCE 474 AA; 52385 MW; 3C25EF7072EFE058 CRC64;
MATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF TLFPSLVPSA
LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT ARLFDIHKQV LKEGIAQTVF
LGLNRSDYMF QRSADGSPAL KQIEINTISA SFGGLASRTP AVHRHVLSVL SKTKEAGKIL
SNNPSKGLAL GIAKAWELYG SPNALVLLIA QEKERNIFDQ RAIENELLAR NIHVIRRTFE
DISEKGSLDQ DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ
LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA IAEALAAPSR
FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK IEPEPFENCL LRPGSPARVV
QCISELGIFG VYVRQEKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV


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Pathways :
WP1708: Terpenoid backbone biosynthesis
WP2248: anthocyanin biosynthesis
WP2199: Seed Development
WP2211: Geranylgeranyldiphosphate biosynthesis II (plastidic)
WP100: Glutathione metabolism
WP702: metapathway biotransformation
WP1124: metapathway biotransformation
WP1286: metapathway biotransformation
WP521: amino acid conjugation of benzoic acid
WP1577: amino acid conjugation of benzoic acid
WP1656: Glutathione metabolism
WP1039: Glutathione metabolism
WP889: metapathway biotransformation
WP1251: metapathway biotransformation
WP469: Glutathione metabolism
WP164: Glutathione metabolism
WP196: Glutathione Biosynthesis
WP1006: metapathway biotransformation
WP730: Glutathione and one carbon metabolism
WP1212: metapathway biotransformation
WP392: Glutathione-Glutaredoxin Redox Reaction
WP2208: Cardiolipin Biosynthesis
WP296: TCA Cycle - biocyc
WP1423: Ganglio Sphingolipid Metabolism
WP677: Momilactone biosynthesis

Related Genes :
[gshB gsh-II b2947 JW2914] Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GSH-S) (GSHase) (Glutathione synthase)
[gshAB gshF SAG1821] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF lmo2770] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF lin2913] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF gbs1862] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gss gsp b2988 JW2956] Bifunctional glutathionylspermidine synthetase/amidase (GspSA) [Includes: Glutathionylspermidine amidase (Gsp amidase) (EC 3.5.1.78) (Glutathionylspermidine amidohydrolase [spermidine-forming]); Glutathionylspermidine synthetase (Gsp synthetase) (EC 6.3.1.8) (Glutathione:spermidine ligase [ADP-forming]) (Gsp synthase)]
[gshAB gshF lwe2717] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[GSH1 CAD2 GCL PAD2 RML1 At4g23100 F7H19.290] Glutamate--cysteine ligase, chloroplastic (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase) (Protein ROOT MERISTEMLESS 1) (AtGCL) (Protein cadmium-sensitive 2) (Protein phytoalexin-deficient 2)
[gshAB gshF MS1683] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF LMOf2365_2760] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF stu1413] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF PM1048] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF SMU_267c] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF EF_3089] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF CPE1573] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF DP1233] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[gshAB gshF str1413] Glutathione biosynthesis bifunctional protein GshAB (Gamma-GCS-GS) (GCS-GS) [Includes: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase); Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GS) (GSH-S) (GSHase) (Glutathione synthase)]
[DUG1 YFR044C] Cys-Gly metallodipeptidase DUG1 (EC 3.4.13.-) (Deficient in utilization of glutathione protein 1) (GSH degradosomal complex subunit DUG1)
[frmA adhC b0356 JW0347] S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) (Alcohol dehydrogenase class-3) (EC 1.1.1.1) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-)
[SFA1 SFA YDL168W] S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) (Alcohol dehydrogenase SFA) (EC 1.1.1.1) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (FLD) (GSH-FDH) (EC 1.1.1.-)
[Adh5 Adh-2 Adh2] Alcohol dehydrogenase class-3 (EC 1.1.1.1) (Alcohol dehydrogenase 2) (Alcohol dehydrogenase 5) (Alcohol dehydrogenase B2) (ADH-B2) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) (S-(hydroxymethyl)glutathione dehydrogenase) (EC 1.1.1.284)
[HPGDS GSTS PGDS PTGDS2] Hematopoietic prostaglandin D synthase (H-PGDS) (EC 5.3.99.2) (GST class-sigma) (Glutathione S-transferase) (EC 2.5.1.18) (Glutathione-dependent PGD synthase) (Glutathione-requiring prostaglandin D synthase) (Prostaglandin-H2 D-isomerase)
[GSH1 ECS1] Glutamate--cysteine ligase, chloroplastic (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase)
[Adh5 Adh-2 Adh2] Alcohol dehydrogenase class-3 (EC 1.1.1.1) (Alcohol dehydrogenase 2) (Alcohol dehydrogenase 5) (Alcohol dehydrogenase B2) (ADH-B2) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) (S-(hydroxymethyl)glutathione dehydrogenase) (EC 1.1.1.284)
[ADH2 ADHIII FDH1 At5g43940 MRH10.4] Alcohol dehydrogenase class-3 (EC 1.1.1.1) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) (S-(hydroxymethyl)glutathione dehydrogenase) (EC 1.1.1.284)
[ADH5 ADHX FDH] Alcohol dehydrogenase class-3 (EC 1.1.1.1) (Alcohol dehydrogenase 5) (Alcohol dehydrogenase class chi chain) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) (S-(hydroxymethyl)glutathione dehydrogenase) (EC 1.1.1.284)
[ADH5] Alcohol dehydrogenase class-3 (EC 1.1.1.1) (Alcohol dehydrogenase 5) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) (S-(hydroxymethyl)glutathione dehydrogenase) (EC 1.1.1.284)
[Hpgds Gsts Pgds Ptgds2] Hematopoietic prostaglandin D synthase (H-PGDS) (EC 5.3.99.2) (GST class-sigma) (Glutathione S-transferase) (EC 2.5.1.18) (Glutathione-dependent PGD synthase) (Glutathione-requiring prostaglandin D synthase) (Prostaglandin-H2 D-isomerase)
[Fdh gfd ODH CG6598] Alcohol dehydrogenase class-3 (EC 1.1.1.1) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) (Octanol dehydrogenase) (EC 1.1.1.73) (S-(hydroxymethyl)glutathione dehydrogenase) (EC 1.1.1.284)
[DHAR1 DHAR5 At1g19570 F14P1.9 F18O14.22] Glutathione S-transferase DHAR1, mitochondrial (EC 2.5.1.18) (Chloride intracellular channel homolog 1) (CLIC homolog 1) (Glutathione-dependent dehydroascorbate reductase 1) (AtDHAR1) (GSH-dependent dehydroascorbate reductase 1) (mtDHAR) (EC 1.8.5.1)

Bibliography :
No related Items