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Protein

Glutathione synthetase

Gene

GSH2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Miscellaneous

Present with 3430 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Pathwayi: glutathione biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes glutathione from L-cysteine and L-glutamate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate--cysteine ligase (GSH1)
  2. Glutathione synthetase (GSH2)
This subpathway is part of the pathway glutathione biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutathione from L-cysteine and L-glutamate, the pathway glutathione biosynthesis and in Sulfur metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei128Substrate1 Publication1
Metal bindingi146Magnesium1
Binding sitei146ATP1
Metal bindingi148MagnesiumBy similarity1
Binding sitei234Substrate1 Publication1
Binding sitei324ATP1
Metal bindingi386Magnesium1
Binding sitei393ATP1
Binding sitei442ATP1
Binding sitei467SubstrateBy similarity1
Binding sitei469ATP1
Binding sitei475ATP; via carbonyl oxygenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi382 – 391ATP10
Nucleotide bindingi415 – 418ATP4

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • glutathione binding Source: UniProtKB
  • glutathione synthase activity Source: SGD
  • magnesium ion binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • cellular amino acid metabolic process Source: GO_Central
  • glutathione biosynthetic process Source: SGD

Keywordsi

Molecular functionLigase
Biological processGlutathione biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YOL049W-MONOMER
BRENDAi6.3.2.3 984
ReactomeiR-SCE-174403 Glutathione synthesis and recycling
UniPathwayiUPA00142; UER00210

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione synthetase (EC:6.3.2.3)
Short name:
GSH synthetase
Short name:
GSH-S
Alternative name(s):
Glutathione synthase
Gene namesi
Name:GSH2
Ordered Locus Names:YOL049W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL049W
SGDiS000005409 GSH2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002112661 – 491Glutathione synthetaseAdd BLAST491

Proteomic databases

MaxQBiQ08220
PaxDbiQ08220
PRIDEiQ08220

PTM databases

iPTMnetiQ08220

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi34354, 128 interactors
IntActiQ08220, 1 interactor
STRINGi4932.YOL049W

Structurei

Secondary structure

1491
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 25Combined sources18
Helixi34 – 36Combined sources3
Beta strandi40 – 43Combined sources4
Beta strandi46 – 49Combined sources4
Beta strandi51 – 54Combined sources4
Helixi55 – 79Combined sources25
Helixi85 – 96Combined sources12
Turni97 – 100Combined sources4
Helixi101 – 111Combined sources11
Beta strandi123 – 136Combined sources14
Beta strandi139 – 148Combined sources10
Helixi155 – 170Combined sources16
Helixi183 – 185Combined sources3
Helixi191 – 208Combined sources18
Beta strandi219 – 224Combined sources6
Helixi231 – 243Combined sources13
Beta strandi249 – 252Combined sources4
Helixi254 – 260Combined sources7
Beta strandi261 – 263Combined sources3
Turni265 – 267Combined sources3
Beta strandi270 – 272Combined sources3
Turni273 – 275Combined sources3
Beta strandi278 – 286Combined sources9
Helixi290 – 292Combined sources3
Helixi296 – 307Combined sources12
Beta strandi308 – 313Combined sources6
Helixi316 – 321Combined sources6
Helixi324 – 329Combined sources6
Helixi333 – 336Combined sources4
Turni337 – 339Combined sources3
Helixi343 – 350Combined sources8
Beta strandi356 – 358Combined sources3
Beta strandi360 – 362Combined sources3
Helixi363 – 374Combined sources12
Helixi376 – 378Combined sources3
Beta strandi379 – 385Combined sources7
Helixi394 – 396Combined sources3
Helixi397 – 402Combined sources6
Helixi406 – 411Combined sources6
Beta strandi412 – 416Combined sources5
Beta strandi428 – 430Combined sources3
Beta strandi433 – 435Combined sources3
Beta strandi439 – 451Combined sources13
Beta strandi456 – 469Combined sources14
Beta strandi472 – 474Combined sources3
Beta strandi477 – 480Combined sources4
Beta strandi483 – 485Combined sources3
Beta strandi488 – 491Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M0TX-ray2.30A/B1-491[»]
1M0WX-ray1.80A/B1-491[»]
ProteinModelPortaliQ08220
SMRiQ08220
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08220

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 153Substrate binding4
Regioni228 – 230Substrate binding3
Regioni285 – 288Substrate binding4
Regioni478 – 479Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the eukaryotic GSH synthase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000013764
HOGENOMiHOG000172641
InParanoidiQ08220
KOiK21456
OMAiFRSDYMV
OrthoDBiEOG092C36B7

Family and domain databases

CDDicd00228 eu-GS, 1 hit
Gene3Di1.10.1080.10, 2 hits
3.30.1490.50, 1 hit
3.30.1490.80, 3 hits
3.40.50.1760, 1 hit
InterProiView protein in InterPro
IPR005615 Glutathione_synthase
IPR014042 Glutathione_synthase_a-hlx
IPR014709 Glutathione_synthase_C_euk
IPR014049 Glutathione_synthase_N_euk
IPR037013 GSH-S_sub-bd_sf
IPR004887 GSH_synth_subst-bd
IPR016185 PreATP-grasp_dom_sf
PANTHERiPTHR11130 PTHR11130, 1 hit
PfamiView protein in Pfam
PF03917 GSH_synth_ATP, 1 hit
PF03199 GSH_synthase, 1 hit
PIRSFiPIRSF001558 GSHase, 1 hit
SUPFAMiSSF52440 SSF52440, 1 hit
TIGRFAMsiTIGR01986 glut_syn_euk, 1 hit

Sequencei

Sequence statusi: Complete.

Q08220-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHYPPSKDQ LNELIQEVNQ WAITNGLSMY PPKFEENPSN ASVSPVTIYP
60 70 80 90 100
TPIPRKCFDE AVQIQPVFNE LYARITQDMA QPDSYLHKTT EALALSDSEF
110 120 130 140 150
TGKLWSLYLA TLKSAQYKKQ NFRLGIFRSD YLIDKKKGTE QIKQVEFNTV
160 170 180 190 200
SVSFAGLSEK VDRLHSYLNR ANKYDPKGPI YNDQNMVISD SGYLLSKALA
210 220 230 240 250
KAVESYKSQQ SSSTTSDPIV AFIVQRNERN VFDQKVLELN LLEKFGTKSV
260 270 280 290 300
RLTFDDVNDK LFIDDKTGKL FIRDTEQEIA VVYYRTGYTT TDYTSEKDWE
310 320 330 340 350
ARLFLEKSFA IKAPDLLTQL SGSKKIQQLL TDEGVLGKYI SDAEKKSSLL
360 370 380 390 400
KTFVKIYPLD DTKLGREGKR LALSEPSKYV LKPQREGGGN NVYKENIPNF
410 420 430 440 450
LKGIEERHWD AYILMELIEP ELNENNIILR DNKSYNEPII SELGIYGCVL
460 470 480 490
FNDEQVLSNE FSGSLLRSKF NTSNEGGVAA GFGCLDSIIL Y
Length:491
Mass (Da):55,815
Last modified:November 1, 1996 - v1
Checksum:iD2AE50A487E0791C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13804 Genomic DNA Translation: CAA74136.1
Z74791 Genomic DNA Translation: CAA99054.1
AY723864 Genomic DNA Translation: AAU09781.1
BK006948 Genomic DNA Translation: DAA10734.1
PIRiS66734
RefSeqiNP_014593.1, NM_001183303.1

Genome annotation databases

EnsemblFungiiYOL049W; YOL049W; YOL049W
GeneIDi854108
KEGGisce:YOL049W

Similar proteinsi

Entry informationi

Entry nameiGSHB_YEAST
AccessioniPrimary (citable) accession number: Q08220
Secondary accession number(s): D6W218
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 165 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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