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Protein

Glutathione synthetase

Gene

Gss

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

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 regulatory subunit (Gclm), Glutamate--cysteine ligase catalytic subunit (Gclc)
  2. Glutathione synthetase (Gss)
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 sitei125SubstrateBy similarity1
Metal bindingi144MagnesiumBy similarity1
Binding sitei144ATPBy similarity1
Metal bindingi146MagnesiumBy similarity1
Binding sitei220SubstrateBy similarity1
Binding sitei305ATPBy similarity1
Metal bindingi368MagnesiumBy similarity1
Binding sitei375ATPBy similarity1
Binding sitei425ATPBy similarity1
Binding sitei450SubstrateBy similarity1
Binding sitei452ATPBy similarity1
Binding sitei458ATP; via carbonyl oxygenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi364 – 373ATPBy similarity10
Nucleotide bindingi398 – 401ATPBy similarity4

GO - Molecular functioni

  • ATP binding Source: RGD
  • glutathione binding Source: RGD
  • glutathione synthase activity Source: RGD
  • glycine binding Source: RGD
  • magnesium ion binding Source: UniProtKB
  • peptide binding Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • cellular amino acid metabolic process Source: GO_Central
  • glutathione biosynthetic process Source: RGD
  • response to amino acid Source: RGD
  • response to cadmium ion Source: Ensembl
  • response to nutrient levels Source: RGD
  • response to tumor necrosis factor Source: RGD
  • response to xenobiotic stimulus Source: RGD

Keywordsi

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

Enzyme and pathway databases

BRENDAi6.3.2.3 5301
ReactomeiR-RNO-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:Gss
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi

Organism-specific databases

RGDi2752 Gss

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome 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
Initiator methionineiRemovedBy similarity
ChainiPRO_00002112632 – 474Glutathione synthetaseAdd BLAST473

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei415PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP46413
PRIDEiP46413

PTM databases

iPTMnetiP46413
PhosphoSitePlusiP46413

Expressioni

Gene expression databases

BgeeiENSRNOG00000018964
GenevisibleiP46413 RN

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025657

Structurei

3D structure databases

ProteinModelPortaliP46413
SMRiP46413
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni148 – 151Substrate bindingBy similarity4
Regioni214 – 216Substrate bindingBy similarity3
Regioni267 – 270Substrate bindingBy similarity4
Regioni461 – 462Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the eukaryotic GSH synthase family.Curated

Phylogenomic databases

eggNOGiKOG0021 Eukaryota
ENOG410XPHH LUCA
GeneTreeiENSGT00390000013764
HOGENOMiHOG000172641
HOVERGENiHBG002458
InParanoidiP46413
KOiK21456
OMAiFRSDYMV
OrthoDBiEOG091G05V8
PhylomeDBiP46413
TreeFamiTF105187

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46413-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSWGSILQ DEKQLEELAQ QAIDRALAEG VLLRSAKNPS SSDVVTYAPF
60 70 80 90 100
TLFPSPVPST LLEQAYAVQM DFNILVDAVS QNSAFLEQTL SSTIKKDEYT
110 120 130 140 150
ARLFDIYKQV LKEGIAQTVF LGLNRSDYMF QCSADGSKAL KQIEINTISA
160 170 180 190 200
SFGGLASRTP AVHRHVLNVL NKTNEASKIL SNNPSKGLAL GIAKAWELYG
210 220 230 240 250
SANAVVLLIA QEKERNIFDQ RAIENELLDR KIHVIRRRFE DVSERGSLDQ
260 270 280 290 300
NRRLFMEDQE VAVVYFRDGY MPSQYNAQNW EARLLLERSC AAKCPDIATQ
310 320 330 340 350
LAGTKKVQQE LSRVGLLEAL LPGQPEAVAR LRATFAGLYS LDMGEEGDQA
360 370 380 390 400
VAEALAAPSH FVLKPQREGG GNNFYGEEMV HALEQLKDSE ERASYILMEK
410 420 430 440 450
IEPEPFRNCL LRPGSPAQVV QCISELGIFG VYVRQGTTLV MNKHVGHLLR
460 470
TKAIEHADGG VAAGVAVLDN PYPV
Length:474
Mass (Da):52,345
Last modified:November 1, 1995 - v1
Checksum:i962B742FD19851A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38615 mRNA Translation: AAA64618.1
BC078700 mRNA Translation: AAH78700.1
PIRiI59346
RefSeqiNP_037094.1, NM_012962.1
UniGeneiRn.1692

Genome annotation databases

EnsembliENSRNOT00000025657; ENSRNOP00000025657; ENSRNOG00000018964
GeneIDi25458
KEGGirno:25458
UCSCiRGD:2752 rat

Similar proteinsi

Entry informationi

Entry nameiGSHB_RAT
AccessioniPrimary (citable) accession number: P46413
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 134 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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