Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione synthetase

Gene

gshB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg2+ or Mn2+ ion per subunit.By similarity

Enzyme regulationi

Inhibited by 7,8-dihydrofolate, methotrexate and trimethoprim.

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 (gshA)
  2. Glutathione synthetase (gshB)
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
Metal bindingi281Magnesium or manganeseBy similarity1
Metal bindingi283Magnesium or manganeseBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi151 – 207ATPBy similarityAdd BLAST57

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • glutathione synthase activity Source: EcoCyc
  • magnesium ion binding Source: EcoCyc
  • manganese ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • glutathione biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:GLUTATHIONE-SYN-MONOMER.
ECOL316407:JW2914-MONOMER.
MetaCyc:GLUTATHIONE-SYN-MONOMER.
BRENDAi6.3.2.3. 2026.
UniPathwayiUPA00142; UER00210.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione synthetase (EC:6.3.2.3)
Alternative name(s):
GSH synthetase
Short name:
GSH-S
Short name:
GSHase
Glutathione synthase
Gene namesi
Name:gshB
Synonyms:gsh-II
Ordered Locus Names:b2947, JW2914
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10419. gshB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi122C → A: No loss of activity. 1 Publication1
Mutagenesisi195C → A: No loss of activity. 1 Publication1
Mutagenesisi222C → A: No loss of activity. 1 Publication1
Mutagenesisi227P → V: Loss of activity. 1 Publication1
Mutagenesisi233R → A or K: Loss of activity. 1 Publication1
Mutagenesisi240G → V: Loss of activity. 1 Publication1
Mutagenesisi241R → A or K: No loss of activity. 1 Publication1
Mutagenesisi289C → A: No loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001974651 – 316Glutathione synthetaseAdd BLAST316

Proteomic databases

EPDiP04425.
PaxDbiP04425.
PRIDEiP04425.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi4259406. 5 interactors.
DIPiDIP-9840N.
IntActiP04425. 5 interactors.
STRINGi511145.b2947.

Structurei

Secondary structure

1316
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Helixi11 – 13Combined sources3
Turni16 – 18Combined sources3
Helixi20 – 30Combined sources11
Beta strandi34 – 38Combined sources5
Helixi40 – 42Combined sources3
Beta strandi43 – 46Combined sources4
Beta strandi49 – 59Combined sources11
Beta strandi67 – 76Combined sources10
Helixi77 – 79Combined sources3
Beta strandi80 – 85Combined sources6
Helixi93 – 107Combined sources15
Beta strandi111 – 114Combined sources4
Helixi116 – 121Combined sources6
Helixi126 – 131Combined sources6
Turni132 – 134Combined sources3
Beta strandi138 – 142Combined sources5
Helixi144 – 154Combined sources11
Beta strandi155 – 160Combined sources6
Turni166 – 169Combined sources4
Beta strandi171 – 173Combined sources3
Helixi180 – 187Combined sources8
Turni188 – 192Combined sources5
Beta strandi195 – 199Combined sources5
Helixi202 – 206Combined sources5
Beta strandi208 – 214Combined sources7
Beta strandi220 – 226Combined sources7
Helixi236 – 238Combined sources3
Beta strandi241 – 246Combined sources6
Helixi249 – 264Combined sources16
Beta strandi269 – 275Combined sources7
Beta strandi278 – 283Combined sources6
Helixi290 – 296Combined sources7
Helixi301 – 312Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GLVX-ray2.70A1-316[»]
1GSAX-ray2.00A1-316[»]
1GSHX-ray2.00A1-316[»]
2GLTX-ray2.20A1-316[»]
ProteinModelPortaliP04425.
SMRiP04425.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04425.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini125 – 310ATP-graspAdd BLAST186

Sequence similaritiesi

Belongs to the prokaryotic GSH synthase family.Curated
Contains 1 ATP-grasp domain.Curated

Phylogenomic databases

eggNOGiENOG4105D7Z. Bacteria.
COG0189. LUCA.
HOGENOMiHOG000265022.
InParanoidiP04425.
KOiK01920.
OMAiGMGIFRV.
PhylomeDBiP04425.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPiMF_00162. GSH_S. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006284. Glut_synth_pro.
IPR004218. GSHS_ATP-bd.
IPR004215. GSHS_N.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02955. GSH-S_ATP. 1 hit.
PF02951. GSH-S_N. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01380. glut_syn. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04425-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKLGIVMDP IANINIKKDS SFAMLLEAQR RGYELHYMEM GDLYLINGEA
60 70 80 90 100
RAHTRTLNVK QNYEEWFSFV GEQDLPLADL DVILMRKDPP FDTEFIYATY
110 120 130 140 150
ILERAEEKGT LIVNKPQSLR DCNEKLFTAW FSDLTPETLV TRNKAQLKAF
160 170 180 190 200
WEKHSDIILK PLDGMGGASI FRVKEGDPNL GVIAETLTEH GTRYCMAQNY
210 220 230 240 250
LPAIKDGDKR VLVVDGEPVP YCLARIPQGG ETRGNLAAGG RGEPRPLTES
260 270 280 290 300
DWKIARQIGP TLKEKGLIFV GLDIIGDRLT EINVTSPTCI REIEAEFPVS
310
ITGMLMDAIE ARLQQQ
Length:316
Mass (Da):35,561
Last modified:August 13, 1987 - v1
Checksum:iF2E67AB29DE113DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01666 Genomic DNA. Translation: CAA25826.1.
U28377 Genomic DNA. Translation: AAA69114.1.
U00096 Genomic DNA. Translation: AAC75984.1.
AP009048 Genomic DNA. Translation: BAE77010.1.
PIRiA01194. SYECGS.
RefSeqiNP_417422.1. NC_000913.3.
WP_000593273.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75984; AAC75984; b2947.
BAE77010; BAE77010; BAE77010.
GeneIDi947445.
KEGGiecj:JW2914.
eco:b2947.
PATRICi32121304. VBIEscCol129921_3040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01666 Genomic DNA. Translation: CAA25826.1.
U28377 Genomic DNA. Translation: AAA69114.1.
U00096 Genomic DNA. Translation: AAC75984.1.
AP009048 Genomic DNA. Translation: BAE77010.1.
PIRiA01194. SYECGS.
RefSeqiNP_417422.1. NC_000913.3.
WP_000593273.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GLVX-ray2.70A1-316[»]
1GSAX-ray2.00A1-316[»]
1GSHX-ray2.00A1-316[»]
2GLTX-ray2.20A1-316[»]
ProteinModelPortaliP04425.
SMRiP04425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259406. 5 interactors.
DIPiDIP-9840N.
IntActiP04425. 5 interactors.
STRINGi511145.b2947.

Proteomic databases

EPDiP04425.
PaxDbiP04425.
PRIDEiP04425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75984; AAC75984; b2947.
BAE77010; BAE77010; BAE77010.
GeneIDi947445.
KEGGiecj:JW2914.
eco:b2947.
PATRICi32121304. VBIEscCol129921_3040.

Organism-specific databases

EchoBASEiEB0414.
EcoGeneiEG10419. gshB.

Phylogenomic databases

eggNOGiENOG4105D7Z. Bacteria.
COG0189. LUCA.
HOGENOMiHOG000265022.
InParanoidiP04425.
KOiK01920.
OMAiGMGIFRV.
PhylomeDBiP04425.

Enzyme and pathway databases

UniPathwayiUPA00142; UER00210.
BioCyciEcoCyc:GLUTATHIONE-SYN-MONOMER.
ECOL316407:JW2914-MONOMER.
MetaCyc:GLUTATHIONE-SYN-MONOMER.
BRENDAi6.3.2.3. 2026.

Miscellaneous databases

EvolutionaryTraceiP04425.
PROiP04425.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPiMF_00162. GSH_S. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006284. Glut_synth_pro.
IPR004218. GSHS_ATP-bd.
IPR004215. GSHS_N.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02955. GSH-S_ATP. 1 hit.
PF02951. GSH-S_N. 1 hit.
[Graphical view]
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01380. glut_syn. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSHB_ECOLI
AccessioniPrimary (citable) accession number: P04425
Secondary accession number(s): Q2M9P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 2, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.