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P04425 (GSHB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione synthetase

EC=6.3.2.3
Alternative name(s):
GSH synthetase
Short name=GSH-S
Short name=GSHase
Glutathione synthase
Gene names
Name:gshB
Synonyms:gsh-II
Ordered Locus Names:b2947, JW2914
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione. HAMAP-Rule MF_00162

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Enzyme regulation

Inhibited by 7,8-dihydrofolate, methotrexate and trimethoprim. HAMAP-Rule MF_00162

Pathway

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2. HAMAP-Rule MF_00162

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the prokaryotic GSH synthase family.

Contains 1 ATP-grasp domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Glutathione synthetase HAMAP-Rule MF_00162
PRO_0000197465

Regions

Domain125 – 310186ATP-grasp
Nucleotide binding151 – 20757ATP By similarity

Sites

Metal binding2811Magnesium or manganese By similarity
Metal binding2831Magnesium or manganese By similarity

Experimental info

Mutagenesis1221C → A: No loss of activity. Ref.8
Mutagenesis1951C → A: No loss of activity. Ref.8
Mutagenesis2221C → A: No loss of activity. Ref.8
Mutagenesis2271P → V: Loss of activity. Ref.6 Ref.8
Mutagenesis2331R → A or K: Loss of activity. Ref.7 Ref.8
Mutagenesis2401G → V: Loss of activity. Ref.6 Ref.8
Mutagenesis2411R → A or K: No loss of activity. Ref.7 Ref.8
Mutagenesis2891C → A: No loss of activity. Ref.8

Secondary structure

............................................................... 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04425 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: F2E67AB29DE113DD

FASTA31635,561
        10         20         30         40         50         60 
MIKLGIVMDP IANINIKKDS SFAMLLEAQR RGYELHYMEM GDLYLINGEA RAHTRTLNVK 

        70         80         90        100        110        120 
QNYEEWFSFV GEQDLPLADL DVILMRKDPP FDTEFIYATY ILERAEEKGT LIVNKPQSLR 

       130        140        150        160        170        180 
DCNEKLFTAW FSDLTPETLV TRNKAQLKAF WEKHSDIILK PLDGMGGASI FRVKEGDPNL 

       190        200        210        220        230        240 
GVIAETLTEH GTRYCMAQNY LPAIKDGDKR VLVVDGEPVP YCLARIPQGG ETRGNLAAGG 

       250        260        270        280        290        300 
RGEPRPLTES DWKIARQIGP TLKEKGLIFV GLDIIGDRLT EINVTSPTCI REIEAEFPVS 

       310 
ITGMLMDAIE ARLQQQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II."
Gushima H., Yasuda S., Soeda E., Yokota M., Kondo M., Kimura A.
Nucleic Acids Res. 12:9299-9307(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0-A resolution."
Yamaguchi H., Kato H., Hata Y., Nishioka T., Kimura A., Oda J., Katsube Y.
J. Mol. Biol. 229:1083-1100(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: B.
[5]"Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins."
Matsuda K., Mizuguchi K., Nishioka T., Kato H., Go N., Oda J.
Protein Eng. 9:1083-1092(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: B.
[6]"Flexibility impaired by mutations revealed the multifunctional roles of the loop in glutathione synthetase."
Tanaka T., Yamaguchi H., Kato H., Nishioka T., Katsube Y., Oda J.
Biochemistry 32:12398-12404(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PRO-227 AND GLY-240.
[7]"Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reaction."
Tanaka T., Kato H., Nishioka T., Oda J.
Biochemistry 31:2259-2265(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 234-242, MUTAGENESIS OF ARG-233 AND ARG-241.
Strain: B.
[8]"Role of cysteine residues in glutathione synthetase from Escherichia coli B. Chemical modification and oligonucleotide site-directed mutagenesis."
Kato H., Tanaka T., Nishioka T., Kimura A., Oda J.
J. Biol. Chem. 263:11646-11651(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYSTEINE RESIDUES.
Strain: B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01666 Genomic DNA. Translation: CAA25826.1.
U28377 Genomic DNA. Translation: AAA69114.1.
U00096 Genomic DNA. Translation: AAC75984.1.
AP009048 Genomic DNA. Translation: BAE77010.1.
PIRSYECGS. A01194.
RefSeqNP_417422.1. NC_000913.3.
YP_491146.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GLVX-ray2.70A1-316[»]
1GSAX-ray2.00A1-316[»]
1GSHX-ray2.00A1-316[»]
2GLTX-ray2.20A1-316[»]
ProteinModelPortalP04425.
SMRP04425. Positions 1-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9840N.
IntActP04425. 5 interactions.
STRING511145.b2947.

Proteomic databases

PaxDbP04425.
PRIDEP04425.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75984; AAC75984; b2947.
BAE77010; BAE77010; BAE77010.
GeneID12930412.
947445.
KEGGecj:Y75_p2877.
eco:b2947.
PATRIC32121304. VBIEscCol129921_3040.

Organism-specific databases

EchoBASEEB0414.
EcoGeneEG10419. gshB.

Phylogenomic databases

eggNOGCOG0189.
HOGENOMHOG000265022.
KOK01920.
OMAPTCFQEI.
OrthoDBEOG6WMHWB.
PhylomeDBP04425.
ProtClustDBPRK05246.

Enzyme and pathway databases

BioCycEcoCyc:GLUTATHIONE-SYN-MONOMER.
ECOL316407:JW2914-MONOMER.
MetaCyc:GLUTATHIONE-SYN-MONOMER.
UniPathwayUPA00142; UER00210.

Gene expression databases

GenevestigatorP04425.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPMF_00162. GSH_S.
InterProIPR011761. 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]
PfamPF02955. GSH-S_ATP. 1 hit.
PF02951. GSH-S_N. 1 hit.
[Graphical view]
SUPFAMSSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01380. glut_syn. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04425.
PROP04425.

Entry information

Entry nameGSHB_ECOLI
AccessionPrimary (citable) accession number: P04425
Secondary accession number(s): Q2M9P6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene