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P04425

- GSHB_ECOLI

UniProt

P04425 - GSHB_ECOLI

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Protein

Glutathione synthetase

Gene

gshB

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Binds 1 magnesium or manganese ion per subunit.By similarity

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi281 – 2811Magnesium or manganeseBy similarity
Metal bindingi283 – 2831Magnesium or manganeseBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi151 – 20757ATPBy similarityAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutathione synthase activity Source: EcoCyc
  3. magnesium ion binding Source: EcoCyc
  4. manganese ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10419. gshB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi122 – 1221C → A: No loss of activity. 1 Publication
Mutagenesisi195 – 1951C → A: No loss of activity. 1 Publication
Mutagenesisi222 – 2221C → A: No loss of activity. 1 Publication
Mutagenesisi227 – 2271P → V: Loss of activity. 1 Publication
Mutagenesisi233 – 2331R → A or K: Loss of activity. 1 Publication
Mutagenesisi240 – 2401G → V: Loss of activity. 1 Publication
Mutagenesisi241 – 2411R → A or K: No loss of activity. 1 Publication
Mutagenesisi289 – 2891C → A: No loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Glutathione synthetasePRO_0000197465Add
BLAST

Proteomic databases

PaxDbiP04425.
PRIDEiP04425.

Expressioni

Gene expression databases

GenevestigatoriP04425.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
mapP0AE181EBI-909107,EBI-553355
nadEP188431EBI-909107,EBI-548960

Protein-protein interaction databases

DIPiDIP-9840N.
IntActiP04425. 5 interactions.
STRINGi511145.b2947.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75
Helixi11 – 133
Turni16 – 183
Helixi20 – 3011
Beta strandi34 – 385
Helixi40 – 423
Beta strandi43 – 464
Beta strandi49 – 5911
Beta strandi67 – 7610
Helixi77 – 793
Beta strandi80 – 856
Helixi93 – 10715
Beta strandi111 – 1144
Helixi116 – 1216
Helixi126 – 1316
Turni132 – 1343
Beta strandi138 – 1425
Helixi144 – 15411
Beta strandi155 – 1606
Turni166 – 1694
Beta strandi171 – 1733
Helixi180 – 1878
Turni188 – 1925
Beta strandi195 – 1995
Helixi202 – 2065
Beta strandi208 – 2147
Beta strandi220 – 2267
Helixi236 – 2383
Beta strandi241 – 2466
Helixi249 – 26416
Beta strandi269 – 2757
Beta strandi278 – 2836
Helixi290 – 2967
Helixi301 – 31212

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GLVX-ray2.70A1-316[»]
1GSAX-ray2.00A1-316[»]
1GSHX-ray2.00A1-316[»]
2GLTX-ray2.20A1-316[»]
ProteinModelPortaliP04425.
SMRiP04425. Positions 1-314.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04425.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 310186ATP-graspAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0189.
HOGENOMiHOG000265022.
InParanoidiP04425.
KOiK01920.
OMAiDWKIARA.
OrthoDBiEOG6WMHWB.
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.
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:
EMBL
GenBank
DDBJ
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.
YP_491146.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75984; AAC75984; b2947.
BAE77010; BAE77010; BAE77010.
GeneIDi12930412.
947445.
KEGGiecj:Y75_p2877.
eco:b2947.
PATRICi32121304. VBIEscCol129921_3040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A01194. SYECGS.
RefSeqi NP_417422.1. NC_000913.3.
YP_491146.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GLV X-ray 2.70 A 1-316 [» ]
1GSA X-ray 2.00 A 1-316 [» ]
1GSH X-ray 2.00 A 1-316 [» ]
2GLT X-ray 2.20 A 1-316 [» ]
ProteinModelPortali P04425.
SMRi P04425. Positions 1-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9840N.
IntActi P04425. 5 interactions.
STRINGi 511145.b2947.

Proteomic databases

PaxDbi P04425.
PRIDEi P04425.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75984 ; AAC75984 ; b2947 .
BAE77010 ; BAE77010 ; BAE77010 .
GeneIDi 12930412.
947445.
KEGGi ecj:Y75_p2877.
eco:b2947.
PATRICi 32121304. VBIEscCol129921_3040.

Organism-specific databases

EchoBASEi EB0414.
EcoGenei EG10419. gshB.

Phylogenomic databases

eggNOGi COG0189.
HOGENOMi HOG000265022.
InParanoidi P04425.
KOi K01920.
OMAi DWKIARA.
OrthoDBi EOG6WMHWB.
PhylomeDBi P04425.

Enzyme and pathway databases

UniPathwayi UPA00142 ; UER00210 .
BioCyci EcoCyc:GLUTATHIONE-SYN-MONOMER.
ECOL316407:JW2914-MONOMER.
MetaCyc:GLUTATHIONE-SYN-MONOMER.

Miscellaneous databases

EvolutionaryTracei P04425.
PROi P04425.

Gene expression databases

Genevestigatori P04425.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPi MF_00162. GSH_S.
InterProi IPR011761. 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 ]
Pfami PF02955. GSH-S_ATP. 1 hit.
PF02951. GSH-S_N. 1 hit.
[Graphical view ]
SUPFAMi SSF52440. SSF52440. 1 hit.
TIGRFAMsi TIGR01380. glut_syn. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

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: October 29, 2014
This is version 140 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

External Data

Dasty 3