Glutathione synthetase - Escherichia coli (strain K12)

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P04425 (GSHB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP glutathione synthase activity Inferred from direct assay PubMed 6389479. Source: EcoCyc magnesium ion binding Inferred from direct assay PubMed 6389479. Source: EcoCyc manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
map	P0AE18	1	EBI-909107,EBI-553355
nadE	P18843	1	EBI-909107,EBI-548960

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 316

316

Glutathione synthetase HAMAP-Rule MF_00162

PRO_0000197465

Regions

Domain

125 – 310

186

ATP-grasp

Nucleotide binding

151 – 207

ATP By similarity

Sites

Metal binding

281

Magnesium or manganese By similarity

Metal binding

283

Magnesium or manganese By similarity

Experimental info

Mutagenesis

122

C → A: No loss of activity. Ref.8

Mutagenesis

195

C → A: No loss of activity. Ref.8

Mutagenesis

222

C → A: No loss of activity. Ref.8

Mutagenesis

227

P → V: Loss of activity. Ref.6 Ref.8

Mutagenesis

233

R → A or K: Loss of activity. Ref.7 Ref.8

Mutagenesis

240

G → V: Loss of activity. Ref.6 Ref.8

Mutagenesis

241

R → A or K: No loss of activity. Ref.7 Ref.8

Mutagenesis

289

C → A: No loss of activity. Ref.8

Secondary structure

316

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P04425 [UniParc].

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

FASTA

316

35,561

        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' referencesShow '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 277:1453-1474(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.

PIR

SYECGS. A01194.

RefSeq

NP_417422.1. NC_000913.2.
YP_491146.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P04425.

SMR

P04425. Positions 1-314.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9840N.

IntAct

P04425. 4 interactions.

STRING

511145.b2947.

Proteomic databases

PaxDb

P04425.

PRIDE

P04425.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75984; AAC75984; b2947.
BAE77010; BAE77010; BAE77010.

GeneID

12930412.
947445.

KEGG

ecj:Y75_p2877.
eco:b2947.

PATRIC

32121304. VBIEscCol129921_3040.

Organism-specific databases

EchoBASE

EB0414.

EcoGene

EG10419. gshB.

Phylogenomic databases

eggNOG

COG0189.

HOGENOM

HOG000265022.

K01920.

OMA

WMRKDPP.

ProtClustDB

PRK05246.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUTATHIONE-SYN-MONOMER.
ECOL316407:JW2914-MONOMER.
MetaCyc:GLUTATHIONE-SYN-MONOMER.

UniPathway

UPA00142; UER00210.

Gene expression databases

Genevestigator

P04425.

Family and domain databases

Gene3D

3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.

HAMAP

MF_00162. GSH-S.

InterPro

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]

Pfam

PF02955. GSH-S_ATP. 1 hit.
PF02951. GSH-S_N. 1 hit.
[Graphical view]

SUPFAM

SSF52440. PreATP-grasp-like. 1 hit.

TIGRFAMs

TIGR01380. glut_syn. 1 hit.

PROSITE

PS50975. ATP_GRASP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P04425.

Entry information

Entry name

GSHB_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents