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P58581 (GSHB_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Ordered Locus Names:STY3248, t3007
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Pathway

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

Sequence similarities

Belongs to the prokaryotic GSH synthase family.

Contains 1 ATP-grasp domain.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Cellular_componentcytosol

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutathione synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 315315Glutathione synthetase HAMAP-Rule MF_00162
PRO_0000197483

Regions

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

Sites

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

Secondary structure

............................................................. 315
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P58581 [UniParc].

Last modified January 23, 2002. Version 1.
Checksum: D9AC53F9B23070C3

FASTA31535,380
        10         20         30         40         50         60 
MIKLGIVMDP IAHINIKKDT SFAMLLEAQR RGYELHYMEM ADLYLINGEA RACTRTLSVE 

        70         80         90        100        110        120 
QNYDKWYEFG SEQEIKLADL DVILMRKDPP FDTEFIYATY ILERAEEEGT LIVNKPQSLR 

       130        140        150        160        170        180 
DCNEKLYTAW FADLTPETLV TRNKAQLKAF WEKHGDIIMK PLDGMGGASI FRVKEGDPNI 

       190        200        210        220        230        240 
GVIAETLTEL GNRYCMAQNY LPAIKDGDKR VLVVDGEPVP YCLARIPQGG ETRGNLAAGG 

       250        260        270        280        290        300 
RGEPRPLSES DWEIARRVGP TLKAKGLIFV GLDIIGDRLT EINVTSPTCV REIEAEYPIS 

       310 
ITGMLMDAIE ARLAK 

« Hide

References

[1]"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. expand/collapse author list , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.
[2]"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL513382 Genomic DNA. Translation: CAD02919.1.
AE014613 Genomic DNA. Translation: AAO70559.1.
RefSeqNP_457487.1. NC_003198.1.
NP_806699.1. NC_004631.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LP5model-A1-315[»]
ProteinModelPortalP58581.
SMRP58581. Positions 1-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220341.STY3248.

Proteomic databases

PRIDEP58581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO70559; AAO70559; t3007.
CAD02919; CAD02919; CAD02919.
GeneID1249530.
PATRIC18544572. VBISalEnt120419_3312.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayUPA00142; UER00210.

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...

Entry information

Entry nameGSHB_SALTI
AccessionPrimary (citable) accession number: P58581
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: April 16, 2014
This is version 88 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