Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q87LK1 (GSHB_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:VP2611
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length316 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 termComplete 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 – 316316Glutathione synthetase HAMAP-Rule MF_00162
PRO_0000197492

Regions

Domain124 – 310187ATP-grasp
Nucleotide binding150 – 20758ATP By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q87LK1 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: B234FB14C99FB675

FASTA31635,241
        10         20         30         40         50         60 
MIKLGIVMDP ISSINIKKDS SFAMMLEAQR RGYEIHYMEM NDLHLDQGKA IADTKVVELK 

        70         80         90        100        110        120 
EDPNGWYEFK SEQMIELSEL DAVLMRKDPP FDTEYIYATY ILERAEEQGA LIVNKPQSLR 

       130        140        150        160        170        180 
DCNEKLFTAW FPELTPTTIV TRKAEKIKAF REEHGDVILK PLDGMGGASI FRVKENDPNV 

       190        200        210        220        230        240 
SVIIETLTNH GQNYAMAQTF VPDISNGDKR ILVVDGEPMP YCLARIPAKG ETRGNLAAGG 

       250        260        270        280        290        300 
TGEARPLSET DMKIAQAVAP TLKEKGLIFV GLDVIGDKLT EINVTSPTCI REIEAAFDIS 

       310 
ITGKLMDAIE RRVKGE 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC60874.1.
RefSeqNP_798990.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87LK1.
SMRQ87LK1. Positions 1-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP2611.

Proteomic databases

PRIDEQ87LK1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC60874; BAC60874; BAC60874.
GeneID1190135.
KEGGvpa:VP2611.
PATRIC20143378. VBIVibPar50997_2507.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycVPAR223926:GHK4-2679-MONOMER.
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_VIBPA
AccessionPrimary (citable) accession number: Q87LK1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: February 19, 2014
This is version 71 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

PATHWAY comments

Index of metabolic and biosynthesis pathways