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Q7NQ65 (GSHB_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. 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:CV_4275
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium

Protein attributes

Sequence length314 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 – 314314Glutathione synthetase HAMAP-Rule MF_00162
PRO_0000197463

Regions

Domain122 – 309188ATP-grasp
Nucleotide binding149 – 20658ATP By similarity

Sites

Metal binding2801Magnesium or manganese By similarity
Metal binding2821Magnesium or manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NQ65 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: CAEB175EC4C135E2

FASTA31435,087
        10         20         30         40         50         60 
MRILFIADPL EHFKIYKDTT FAMMEEAHRR GHAISFAEAH QLSVEGGRLQ VDACDLAVTD 

        70         80         90        100        110        120 
ERPDWYKLGP KLRQPLTAFS AVVMRKDPPF DMEYLYASQL FTLAEAQGVK VFTSGQALRD 

       130        140        150        160        170        180 
FNEKLAILHF PELISPTLIS GEAHRLRAFV NQHQDVILKP LDSMGGDSIF RVKPDDPNLS 

       190        200        210        220        230        240 
VIIETITWRG KRTVMAQRYI PEIRDGDKRI LVIDGVPVDH CLARIPAAGE TRGNLAAGGR 

       250        260        270        280        290        300 
GEARPLSARD REIAETVGPE LKKRGILLAG LDVIGNYLTE VNVTSPTCFR EIMDQTGVNV 

       310 
AGLYIDALER RCQH 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ61935.1.
RefSeqNP_903945.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NQ65.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243365.CV_4275.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ61935; AAQ61935; CV_4275.
GeneID2548852.
KEGGcvi:CV_4275.
PATRIC21443409. VBIChrVio67196_4194.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0189.
HOGENOMHOG000265022.
KOK01920.
OMAWVRNYPE.
OrthoDBEOG6WMHWB.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-4396-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_CHRVO
AccessionPrimary (citable) accession number: Q7NQ65
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 74 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