P0A6X0 (GSH1_ECOL6) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 49.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glutamate--cysteine ligase EC=6.3.2.2 Alternative name(s): Gamma-ECS Short name=GCS Gamma-glutamylcysteine synthetase | ||||
| Gene names |
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| Organism | Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 199310 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 518 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine. HAMAP-Rule MF_00578 |
| Pathway | Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. HAMAP-Rule MF_00578 |
| Sequence similarities | Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glutathione biosynthesis |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | glutathione biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-cysteine ligase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 518 | 518 | Glutamate--cysteine ligase HAMAP-Rule MF_00578 | PRO_0000192525 | |||
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CFT073 / ATCC 700928 / UPEC. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014075 Genomic DNA. Translation: AAN81697.1. |
| RefSeq | NP_755127.1. NC_004431.1. |
3D structure databases | |
| ProteinModelPortal | P0A6X0. |
| SMR | P0A6X0. Positions 1-518. |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-1302356. |
| STRING | 199310.c3245. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAN81697; AAN81697; c3245. |
| GeneID | 1039015. |
| KEGG | ecc:c3245. |
| PATRIC | 18284319. VBIEscCol75197_3055. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000266224. |
| KO | K01919. |
| OMA | EYIEVRA. |
| ProtClustDB | PRK02107. |
Enzyme and pathway databases | |
| SABIO-RK | P0A6X0. |
| UniPathway | UPA00142; UER00209. |
Family and domain databases | |
| HAMAP | MF_00578. Glu_cys_ligase. |
| InterPro | IPR007370. Glu_cys_ligase. IPR006334. Glut_cys_ligase. [Graphical view] |
| Pfam | PF04262. Glu_cys_ligase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01434. glu_cys_ligase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GSH1_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: P0A6X0 Secondary accession number(s): P06980, P78228 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
