Reviewed,
UniProtKB/Swiss-Prot Q1R808 (GSH1_ECOUT)
Last modified
June 16, 2009.
Version 19.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Glutamate--cysteine ligase EC=6.3.2.2 Alternative name(s): Gamma-glutamylcysteine synthetase Gamma-ECS Short name=GCS | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 364106 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 518 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine. HAMAP MF_00578 |
| Pathway | Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. HAMAP 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 MF_00578 | PRO_1000025171 | |||
Sequences
| ||||||||||||||||||
References
| [1] | "Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000243 Genomic DNA. Translation: ABE08506.1. | |
| RefSeq | YP_542037.1. |
3D structure databases | |
| SMR | Q1R808. Positions 1-515. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3990585. |
| GenomeReviews | Gene locus UTI89_C3050 in contig CP000243_GR. |
| KEGG | eci:UTI89_C3050. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q1R808. |
| OMA | Q1R808. EYIEVRA. |
Enzyme and pathway databases | |
| BioCyc | ECOL364106:UTI89_C3050-MON. |
Family and domain databases | |
| HAMAP | MF_00578. [Tree] |
| 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_ECOUT | ||||||||
| Accession | Primary (citable) accession number: Q1R808 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


