Reviewed,
UniProtKB/Swiss-Prot B1XBX8 (MURI_ECODH)
Last modified
February 9, 2010.
Version 16.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glutamate racemase EC=5.1.1.3 | ||||
| Gene names |
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| Organism | Escherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 316385 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 285 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Provides the (R)-glutamate required for cell wall biosynthesis By similarity. HAMAP MF_00258 |
| Catalytic activity | L-glutamate = D-glutamate. HAMAP MF_00258 |
| Pathway | Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00258 |
| Sequence similarities | Belongs to the aspartate/glutamate racemases family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Molecular function | Isomerase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from electronic annotation. Source: HAMAP regulation of cell shapeInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | glutamate racemase activity Inferred 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 – 285 | 285 | Glutamate racemase HAMAP MF_00258 | PRO_1000114041 | |||
Sequences
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References
| [1] | "The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse." Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R. J. Bacteriol. 190:2597-2606(2008) [PubMed: 18245285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000948 Genomic DNA. Translation: ACB04978.1. |
| RefSeq | YP_001732756.1. |
3D structure databases | |
| SMR | B1XBX8. Positions 20-285. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 6058260. |
| GenomeReviews | Gene locus ECDH10B_4156 in contig CP000948_GR. |
| KEGG | ecd:ECDH10B_4156. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG645102. |
| OMA | VITQPCP. |
Family and domain databases | |
| HAMAP | MF_00258. Glu_racemase. [Tree] |
| InterPro | IPR015942. Asp/Glu/hydantoin_racemase. IPR001920. Asp/Glu_race. IPR018187. Asp/Glu_racemase_AS. IPR004391. Glu_race. [Graphical view] |
| Gene3D | G3DSA:3.40.50.1860. Asp/Glu_race. 1 hit. |
| Pfam | PF01177. Asp_Glu_race. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00067. glut_race. 1 hit. |
| PROSITE | PS00923. ASP_GLU_RACEMASE_1. 1 hit. PS00924. ASP_GLU_RACEMASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MURI_ECODH | ||||||||
| Accession | Primary (citable) accession number: B1XBX8 | ||||||||
| Entry history |
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| 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


