P22634 (MURI_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 112.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glutamate racemase EC=5.1.1.3 | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 285 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Provides the (R)-glutamate required for cell wall biosynthesis. 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. |
| Sequence caution | The sequence AAA23677.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAC43073.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA23637.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA23638.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Molecular function | Isomerase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW regulation of cell shapeInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | glutamate racemase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| tufA | P0CE47 | 1 | EBI-554903,EBI-301077 |
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_0000095470 | |||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 21 – 28 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 35 – 43 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 47 – 53 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 55 – 57 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 65 – 82 | 18 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 86 – 90 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 106 | 14 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 118 – 124 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 142 – 150 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 157 – 160 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 163 – 173 | 11 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 180 – 186 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 188 – 191 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 198 – 201 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 207 – 210 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 211 – 217 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 223 – 225 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 230 – 241 | 12 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 253 – 258 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 264 – 266 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 267 – 272 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 277 – 280 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Gene organization and primary structure of a ribosomal RNA operon from Escherichia coli." Brosius J., Dull T.J., Sleeter D.D., Noller H.F. J. Mol. Biol. 148:107-127(1981) [PubMed: 7028991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Identification of two new promoters probably involved in the transcription of a ribosomal RNA gene of Escherichia coli." Boros I., Csordas-Toth E., Kiss A., Kiss I., Toeroek I., Udvardy A., Udvardy K., Venetianer P. Biochim. Biophys. Acta 739:173-180(1983) [PubMed: 6297582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "The Escherichia coli mutant requiring D-glutamic acid is the result of mutations in two distinct genetic loci." Dougherty T.J., Thanassi J.A., Pucci M.J. J. Bacteriol. 175:111-116(1993) [PubMed: 8093236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B. |
| [4] | "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [5] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [6] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [7] | "Identification of the Escherichia coli murI gene, which is required for the biosynthesis of D-glutamic acid, a specific component of bacterial peptidoglycan." Doublet P., van Heijenoort J., Mengin-Lecreulx D. J. Bacteriol. 174:5772-5779(1992) [PubMed: 1355768] [Abstract] Cited for: CHARACTERIZATION. Strain: K12. |
| [8] | "The murI gene of Escherichia coli is an essential gene that encodes a glutamate racemase activity." Doublet P., van Heijenoort J., Bohin J.-P., Mengin-Lecreulx D. J. Bacteriol. 175:2970-2979(1993) [PubMed: 8098327] [Abstract] Cited for: CHARACTERIZATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | V00348 Genomic DNA. Translation: CAA23638.1. Different initiation. V00347 Genomic DNA. Translation: CAA23637.1. Different initiation. L14556 Genomic DNA. Translation: AAA23677.1. Different initiation. U00006 Genomic DNA. Translation: AAC43073.1. Different initiation. U00096 Genomic DNA. Translation: AAC76949.2. AP009048 Genomic DNA. Translation: BAE77344.1. | ||||||||||||
| PIR | I41187. | ||||||||||||
| RefSeq | NP_418402.2. NC_000913.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P22634. | ||||||||||||
| SMR | P22634. Positions 20-285. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-10283N. | ||||||||||||
| IntAct | P22634. 5 interactions. | ||||||||||||
| MINT | MINT-1222611. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBESCT00000000202; EBESCP00000000202; EBESCG00000000161. EBESCT00000014391; EBESCP00000013682; EBESCG00000013452. | ||||||||||||
| GeneID | 948467. | ||||||||||||
| GenomeReviews | Gene locus JW5550 in contig AP009048_GR. Gene locus b3967 in contig U00096_GR. | ||||||||||||
| KEGG | ecj:JW5550. eco:b3967. | ||||||||||||
| PATRIC | 32123455. VBIEscCol129921_4088. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB1189. | ||||||||||||
| EcoGene | EG11204. murI. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0796. | ||||||||||||
| GeneTree | EBGT00050000010644. | ||||||||||||
| HOGENOM | HBG645102. | ||||||||||||
| OMA | PQEDTIY. | ||||||||||||
| PhylomeDB | P22634. | ||||||||||||
| ProtClustDB | PRK00865. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:GLUTRACE-MONOMER. MetaCyc:GLUTRACE-MONOMER. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P22634. | ||||||||||||
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. | ||||||||||||
| KO | K01776. | ||||||||||||
| PANTHER | PTHR21198. PTHR21198. 1 hit. | ||||||||||||
| Pfam | PF01177. Asp_Glu_race. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF53681. Asp/Glu_race. 2 hits. | ||||||||||||
| 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_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P22634 Secondary accession number(s): P78133, Q2M8R2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with