Reviewed,
UniProtKB/Swiss-Prot Q0T9J6 (ULAE_ECOL5)
Last modified
June 16, 2009.
Version 24.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: L-ribulose-5-phosphate 3-epimerase ulaE EC=5.1.3.22 Alternative name(s): L-xylulose-5-phosphate 3-epimerase L-ascorbate utilization protein E | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 362663 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 284 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization By similarity. |
| Catalytic activity | L-ribulose 5-phosphate = L-xylulose 5-phosphate. HAMAP MF_01951 |
| Pathway | Cofactor degradation; L-ascorbic acid degradation; D-xylulose 5-phosphate from L-ascorbic acid: step 3/4. HAMAP MF_01951 |
| Induction | Induced by L-ascorbate. Repressed by ulaR By similarity. |
| Sequence similarities | Belongs to the HUMPI family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Isomerase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | L-ascorbic acid metabolic process Inferred from electronic annotation. Source: HAMAP carbohydrate metabolic processInferred from electronic annotation. Source: InterPro |
| Molecular function | L-ribulose-5-phosphate 3-epimerase activity Inferred from electronic annotation. Source: HAMAP intramolecular oxidoreductase activity, interconverting aldoses and ketosesInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 284 | 284 | L-ribulose-5-phosphate 3-epimerase ulaE HAMAP MF_01951 | PRO_1000070633 | |||
Sequences
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References
| [1] | "Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000247 Genomic DNA. Translation: ABG72383.1. | |
| RefSeq | YP_672284.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4190034. |
| GenomeReviews | Gene locus ECP_4442 in contig CP000247_GR. |
| KEGG | ecp:ECP_4442. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q0T9J6. |
| OMA | Q0T9J6. VVKARDW. |
Enzyme and pathway databases | |
| BioCyc | ECOL362663:ECP_4442-MON. |
Family and domain databases | |
| HAMAP | MF_01951. [Tree] |
| InterPro | IPR004560. Hxl6Piso_put. IPR013022. Xyl_isomerase-like_TIM-brl. IPR012307. Xyl_isomerase-typ_TIM-brl. [Graphical view] |
| Gene3D | G3DSA:3.20.20.150. Xyl_isomerase-like_TIM-brl. 1 hit. |
| Pfam | PF01261. AP_endonuc_2. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00542. hxl6Piso_put. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ULAE_ECOL5 | ||||||||
| Accession | Primary (citable) accession number: Q0T9J6 | ||||||||
| 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


