B7UQK7 (B7UQK7_ECO27) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 20.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: L-ribulose-5-phosphate 4-epimerase UlaF HAMAP MF_01952 EC=5.1.3.4 HAMAP MF_01952 Alternative name(s): L-ascorbate utilization protein F HAMAP MF_01952 Phosphoribulose isomerase HAMAP MF_01952 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O127:H6 (strain E2348/69 / EPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 574521 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 226 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization By similarity. HAMAP MF_01952 |
| Catalytic activity | L-ribulose 5-phosphate = D-xylulose 5-phosphate. HAMAP MF_01952 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_01952 |
| Pathway | Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 4/4. HAMAP MF_01952 |
| Induction | Induced by L-ascorbate. Repressed by UlaR By similarity. HAMAP MF_01952 |
| Sequence similarities | Belongs to the aldolase class II family. AraD/FucA subfamily. HAMAP MF_01952 |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding HAMAP MF_01952 Zinc HAMAP MF_01952 |
| Molecular function | Isomerase HAMAP MF_01952 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | L-ascorbic acid metabolic process Inferred from electronic annotation. Source: HAMAP |
| Molecular function | L-ribulose-phosphate 4-epimerase activity Inferred from electronic annotation. Source: HAMAP zinc ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Metal binding | 74 | 1 | Zinc By similarity HAMAP MF_01952 | ||||||
| Metal binding | 93 | 1 | Zinc By similarity HAMAP MF_01952 | ||||||
| Metal binding | 95 | 1 | Zinc By similarity HAMAP MF_01952 | ||||||
| Metal binding | 165 | 1 | Zinc By similarity HAMAP MF_01952 | ||||||
Sequences
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References
| [1] | "Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69." Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G. J. Bacteriol. 191:347-354(2009) [PubMed: 18952797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E2348/69 / EPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FM180568 Genomic DNA. Translation: CAS12069.1. |
| RefSeq | YP_002331973.1. NC_011601.1. |
3D structure databases | |
| ProteinModelPortal | B7UQK7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B7UQK7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000114020; EBESCP00000108491; EBESCG00000113898. |
| GeneID | 7062320. |
| GenomeReviews | Gene locus E2348_C_4521 in contig FM180568_GR. |
| KEGG | ecg:E2348C_4521. |
| PATRIC | 18348348. VBIEscCol90278_4626. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009319. |
| HOGENOM | HBG541069. |
| OMA | IDSYLMN. |
| ProtClustDB | PRK12348. |
Family and domain databases | |
| HAMAP | MF_01952. UlaF. [Tree] |
| InterPro | IPR001303. Aldolase_II/adducin_N. IPR023499. UlaF. [Graphical view] |
| Gene3D | G3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit. |
| KO | K03077. |
| Pfam | PF00596. Aldolase_II. 1 hit. [Graphical view] |
| SMART | SM01007. Aldolase_II. 1 hit. [Graphical view] |
| SUPFAM | SSF53639. Aldolase_II_N. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | B7UQK7_ECO27 | ||||||||
| Accession | Primary (citable) accession number: B7UQK7 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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